CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023274
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 
Protein Synonyms/Alias
 620 kDa actin-binding protein; ABP620; Actin cross-linking family protein 7; Macrophin-1; Trabeculin-alpha 
Gene Name
 MACF1 
Gene Synonyms/Alias
 ABP620; ACF7; KIAA0465; KIAA1251 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
90TFTKWVNKHLMKVRKacetylation[1]
2642SELVKKCKIDIESGQubiquitination[2]
2667IKDGVSDKVLTLSQAubiquitination[3]
3279LGSFLPEKLFKGVSQubiquitination[2, 3]
3458KDAKNLQKSLSSVSDubiquitination[3]
3506LRAWVGNKNLILNSKubiquitination[3]
4306DRVQNLRKDFTELQKubiquitination[3]
6210LWENLGEKIAHRQHKacetylation[1]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] 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
 Isoform 2 is a F-actin-binding protein which may play a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2- dependent stabilization of microtubules at the cell cortex. Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane. Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics. May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4. Plays a key role in wound healing and epidermal cell migration. Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate MT dynamics and polarize hair follicle stem cells (By similarity). 
Sequence Annotation
 DOMAIN 1 295 Actin-binding.
 DOMAIN 78 181 CH 1.
 REPEAT 148 171 LRR 1.
 DOMAIN 194 295 CH 2.
 REPEAT 240 264 LRR 2.
 REPEAT 377 399 LRR 3.
 REPEAT 441 464 LRR 4.
 DOMAIN 871 923 SH3.
 REPEAT 1050 1073 LRR 5.
 REPEAT 1128 1154 LRR 6.
 REPEAT 1187 1210 LRR 7.
 REPEAT 1257 1282 LRR 8.
 REPEAT 1577 1621 Plectin 1.
 REPEAT 1654 1696 Plectin 2.
 REPEAT 1769 1809 Plectin 3.
 REPEAT 1811 1848 Plectin 4.
 REPEAT 1855 1886 Plectin 5.
 REPEAT 2290 2332 Plectin 6.
 REPEAT 2367 2410 Plectin 7.
 REPEAT 2411 2437 Plectin 8.
 REPEAT 2501 2543 Plectin 9.
 REPEAT 2581 2612 Plectin 10.
 REPEAT 2686 2730 Plectin 11.
 REPEAT 3239 3262 LRR 9.
 REPEAT 3264 3283 LRR 10.
 REPEAT 3646 3669 LRR 11.
 REPEAT 3696 3720 LRR 12.
 REPEAT 3883 3957 Spectrin 1.
 REPEAT 3936 3958 LRR 13.
 REPEAT 4000 4108 Spectrin 2.
 REPEAT 4125 4150 LRR 14.
 REPEAT 4261 4287 LRR 15.
 REPEAT 4466 4574 Spectrin 3.
 REPEAT 4511 4534 LRR 16.
 REPEAT 4601 4624 LRR 17.
 REPEAT 4769 4792 LRR 18.
 REPEAT 4800 4904 Spectrin 4.
 REPEAT 4909 5012 Spectrin 5.
 REPEAT 5051 5076 LRR 19.
 REPEAT 5172 5194 LRR 20.
 REPEAT 5236 5341 Spectrin 6.
 REPEAT 5281 5304 LRR 21.
 REPEAT 5348 5450 Spectrin 7.
 REPEAT 5455 5557 Spectrin 8.
 REPEAT 5695 5719 LRR 22.
 REPEAT 5783 5885 Spectrin 9.
 REPEAT 5804 5828 LRR 23.
 REPEAT 6005 6110 Spectrin 10.
 REPEAT 6115 6219 Spectrin 11.
 REPEAT 6225 6328 Spectrin 12.
 REPEAT 6333 6439 Spectrin 13.
 REPEAT 6443 6547 Spectrin 14.
 REPEAT 6496 6519 LRR 24.
 REPEAT 6552 6658 Spectrin 15.
 REPEAT 6665 6766 Spectrin 16.
 REPEAT 6771 6874 Spectrin 17.
 DOMAIN 7041 7076 EF-hand 1.
 DOMAIN 7077 7112 EF-hand 2.
 DOMAIN 7117 7189 GAR.
 REGION 7117 7388 C-terminal tail (By similarity).
 REGION 7313 7328 4 X 4 AA tandem repeats of [GS]-S-R-[AR].
 MOD_RES 280 280 Phosphoserine.
 MOD_RES 1376 1376 Phosphoserine.
 MOD_RES 3927 3927 Phosphoserine.
 MOD_RES 4495 4495 Phosphoserine.
 MOD_RES 4496 4496 Phosphoserine.
 MOD_RES 4521 4521 Phosphoserine.
 MOD_RES 4962 4962 Phosphoserine.
 MOD_RES 6032 6032 Phosphoserine (By similarity).
 MOD_RES 6210 6210 N6-acetyllysine.
