CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014287
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Laminin subunit alpha-5 
Protein Synonyms/Alias
 Laminin-10 subunit alpha; Laminin-11 subunit alpha; Laminin-15 subunit alpha 
Gene Name
 Lama5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
260PLLRDFTKATNIRLRacetylation[1]
Reference
 [1] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379] 
Functional Description
 Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Alpha-5 may be the major laminin alpha chain of adult epithelial and/or endothelial basal laminae. 
Sequence Annotation
 DOMAIN 46 304 Laminin N-terminal.
 DOMAIN 305 363 Laminin EGF-like 1.
 DOMAIN 364 433 Laminin EGF-like 2.
 DOMAIN 434 479 Laminin EGF-like 3.
 DOMAIN 500 546 Laminin EGF-like 4.
 DOMAIN 547 592 Laminin EGF-like 5.
 DOMAIN 593 637 Laminin EGF-like 6.
 DOMAIN 638 682 Laminin EGF-like 7.
 DOMAIN 683 728 Laminin EGF-like 8.
 DOMAIN 729 781 Laminin EGF-like 9.
 DOMAIN 782 833 Laminin EGF-like 10.
 DOMAIN 834 855 Laminin EGF-like 11; truncated.
 DOMAIN 1443 1488 Laminin EGF-like 12.
 DOMAIN 1489 1532 Laminin EGF-like 13.
 DOMAIN 1533 1581 Laminin EGF-like 14.
 DOMAIN 1582 1632 Laminin EGF-like 15.
 DOMAIN 1633 1642 Laminin EGF-like 16; first part.
 DOMAIN 1646 1831 Laminin IV type A.
 DOMAIN 1832 1864 Laminin EGF-like 16; second part.
 DOMAIN 1865 1914 Laminin EGF-like 17.
 DOMAIN 1915 1970 Laminin EGF-like 18.
 DOMAIN 1971 2024 Laminin EGF-like 19.
 DOMAIN 2025 2071 Laminin EGF-like 20.
 DOMAIN 2072 2118 Laminin EGF-like 21.
 DOMAIN 2119 2168 Laminin EGF-like 22.
 DOMAIN 2736 2933 Laminin G-like 1.
 DOMAIN 2947 3119 Laminin G-like 2.
 DOMAIN 3128 3296 Laminin G-like 3.
 DOMAIN 3337 3511 Laminin G-like 4.
 DOMAIN 3518 3689 Laminin G-like 5.
 REGION 856 1442 Domain IV 1 (domain IV B).
 REGION 2169 2735 Domain II and I.
 MOTIF 1723 1725 Cell attachment site (Potential).
 MOTIF 1839 1841 Cell attachment site (Potential).
 CARBOHYD 100 100 N-linked (GlcNAc...) (Potential).
 CARBOHYD 148 148 N-linked (GlcNAc...) (Potential).
 CARBOHYD 248 248 N-linked (GlcNAc...).
 CARBOHYD 383 383 N-linked (GlcNAc...) (Potential).
 CARBOHYD 457 457 N-linked (GlcNAc...) (Potential).
 CARBOHYD 485 485 N-linked (GlcNAc...) (Potential).
 CARBOHYD 905 905 N-linked (GlcNAc...) (Potential).
 CARBOHYD 926 926 N-linked (GlcNAc...).
 CARBOHYD 964 964 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1335 1335 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1534 1534 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2021 2021 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2198 2198 N-linked (GlcNAc...).
 CARBOHYD 2211 2211 N-linked (GlcNAc...).
 CARBOHYD 2365 2365 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2395 2395 N-linked (GlcNAc...).
 CARBOHYD 2425 2425 N-linked (GlcNAc...).
 CARBOHYD 2503 2503 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2570 2570 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2709 2709 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3111 3111 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3213 3213 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3261 3261 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3291 3291 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3623 3623 N-linked (GlcNAc...).
 CARBOHYD 3673 3673 N-linked (GlcNAc...) (Potential).
 DISULFID 305 314 By similarity.
