CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012323
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protocadherin Fat 1 
Protein Synonyms/Alias
 Cadherin family member 7; Cadherin-related tumor suppressor homolog; Protein fat homolog; Protocadherin Fat 1, nuclear form 
Gene Name
 FAT1 
Gene Synonyms/Alias
 CDHF7; FAT 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
101CFLRIRTKGGNTAILubiquitination[1]
189GEFYYSFKDRTDMFAubiquitination[1]
216RLDYLETKLYEMEILubiquitination[1]
341LTLQAKDKGTPPQFSubiquitination[1, 2]
351PPQFSSVKVIHVTSPubiquitination[1]
366QFKAGPVKFEKDVYRubiquitination[2]
369AGPVKFEKDVYRAEIubiquitination[2]
390NTPVVMVKAIPAYSHubiquitination[1, 2]
403SHLRYVFKSTPGKAKubiquitination[1]
427ISILEPVKRQQAAHFubiquitination[1, 2]
452ASTKVLVKVLGANSNubiquitination[1]
637LMDGLGAKVSFHSLRubiquitination[1]
686VAKMLAEKLLQANKLubiquitination[1, 2, 3]
692EKLLQANKLHNQGEVubiquitination[1, 3]
727LPTGIQVKENQPVGSubiquitination[1, 3]
894LQHEHSLKIEARDQAubiquitination[1, 2, 3]
935IPPNYRVKVREDLPEubiquitination[3]
978EGNFDVDKLSGAVRIubiquitination[1, 2, 3]
993VQQLDFEKKQVYNLTubiquitination[1, 2, 3]
994QQLDFEKKQVYNLTVubiquitination[2]
1083GSGVGVFKIGEETGVubiquitination[1, 3]
1173PDSSSNDKLMYKITSubiquitination[1, 3]
1192GFFSIHPKTGLITTTubiquitination[1, 2, 3]
1234TIARVIVKILDENDNubiquitination[2]
1242ILDENDNKPQFLQKFubiquitination[3]
1248NKPQFLQKFYKIRLPubiquitination[1, 2, 3]
1305GKFFIEPKTGVVSSKubiquitination[1, 3]
1326EYDILSIKAVDNGRPubiquitination[1, 3]
1335VDNGRPQKSSTTRLHubiquitination[3]
1415TGTIIVAKPLDAEQKubiquitination[3]
1460RPQFSTSKYEVVIPEubiquitination[1, 3]
1486SAVDQDEKNKLIYTLubiquitination[1, 3]
1503SRDPLSLKKFRLDPAubiquitination[1, 3]
1542RDQDVPVKRNFARIVubiquitination[1, 2, 3]
1568WFTASSYKGRVYESAubiquitination[1, 2, 3]
1593ALDKDKGKNAEVLYSubiquitination[1]
1620DPVLGSIKTAKELDRubiquitination[1]
1638AEYDLMVKATDKGSPubiquitination[1, 3]
1642LMVKATDKGSPPMSEubiquitination[1, 3]
1666IADNASPKFTSKEYSubiquitination[1, 2, 3]
1894SLLLPTYKGVKVITVubiquitination[1]
1932EKFSMDYKTGALTVQubiquitination[1, 2, 3]
1966FAGLTSVKINVKESKubiquitination[3]
1970TSVKINVKESKESHLubiquitination[3]
1978ESKESHLKFTQDVYSubiquitination[1, 3]
2091LPYYAVVKVDTEVGHubiquitination[1]
2138PLGEISLKKQFELDTubiquitination[1]
2139LGEISLKKQFELDTLubiquitination[1, 2, 3]
2424ADSSDIDKLQYSILSubiquitination[3]
2553GQIFTLEKLDRETPAubiquitination[1, 2, 3]
2600APQFRATKYEVNIGSubiquitination[1, 2, 3]