 MOD_RES 6967 6967 Phosphoserine.
 MOD_RES 7254 7254 Phosphothreonine.
 MOD_RES 7292 7292 Phosphoserine.
 MOD_RES 7330 7330 Phosphoserine.
 MOD_RES 7333 7333 Phosphoserine (By similarity).  
Keyword
 Acetylation; Actin-binding; Alternative splicing; Calcium; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Golgi apparatus; Leucine-rich repeat; Membrane; Metal-binding; Microtubule; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain; Wnt signaling pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 7388 AA 
Protein Sequence
MSSSDEETLS ERSCRSERSC RSERSYRSER SGSLSPCPPG DTLPWNLPLH EQKKRKSQDS 60
VLDPAERAVV RVADERDRVQ KKTFTKWVNK HLMKVRKHIN DLYEDLRDGH NLISLLEVLS 120
GIKLPREKGR MRFHRLQNVQ IALDFLKQRQ VKLVNIRNDD ITDGNPKLTL GLIWTIILHF 180
QISDIYISGE SGDMSAKEKL LLWTQKVTAG YTGIKCTNFS SCWSDGKMFN ALIHRYRPDL 240
VDMERVQIQS NRENLEQAFE VAERLGVTRL LDAEDVDVPS PDEKSVITYV SSIYDAFPKV 300
PEGGEGISAT EVDSRWQEYQ SRVDSLIPWI KQHTILMSDK TFPQNPVELK ALYNQYIHFK 360
ETEILAKERE KGRIEELYKL LEVWIEFGRI KLPQGYHPND VEEEWGKLII EMLEREKSLR 420
PAVERLELLL QIANKIQNGA LNCEEKLTLA KNTLQADAAH LESGQPVQCE SDVIMYIQEC 480
EGLIRQLQVD LQILRDENYY QLEELAFRVM RLQDELVTLR LECTNLYRKG HFTSLELVPP 540
STLTTTHLKA EPLTKATHSS STSWFRKPMT RAELVAISSS EDEGNLRFVY ELLSWVEEMQ 600
MKLERAEWGN DLPSVELQLE TQQHIHTSVE ELGSSVKEAR LYEGKMSQNF HTSYAETLGK 660
LETQYCKLKE TSSFRMRHLQ SLHKFVSRAT AELIWLNEKE EEELAYDWSD NNSNISAKRN 720
YFSELTMELE EKQDVFRSLQ DTAELLSLEN HPAKQTVEAY SAAVQSQLQW MKQLCLCVEQ 780
HVKENTAYFQ FFSDARELES FLRNLQDSIK RKYSCDHNTS LSRLEDLLQD SMDEKEQLIQ 840
SKSSVASLVG RSKTIVQLKP RSPDHVLKNT ISVKAVCDYR QIEITICKND ECVLEDNSQR 900
TKWKVISPTG NEAMVPSVCF LIPPPNKDAI EMASRVEQSY QKVMALWHQL HVNTKSLISW 960
NYLRKDLDLV QTWNLEKLRS SAPGECHQIM KNLQAHYEDF LQDSRDSVLF SVADRLRLEE 1020
EVEACKARFQ HLMKSMENED KEETVAKMYI SELKNIRLRL EEYEQRVVKR IQSLASSRTD 1080
RDAWQDNALR IAEQEHTQED LQQLRSDLDA VSMKCDSFLH QSPSSSSVPT LRSELNLLVE 1140
KMDHVYGLST VYLNKLKTVD VIVRSIQDAE LLVKGYEIKL SQEEVVLADL SALEAHWSTL 1200
RHWLSDVKDK NSVFSVLDEE IAKAKVVAEQ MSRLTPERNL DLERYQEKGS QLQERWHRVI 1260
AQLEIRQSEL ESIQEVLGDY RACHGTLIKW IEETTAQQEM MKPGQAEDSR VLSEQLSQQT 1320
ALFAEIERNQ TKLDQCQKFS QQYSTIVKDY ELQLMTYKAF VESQQKSPGK RRRMLSSSDA 1380
ITQEFMDLRT RYTALVTLTT QHVKYISDAL RRLEEEEKVV EEEKQEHVEK VKELLGWVST 1440
LARNTQGKAT SSETKESTDI EKAILEQQVL SEELTTKKEQ VSEAIKTSQI FLAKHGHKLS 1500
EKEKKQISEQ LNALNKAYHD LCDGSANQLQ QLQSQLAHQT EQKECRAVAG VIDLGTVEIF 1560