 DISULFID 307 327 By similarity.
 DISULFID 329 338 By similarity.
 DISULFID 341 361 By similarity.
 DISULFID 364 373 By similarity.
 DISULFID 366 398 By similarity.
 DISULFID 401 410 By similarity.
 DISULFID 413 431 By similarity.
 DISULFID 434 445 By similarity.
 DISULFID 436 452 By similarity.
 DISULFID 454 463 By similarity.
 DISULFID 466 476 By similarity.
 DISULFID 500 512 By similarity.
 DISULFID 502 521 By similarity.
 DISULFID 523 532 By similarity.
 DISULFID 535 544 By similarity.
 DISULFID 547 559 By similarity.
 DISULFID 549 566 By similarity.
 DISULFID 568 577 By similarity.
 DISULFID 580 590 By similarity.
 DISULFID 593 605 By similarity.
 DISULFID 595 611 By similarity.
 DISULFID 613 622 By similarity.
 DISULFID 625 635 By similarity.
 DISULFID 638 650 By similarity.
 DISULFID 640 656 By similarity.
 DISULFID 658 667 By similarity.
 DISULFID 670 680 By similarity.
 DISULFID 683 695 By similarity.
 DISULFID 685 702 By similarity.
 DISULFID 704 713 By similarity.
 DISULFID 716 731 By similarity.
 DISULFID 752 761 By similarity.
 DISULFID 764 779 By similarity.
 DISULFID 782 796 By similarity.
 DISULFID 784 802 By similarity.
 DISULFID 804 813 By similarity.
 DISULFID 816 831 By similarity.
 DISULFID 834 846 By similarity.
 DISULFID 836 853 By similarity.
 DISULFID 855 864 By similarity.
 DISULFID 1443 1455 By similarity.
 DISULFID 1445 1462 By similarity.
 DISULFID 1464 1473 By similarity.
 DISULFID 1476 1486 By similarity.
 DISULFID 1489 1496 By similarity.
 DISULFID 1491 1503 By similarity.
 DISULFID 1505 1514 By similarity.
 DISULFID 1517 1530 By similarity.
 DISULFID 1533 1548 By similarity.
 DISULFID 1535 1555 By similarity.
 DISULFID 1557 1566 By similarity.
 DISULFID 1569 1579 By similarity.
 DISULFID 1582 1594 By similarity.
 DISULFID 1584 1601 By similarity.
 DISULFID 1603 1612 By similarity.
 DISULFID 1615 1630 By similarity.
 DISULFID 1865 1874 By similarity.
 DISULFID 1867 1881 By similarity.
 DISULFID 1884 1893 By similarity.
 DISULFID 1896 1912 By similarity.
 DISULFID 1915 1930 By similarity.
 DISULFID 1917 1939 By similarity.
 DISULFID 1941 1950 By similarity.
 DISULFID 1953 1968 By similarity.
 DISULFID 1971 1986 By similarity.
 DISULFID 1973 1993 By similarity.
 DISULFID 1996 2005 By similarity.
 DISULFID 2008 2022 By similarity.
 DISULFID 2025 2035 By similarity.
 DISULFID 2027 2042 By similarity.
 DISULFID 2044 2053 By similarity.
 DISULFID 2056 2069 By similarity.
 DISULFID 2072 2083 By similarity.
 DISULFID 2074 2090 By similarity.
 DISULFID 2092 2101 By similarity.
 DISULFID 2104 2116 By similarity.
 DISULFID 2119 2126 By similarity.
 DISULFID 2121 2133 By similarity.
 DISULFID 2135 2144 By similarity.
 DISULFID 2147 2166 By similarity.
 DISULFID 2169 2169 Interchain (Probable).
 DISULFID 2172 2172 Interchain (Probable).
 DISULFID 2903 2933 By similarity.
 DISULFID 3094 3119 By similarity.
 DISULFID 3265 3296 By similarity.
 DISULFID 3488 3511 By similarity.
 DISULFID 3661 3689 By similarity.  