2611NIGSSAAKGTSVVKVubiquitination[1, 2, 3]
2643EADSESVKENLEINKubiquitination[3]
2650KENLEINKLSGVITTubiquitination[3]
2683VDNGSPSKESVVLVYubiquitination[1, 2, 3]
2739TVLYSLVKGNTPESNubiquitination[1, 2, 3]
2764SGRLKLEKSLDHETTubiquitination[1, 2, 4]
2886KRDNYQIKVVASDHGubiquitination[2, 3]
2981NEWKVYVKKPLDREKubiquitination[2]
3025DNSPVCEKTLYSDTIubiquitination[2, 5]
3069LLGSGAEKFKLNPDTubiquitination[1, 3]
3071GSGAEKFKLNPDTGEacetylation[6]
3071GSGAEKFKLNPDTGEubiquitination[1, 2]
3396RGEVKVTKLLDRETIubiquitination[2]
3504LLTSSAIKRKEKDHYubiquitination[1, 3, 4]
3522VKVADNGKPQLSSLTubiquitination[1, 3]
3736RILNVFQKLCAGLDCubiquitination[2]
3746AGLDCPWKFCDEKVSubiquitination[2]
3751PWKFCDEKVSVDESVubiquitination[2]
3783RAAVCLCKEGRCPPVubiquitination[2]
3813VSDPWEEKHTCVCPSubiquitination[2]
3992QELPLNSKPRSYAHIubiquitination[2, 7]
4094CQLSPYCKDEPCKNGubiquitination[2]
4219HQAEPKDKHLGPATAubiquitination[1, 2, 3, 4, 7, 8]
4236QRPYFDSKLNKNIYSubiquitination[1]
4239YFDSKLNKNIYSDIPubiquitination[1, 2]
4297ESVHGHRKAVAVCSVubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [8] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 
Functional Description
 Plays an essential role for cellular polarization, directed cell migration and modulating cell-cell contact (By similarity). 
Sequence Annotation
 DOMAIN 35 149 Cadherin 1.
 DOMAIN 150 257 Cadherin 2.
 DOMAIN 368 463 Cadherin 3.
 DOMAIN 464 569 Cadherin 4.
 DOMAIN 570 673 Cadherin 5.
 DOMAIN 718 822 Cadherin 6.
 DOMAIN 823 927 Cadherin 7.
 DOMAIN 928 1034 Cadherin 8.
 DOMAIN 1035 1139 Cadherin 9.
 DOMAIN 1140 1245 Cadherin 10.
 DOMAIN 1246 1357 Cadherin 11.
 DOMAIN 1359 1456 Cadherin 12.
 DOMAIN 1457 1562 Cadherin 13.
 DOMAIN 1563 1667 Cadherin 14.
 DOMAIN 1668 1765 Cadherin 15.
 DOMAIN 1766 1879 Cadherin 16.
 DOMAIN 1880 1979 Cadherin 17.
 DOMAIN 1980 2081 Cadherin 18.
 DOMAIN 2082 2182 Cadherin 19.
 DOMAIN 2183 2283 Cadherin 20.
 DOMAIN 2284 2390 Cadherin 21.
 DOMAIN 2391 2492 Cadherin 22.
 DOMAIN 2493 2596 Cadherin 23.
 DOMAIN 2597 2703 Cadherin 24.
 DOMAIN 2704 2809 Cadherin 25.
 DOMAIN 2810 2918 Cadherin 26.
 DOMAIN 2919 3023 Cadherin 27.
 DOMAIN 3024 3125 Cadherin 28.
 DOMAIN 3126 3230 Cadherin 29.
 DOMAIN 3231 3335 Cadherin 30.
 DOMAIN 3336 3440 Cadherin 31.
 DOMAIN 3441 3545 Cadherin 32.
 DOMAIN 3546 3647 Cadherin 33.
 DOMAIN 3790 3827 EGF-like 1.
 DOMAIN 3829 4009 Laminin G-like.