Keyword
 3D-structure; Basement membrane; Cell adhesion; Coiled coil; Complete proteome; Direct protein sequencing; Disulfide bond; Extracellular matrix; Glycoprotein; Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3718 AA 
Protein Sequence
MAKRGGQLCA GSAPGALGPR SPAPRPLLLL LAGLALVGEA RTPGGDGFSL HPPYFNLAEG 60
ARITASATCG EEAPTRSVSR PTEDLYCKLV GGPVAGGDPN QTIQGQYCDI CTAANSNKAH 120
PVSNAIDGTE RWWQSPPLSR GLEYNEVNVT LDLGQVFHVA YVLIKFANSP RPDLWVLERS 180
TDFGHTYQPW QFFASSKRDC LERFGPRTLE RITQDDDVIC TTEYSRIVPL ENGEIVVSLV 240
NGRPGALNFS YSPLLRDFTK ATNIRLRFLR TNTLLGHLMG KALRDPTVTR RYYYSIKDIS 300
IGGRCVCHGH ADVCDAKDPL DPFRLQCACQ HNTCGGSCDR CCPGFNQQPW KPATTDSANE 360
CQSCNCHGHA YDCYYDPEVD RRNASQNQDN VYQGGGVCLD CQHHTTGINC ERCLPGFFRA 420
PDQPLDSPHV CRPCDCESDF TDGTCEDLTG RCYCRPNFTG ELCAACAEGY TDFPHCYPLP 480
SFPHNDTREQ VLPAGQIVNC DCNAAGTQGN ACRKDPRLGR CVCKPNFRGA HCELCAPGFH 540
GPSCHPCQCS SPGVANSLCD PESGQCMCRT GFEGDRCDHC ALGYFHFPLC QLCGCSPAGT 600
LPEGCDEAGR CQCRPGFDGP HCDRCLPGYH GYPDCHACAC DPRGALDQQC GVGGLCHCRP 660
GYTGATCQEC SPGFYGFPSC IPCHCSADGS LHTTCDPTTG QCRCRPRVTG LHCDMCVPGA 720
YNFPYCEAGS CHPAGLAPAN PALPETQAPC MCRAHVEGPS CDRCKPGYWG LSASNPEGCT 780
RCSCDPRGTL GGVTECQGNG QCFCKAHVCG KTCAACKDGF FGLDYADYFG CRSCRCDVGG 840
ALGQGCEPKT GACRCRPNTQ GPTCSEPAKD HYLPDLHHMR LELEEAATPE GHAVRFGFNP 900
LEFENFSWRG YAHMMAIQPR IVARLNVTSP DLFRLVFRYV NRGSTSVNGQ ISVREEGKLS 960
SCTNCTEQSQ PVAFPPSTEP AFVTVPQRGF GEPFVLNPGI WALLVEAEGV LLDYVVLLPS 1020
TYYEAALLQH RVTEACTYRP SALHSTENCL VYAHLPLDGF PSAAGTEALC RHDNSLPRPC 1080
PTEQLSPSHP PLATCFGSDV DIQLEMAVPQ PGQYVLVVEY VGEDSHQEMG VAVHTPQRAP 1140
QQGVLNLHPC PYSSLCRSPA RDTQHHLAIF YLDSEASIRL TAEQAHFFLH SVTLVPVEEF 1200
STEFVEPRVF CVSSHGTFNP SSAACLASRF PKPPQPIILK DCQVLPLPPD LPLTQSQELS 1260
PGAPPEGPQP RPPTAVDPNA EPTLLRHPQG TVVFTTQVPT LGRYAFLLHG YQPVHPSFPV 1320
EVLINGGRIW QGHANASFCP HGYGCRTLVL CEGQTMLDVT DNELTVTVRV PEGRWLWLDY 1380
VLIVPEDAYS SSYLQEEPLD KSYDFISHCA TQGYHISPSS SSPFCRNAAT SLSLFYNNGA 1440
LPCGCHEVGA VSPTCEPFGG QCPCRGHVIG RDCSRCATGY WGFPNCRPCD CGARLCDELT 1500
GQCICPPRTV PPDCLVCQPQ SFGCHPLVGC EECNCSGPGV QELTDPTCDM DSGQCRCRPN 1560
VAGRRCDTCA PGFYGYPSCR PCDCHEAGTM ASVCDPLTGQ CHCKENVQGS RCDQCRVGTF 1620