 DOMAIN 4013 4050 EGF-like 2.
 DOMAIN 4052 4088 EGF-like 3.
 DOMAIN 4089 4125 EGF-like 4.
 DOMAIN 4127 4163 EGF-like 5; calcium-binding (Potential).
 MOTIF 4204 4214 Nuclear localization signal (Potential).
 MOTIF 4378 4382 PTB-like motif (By similarity).
 CARBOHYD 40 40 N-linked (GlcNAc...) (Potential).
 CARBOHYD 333 333 N-linked (GlcNAc...) (Potential).
 CARBOHYD 660 660 N-linked (GlcNAc...) (Potential).
 CARBOHYD 740 740 N-linked (GlcNAc...) (Potential).
 CARBOHYD 791 791 N-linked (GlcNAc...) (Potential).
 CARBOHYD 998 998 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1426 1426 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1551 1551 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1748 1748 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1864 1864 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1902 1902 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1940 1940 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1991 1991 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2325 2325 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2464 2464 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3324 3324 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3415 3415 N-linked (GlcNAc...).
 CARBOHYD 3422 3422 N-linked (GlcNAc...).
 CARBOHYD 3444 3444 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3613 3613 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3640 3640 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3716 3716 N-linked (GlcNAc...).
 CARBOHYD 4152 4152 N-linked (GlcNAc...) (Potential).
 DISULFID 3794 3805 By similarity.
 DISULFID 3799 3816 By similarity.
 DISULFID 3818 3826 By similarity.
 DISULFID 3976 4009 By similarity.
 DISULFID 4017 4028 By similarity.
 DISULFID 4022 4038 By similarity.
 DISULFID 4040 4049 By similarity.
 DISULFID 4056 4067 By similarity.
 DISULFID 4061 4076 By similarity.
 DISULFID 4078 4087 By similarity.
 DISULFID 4093 4104 By similarity.
 DISULFID 4098 4113 By similarity.
 DISULFID 4115 4124 By similarity.
 DISULFID 4131 4142 By similarity.
 DISULFID 4136 4151 By similarity.
 DISULFID 4153 4162 By similarity.  
Keyword
 Calcium; Cell adhesion; Cell membrane; Complete proteome; Cytoplasm; Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Nucleus; Polymorphism; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 4588 AA 
Protein Sequence
MGRHLALLLL LLLLFQHFGD SDGSQRLEQT PLQFTHLEYN VTVQENSAAK TYVGHPVKMG 60
VYITHPAWEV RYKIVSGDSE NLFKAEEYIL GDFCFLRIRT KGGNTAILNR EVKDHYTLIV 120
KALEKNTNVE ARTKVRVQVL DTNDLRPLFS PTSYSVSLPE NTAIRTSIAR VSATDADIGT 180
NGEFYYSFKD RTDMFAIHPT SGVIVLTGRL DYLETKLYEM EILAADRGMK LYGSSGISSM 240
AKLTVHIEQA NECAPVITAV TLSPSELDRD PAYAIVTVDD CDQGANGDIA SLSIVAGDLL 300
QQFRTVRSFP GSKEYKVKAI GGIDWDSHPF GYNLTLQAKD KGTPPQFSSV KVIHVTSPQF 360
KAGPVKFEKD VYRAEISEFA PPNTPVVMVK AIPAYSHLRY VFKSTPGKAK FSLNYNTGLI 420
SILEPVKRQQ AAHFELEVTT SDRKASTKVL VKVLGANSNP PEFTQTAYKA AFDENVPIGT 480
TVMSLSAVDP DEGENGYVTY SIANLNHVPF AIDHFTGAVS TSENLDYELM PRVYTLRIRA 540
SDWGLPYRRE VEVLATITLN NLNDNTPLFE KINCEGTIPR DLGVGEQITT VSAIDADELQ 600
LVQYQIEAGN ELDFFSLNPN SGVLSLKRSL MDGLGAKVSF HSLRITATDG ENFATPLYIN 660
ITVAASHKLV NLQCEETGVA KMLAEKLLQA NKLHNQGEVE DIFFDSHSVN AHIPQFRSTL 720
PTGIQVKENQ PVGSSVIFMN STDLDTGFNG KLVYAVSGGN EDSCFMIDME TGMLKILSPL 780
DRETTDKYTL NITVYDLGIP QKAAWRLLHV VVVDANDNPP EFLQESYFVE VSEDKEVHSE 840
IIQVEATDKD LGPNGHVTYS IVTDTDTFSI DSVTGVVNIA RPLDRELQHE HSLKIEARDQ 900
AREEPQLFST VVVKVSLEDV NDNPPTFIPP NYRVKVREDL PEGTVIMWLE AHDPDLGQSG 960
QVRYSLLDHG EGNFDVDKLS GAVRIVQQLD FEKKQVYNLT VRAKDKGKPV SLSSTCYVEV 1020
EVVDVNENLH PPVFSSFVEK GTVKEDAPVG SLVMTVSAHD EDARRDGEIR YSIRDGSGVG 1080
VFKIGEETGV IETSDRLDRE STSHYWLTVF ATDQGVVPLS SFIEIYIEVE DVNDNAPQTS 1140
EPVYYPEIME NSPKDVSVVQ IEAFDPDSSS NDKLMYKITS GNPQGFFSIH PKTGLITTTS 1200
RKLDREQQDE HILEVTVTDN GSPPKSTIAR VIVKILDEND NKPQFLQKFY KIRLPEREKP 1260
DRERNARREP LYHVIATDKD EGPNAEISYS IEDGNEHGKF FIEPKTGVVS SKRFSAAGEY 1320
DILSIKAVDN GRPQKSSTTR LHIEWISKPK PSLEPISFEE SFFTFTVMES DPVAHMIGVI 1380
SVEPPGIPLW FDITGGNYDS HFDVDKGTGT IIVAKPLDAE QKSNYNLTVE ATDGTTTILT 1440
QVFIKVIDTN DHRPQFSTSK YEVVIPEDTA PETEILQISA VDQDEKNKLI YTLQSSRDPL 1500
SLKKFRLDPA TGSLYTSEKL DHEAVHQHTL TVMVRDQDVP VKRNFARIVV NVSDTNDHAP 1560
WFTASSYKGR VYESAAVGSV VLQVTALDKD KGKNAEVLYS IESGNIGNSF MIDPVLGSIK 1620
TAKELDRSNQ AEYDLMVKAT DKGSPPMSEI TSVRIFVTIA DNASPKFTSK EYSVELSETV 1680
SIGSFVGMVT AHSQSSVVYE IKDGNTGDAF DINPHSGTII TQKALDFETL PIYTLIIQGT 1740
NMAGLSTNTT VLVHLQDEND NAPVFMQAEY TGLISESASI NSVVLTDRNV PLVIRAADAD 1800
KDSNALLVYH IVEPSVHTYF AIDSSTGAIH TVLSLDYEET SIFHFTVQVH DMGTPRLFAE 1860