SLDAANPKGC TRCFCFGATE RCGNSNLARH EFVDMEGWVL LSSDRQVVPH EHRPEIELLH 1680
ADLRSVADTF SELYWQAPPS YLGDRVSSYG GTLHYELHSE TQRGDIFIPY ESRPDVVLQG 1740
NQMSIAFLEL AYPPPGQVHR GQLQLVEGNF RHLETHNPVS REELMMVLAG LEQLQIRALF 1800
SQTSSSVSLR RVVLEVASEA GRGPPASNVE LCMCPANYRG DSCQECAPGY YRDTKGLFLG 1860
RCVPCQCHGH SDRCLPGSGI CVGCQHNTEG DQCERCRPGF VSSDPSNPAS PCVSCPCPLA 1920
VPSNNFADGC VLRNGRTQCL CRPGYAGASC ERCAPGFFGN PLVLGSSCQP CDCSGNGDPN 1980
MIFSDCDPLT GACRGCLRHT TGPHCERCAP GFYGNALLPG NCTRCDCSPC GTETCDPQSG 2040
RCLCKAGVTG QRCDRCLEGY FGFEQCQGCR PCACGPAAKG SECHPQSGQC HCQPGTTGPQ 2100
CLECAPGYWG LPEKGCRRCQ CPRGHCDPHT GHCTCPPGLS GERCDTCSQQ HQVPVPGKPG 2160
GHGIHCEVCD HCVVLLLDDL ERAGALLPAI REQLQGINAS SAAWARLHRL NASIADLQSK 2220
LRSPPGPRYQ AAQQLQTLEQ QSISLQQDTE RLGSQATGVQ GQAGQLLDTT ESTLGRAQKL 2280
LESVRAVGRA LNELASRMGQ GSPGDALVPS GEQLRWALAE VERLLWDMRT RDLGAQGAVA 2340
EAELAEAQRL MARVQEQLTS FWEENQSLAT HIRDQLAQYE SGLMDLREAL NQAVNTTREA 2400
EELNSRNQER LKEALQWKQE LSQDNATLKA TLQAASLILG HVSELLQGID QAKEDLEHLA 2460
ASLDGAWTPL LKRMQAFSPA SSKVDLVEAA EAHAQKLNQL AINLSGIILG INQDRFIQRA 2520
VEASNAYSSI LQAVQAAEDA AGQALRQASR TWEMVVQRGL AAGARQLLAN SSALEETILG 2580
HQGRLGLAQG RLQAAGIQLH NVWARKNQLA AQIQEAQAML AMDTSETSEK IAHAKAVAAE 2640
ALSTATHVQS QLQGMQKNVE RWQSQLGGLQ GQDLSQVERD ASSSVSTLEK TLPQLLAKLS 2700
RLENRGVHNA SLALSANIGR VRKLIAQARS AASKVKVSMK FNGRSGVRLR TPRDLADLAA 2760
YTALKFHIQS PVPAPEPGKN TGDHFVLYMG SRQATGDYMG VSLRNQKVHW VYRLGKAGPT 2820
TLSIDENIGE QFAAVSIDRT LQFGHMSVTV EKQMVHEIKG DTVAPGSEGL LNLHPDDFVF 2880
YVGGYPSNFT PPEPLRFPGY LGCIEMETLN EEVVSLYNFE QTFMLDTAVD KPCARSKATG 2940
DPWLTDGSYL DGSGFARISF EKQFSNTKRF DQELRLVSYN GIIFFLKQES QFLCLAVQEG 3000
TLVLFYDFGS GLKKADPLQP PQALTAASKA IQVFLLAGNR KRVLVRVERA TVFSVDQDNM 3060
LEMADAYYLG GVPPEQLPLS LRQLFPSGGS VRGCIKGIKA LGKYVDLKRL NTTGISFGCT 3120
ADLLVGRTMT FHGHGFLPLA LPDVAPITEV VYSGFGFRGT QDNNLLYYRT SPDGPYQVSL 3180
REGHVTLRFM NQEVETQRVF ADGAPHYVAF YSNVTGVWLY VDDQLQLVKS HERTTPMLQL 3240
QPEEPSRLLL GGLPVSGTFH NFSGCISNVF VQRLRGPQRV FDLHQNMGSV NVSVGCTPAQ 3300
LIETSRATAQ KVSRRSRQPS QDLACTTPWL PGTIQDAYQF GGPLPSYLQF VGISPSHRNR 3360
LHLSMLVRPH AASQGLLLST APMSGRSPSL VLFLNHGHFV AQTEGPGPRL QVQSRQHSRA 3420
GQWHRVSVRW GMQQIQLVVD GSQTWSQKAL HHRVPRAERP QPYTLSVGGL PASSYSSKLP 3480
VSVGFSGCLK KLQLDKRPLR TPTQMVGVTP CVSGPLEDGL FFPGSEGVVT LELPKAKMPY 3540
VSLELEMRPL AAAGLIFHLG QALATPYMQL KVLTEQVLLQ ANDGAGEFST WVTYPKLCDG 3600
RWHRVAVIMG RDTLRLEVDT QSNHTTGRLP ESLAGSPALL HLGSLPKSST ARPELPAYRG 3660
CLRKLLINGA PVNVTASVQI QGAVGMRGCP SGTLALSKQG KALTQRQAKP SVSPLLWH 3718 
Gene Ontology
 GO:0005615; C:extracellular space; IEA:Compara.
 GO:0005606; C:laminin-1 complex; IEA:InterPro.
 GO:0043259; C:laminin-10 complex; IPI:MGI.
 GO:0005178; F:integrin binding; IDA:MGI.
 GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI.
 GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
 GO:0042384; P:cilium assembly; IMP:MGI.
 GO:0090002; P:establishment of protein localization to plasma membrane; IMP:MGI.
 GO:0001942; P:hair follicle development; IMP:MGI.
 GO:0007229; P:integrin-mediated signaling pathway; IEA:Compara.
 GO:0030324; P:lung development; IMP:MGI.
 GO:0001738; P:morphogenesis of a polarized epithelium; IMP:MGI.
 GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
 GO:0007517; P:muscle organ development; IMP:MGI.
 GO:0001755; P:neural crest cell migration; IMP:MGI.
 GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
 GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
 GO:0030334; P:regulation of cell migration; IEA:InterPro.
 GO:0042127; P:regulation of cell proliferation; IMP:MGI.
 GO:0045995; P:regulation of embryonic development; IEA:InterPro.
 GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Compara. 
Interpro
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR013032; EGF-like_CS.
 IPR002049; EGF_laminin.
 IPR018031; Laminin_B_subgr.
 IPR000034; Laminin_B_type_IV.
 IPR001791; Laminin_G.
 IPR009254; Laminin_I.
 IPR010307; Laminin_II.
 IPR008211; Laminin_N. 
Pfam
 PF00052; Laminin_B
 PF00053; Laminin_EGF
 PF02210; Laminin_G_2
 PF06008; Laminin_I
 PF06009; Laminin_II
 PF00055; Laminin_N 
SMART
 SM00180; EGF_Lam
 SM00281; LamB
 SM00282; LamG
 SM00136; LamNT 
PROSITE
 PS00022; EGF_1
 PS01186; EGF_2
 PS01248; EGF_LAM_1
 PS50027; EGF_LAM_2
 PS50025; LAM_G_DOMAIN
 PS51115; LAMININ_IVA
 PS51117; LAMININ_NTER 
PRINTS