YAANVTVHVI DINDCPPVFA KPLYEASLLL PTYKGVKVIT VNATDADSSA FSQLIYSITE 1920
GNIGEKFSMD YKTGALTVQN TTQLRSRYEL TVRASDGRFA GLTSVKINVK ESKESHLKFT 1980
QDVYSAVVKE NSTEAETLAV ITAIGNPINE PLFYHILNPD RRFKISRTSG VLSTTGTPFD 2040
REQQEAFDVV VEVTEEHKPS AVAHVVVKVI VEDQNDNAPV FVNLPYYAVV KVDTEVGHVI 2100
RYVTAVDRDS GRNGEVHYYL KEHHEHFQIG PLGEISLKKQ FELDTLNKEY LVTVVAKDGG 2160
NPAFSAEVIV PITVMNKAMP VFEKPFYSAE IAESIQVHSP VVHVQANSPE GLKVFYSITD 2220
GDPFSQFTIN FNTGVINVIA PLDFEAHPAY KLSIRATDSL TGAHAEVFVD IIVDDINDNP 2280
PVFAQQSYAV TLSEASVIGT SVVQVRATDS DSEPNRGISY QMFGNHSKSH DHFHVDSSTG 2340
LISLLRTLDY EQSRQHTIFV RAVDGGMPTL SSDVIVTVDV TDLNDNPPLF EQQIYEARIS 2400
EHAPHGHFVT CVKAYDADSS DIDKLQYSIL SGNDHKHFVI DSATGIITLS NLHRHALKPF 2460
YSLNLSVSDG VFRSSTQVHV TVIGGNLHSP AFLQNEYEVE LAENAPLHTL VMEVKTTDGD 2520
SGIYGHVTYH IVNDFAKDRF YINERGQIFT LEKLDRETPA EKVISVRLMA KDAGGKVAFC 2580
TVNVILTDDN DNAPQFRATK YEVNIGSSAA KGTSVVKVLA SDADEGSNAD ITYAIEADSE 2640
SVKENLEINK LSGVITTKES LIGLENEFFT FFVRAVDNGS PSKESVVLVY VKILPPEMQL 2700
PKFSEPFYTF TVSEDVPIGT EIDLIRAEHS GTVLYSLVKG NTPESNRDES FVIDRQSGRL 2760
KLEKSLDHET TKWYQFSILA RCTQDDHEMV ASVDVSIQVK DANDNSPVFE SSPYEAFIVE 2820
NLPGGSRVIQ IRASDADSGT NGQVMYSLDQ SQSVEVIESF AINMETGWIT TLKELDHEKR 2880
DNYQIKVVAS DHGEKIQLSS TAIVDVTVTD VNDSPPRFTA EIYKGTVSED DPQGGVIAIL 2940
STTDADSEEI NRQVTYFITG GDPLGQFAVE TIQNEWKVYV KKPLDREKRD NYLLTITATD 3000
GTFSSKAIVE VKVLDANDNS PVCEKTLYSD TIPEDVLPGK LIMQISATDA DIRSNAEITY 3060
TLLGSGAEKF KLNPDTGELK TSTPLDREEQ AVYHLLVRAT DGGGRFCQAS IVLTLEDVND 3120
NAPEFSADPY AITVFENTEP GTLLTRVQAT DADAGLNRKI LYSLIDSADG QFSINELSGI 3180
IQLEKPLDRE LQAVYTLSLK AVDQGLPRRL TATGTVIVSV LDINDNPPVF EYREYGATVS 3240
EDILVGTEVL QVYAASRDIE ANAEITYSII SGNEHGKFSI DSKTGAVFII ENLDYESSHE 3300
YYLTVEATDG GTPSLSDVAT VNVNVTDIND NTPVFSQDTY TTVISEDAVL EQSVITVMAD 3360
DADGPSNSHI HYSIIDGNQG SSFTIDPVRG EVKVTKLLDR ETISGYTLTV QASDNGSPPR 3420
VNTTTVNIDV SDVNDNAPVF SRGNYSVIIQ ENKPVGFSVL QLVVTDEDSS HNGPPFFFTI 3480
VTGNDEKAFE VNPQGVLLTS SAIKRKEKDH YLLQVKVADN GKPQLSSLTY IDIRVIEESI 3540
YPPAILPLEI FITSSGEEYS GGVIGKIHAT DQDVYDTLTY SLDPQMDNLF SVSSTGGKLI 3600
AHKKLDIGQY LLNVSVTDGK FTTVADITVH IRQVTQEMLN HTIAIRFANL TPEEFVGDYW 3660
RNFQRALRNI LGVRRNDIQI VSLQSSEPHP HLDVLLFVEK PGSAQISTKQ LLHKINSSVT 3720
DIEEIIGVRI LNVFQKLCAG LDCPWKFCDE KVSVDESVMS THSTARLSFV TPRHHRAAVC 3780
LCKEGRCPPV HHGCEDDPCP EGSECVSDPW EEKHTCVCPS GRFGQCPGSS SMTLTGNSYV 3840
KYRLTENENK LEMKLTMRLR TYSTHAVVMY ARGTDYSILE IHHGRLQYKF DCGSGPGIVS 3900
VQSIQVNDGQ WHAVALEVNG NYARLVLDQV HTASGTAPGT LKTLNLDNYV FFGGHIRQQG 3960
TRHGRSPQVG NGFRGCMDSI YLNGQELPLN SKPRSYAHIE ESVDVSPGCF LTATEDCASN 4020
PCQNGGVCNP SPAGGYYCKC SALYIGTHCE ISVNPCSSKP CLYGGTCVVD NGGFVCQCRG 4080
LYTGQRCQLS PYCKDEPCKN GGTCFDSLDG AVCQCDSGFR GERCQSDIDE CSGNPCLHGA 4140
LCENTHGSYH CNCSHEYRGR HCEDAAPNQY VSTPWNIGLA EGIGIVVFVA GIFLLVVVFV 4200
LCRKMISRKK KHQAEPKDKH LGPATAFLQR PYFDSKLNKN IYSDIPPQVP VRPISYTPSI 4260
PSDSRNNLDR NSFEGSAIPE HPEFSTFNPE SVHGHRKAVA VCSVAPNLPP PPPSNSPSDS 4320
DSIQKPSWDF DYDTKVVDLD PCLSKKPLEE KPSQPYSARE SLSEVQSLSS FQSESCDDNG 4380
YHWDTSDWMP SVPLPDIQEF PNYEVIDEQT PLYSADPNAI DTDYYPGGYD IESDFPPPPE 4440
DFPAADELPP LPPEFSNQFE SIHPPRDMPA AGSLGSSSRN RQRFNLNQYL PNFYPLDMSE 4500
PQTKGTGENS TCREPHAPYP PGYQRHFEAP AVESMPMSVY ASTASCSDVS ACCEVESEVM 4560
MSDYESGDDG HFEEVTIPPL DSQQHTEV 4588 
Gene Ontology
 GO:0005911; C:cell-cell junction; IDA:UniProtKB.
 GO:0030175; C:filopodium; IEA:Compara.
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0030027; C:lamellipodium; IEA:Compara.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0007015; P:actin filament organization; ISS:UniProtKB.
 GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
 GO:0016477; P:cell migration; ISS:UniProtKB.
 GO:0016337; P:cell-cell adhesion; ISS:UniProtKB.
 GO:0007267; P:cell-cell signaling; TAS:ProtInc.
 GO:0007163; P:establishment or maintenance of cell polarity; ISS:UniProtKB.
 GO:0007156; P:homophilic cell adhesion; IEA:InterPro. 
Interpro
 IPR002126; Cadherin.
 IPR015919; Cadherin-like.
 IPR020894; Cadherin_CS.
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR000742; EG-like_dom.
 IPR001881; EGF-like_Ca-bd.
 IPR013032; EGF-like_CS.
 IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
 IPR018097; EGF_Ca-bd_CS.
 IPR001791; Laminin_G. 
Pfam
 PF00028; Cadherin
 PF00008; EGF
 PF07645; EGF_CA
 PF02210; Laminin_G_2 
SMART
 SM00112; CA
 SM00181; EGF
 SM00179; EGF_CA
 SM00282; LamG 
PROSITE
 PS00010; ASX_HYDROXYL
 PS00232; CADHERIN_1
 PS50268; CADHERIN_2
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS01187; EGF_CA
 PS50025; LAM_G_DOMAIN 
PRINTS
 PR00205; CADHERIN.