PIFKAMQKGL LDQDTGLVLL ESQVIMSGLI APETGENLSL EEGIARNLIN PQMYQQLREL 1620
QDALALISRL TESRGPLSVV EAIEKRIISE TVGLKILEAH LATGGFSLSP SENCINLEEA 1680
FHQGLISAWL HSVLESYLRT SKNLIDPNTA EKIGLLDLMQ RCIVHQESGF KLLPVKQLAG 1740
GMVSLKSGRK VSIFRAVQEG LIDRQVTVRL LEAQLFAGGI VDPRTGHRLT VEEAVRHNLI 1800
DQDMACAILI RQLQTGGIID TVTGQRLTID EAVSNDLVAA KIALVILESL WSFMGLLWPE 1860
SGEILPITDA LEQGIVSTEL AHKILSNRQH IKALFLPATT EILSWKKAIE SGILDRDLAN 1920
NLKSICIPDV MPHMQLADSA EQNINPGAAV LPCSKSHPKA TASQSENLLF QLMTHSYINV 1980
QNGQRLLLLD KELMETLTSR DEYQTSPPKV VEIGHQRQKT PEGLQESANV KISGTFSSGW 2040
TVRLPEFQFS SQNKEYPDRE DCTTEKGKKT TVETEDSSVE NPEQDLFVEQ KERNPNIDAL 2100
KVINKVKLEV QRQLIGTQRE DQTAVSVREN ASRGHLLTIP PAEAEGVPLV VDKDVFSVET 2160
PKKEHQPLRN TSFTCQNEQA HTLETEYIHD ETGGSHIKPQ SKKLQVQVKK TLGIKLELKS 2220
ETDGNVHPLD KKEMLKKTFL AKDDHKESQE AQNIAGGSMM MSEKTDEEDS GREIFLSCSH 2280
PLELLEEATL NVLSAQLLDG GIFHEQTGQK LLLNEAISRG IVPSHTAVKL MEKLNMFQGF 2340
FDSQTCESLT TEEVINEGLM DEKLLHNVLM ADKAISGVLD PRTQTLCSVK DAVTVGLLDK 2400
ETATRILERQ VVTGGIIDLK RGKKVSVTLA STLGLVDVAD QPELINLEKA SKGRDAEKTV 2460
RERLISLQME TTGLIDPDSK APLTVVQSID RGLLEREEAV RLLTKQVVDG GIIHHISGMR 2520
LSVDNAFRHG LIGEDLAEKL KRVENLNIHQ IFNPETKENI SLPKAIKLDL ITSDLKREIQ 2580
EVQAFTGNFV DLISGQRLTL AEAKKEGLLT NEAVLSPGMM HGIVDPENCR IVPYSELVKK 2640
CKIDIESGQR YLEVIPFSDI KDGVSDKVLT LSQAIQLGKV DFASTLKVLE AQANTGGIID 2700
TATGKRLTLA SALEEKLVDE NMVRIIASHQ VLNGGIVDIF SDQRVTLVEA IEKRLISPEL 2760
ANMIQIDSSE FSDHRAQIEK QEGIEVCALQ NEFLGKDMLI ACNQTAEMSC NKVEESERLF 2820
QVENQSAQEK VKVRVSDGEQ AKKSREISLK EFGCKDQRKP RMSSDAKEFI SIINPHNLKG 2880
KSLGQVSLTH PYSECDFKLK EVARNNMGND TNEEQEKAVT KIEIISHMKQ STSCLDSEEI 2940
RENQGEVILE VQETYCETSG KLPSEQVLQQ PMNARVKSKR EKREVIVEES IRTCKPAFLS 3000
EEKLYQETAI RDEHDSHIKS QPREMTSSEK GKEADTEMGF SITFKIEESS SQVVPQGISV 3060
KHLDALTLFS SKQANEGKVN NLSLCLTLKP EENLSREIAC GAQSEPFPCM TPRPEGLHYQ 3120
ESDGKAQVTG PSQISKTDKS FQGTTRQETN YQDSWVTSKT KETKHQISSS NECKEKSYQE 3180
VSFDPARGLK LEEITVSRPD SKEVRYLEFS DRKDLHHQGS KSDDKLCGTL KSEIATQELT 3240
GEKFLEMANP NVAGLEAGSI EDIVTQRGSR VLGSFLPEKL FKGVSQKENT GQQNAIISPT 3300
VLETSEEKTV SLTVCSAVKT EKTPQEKLRE SPGSEQTPFM TAPEGKGNGG VNPEPFRATQ 3360
NVFTRQLCLE HDEKLVSYLS LLRNIEMRTK QIQPLELNLA ELQDLLCQAK VLERELKDLT 3420
TLVSQELECV NQIIISQPQE VPAQLLKALE KDAKNLQKSL SSVSDTWNSR LLHFQNAVEI 3480
EKTKVLNQHT QLEGRLQDLR AWVGNKNLIL NSKGSNSEID VDSLNLCLQQ YEDLKQPMAE 3540
RKAQLDALAF DIQFFISEHA QDLSPQQNRQ MLRLLNELQR SFQDILEQTA AQVDALQGHL 3600
QQMEQEALVK TLQKQQNTCH QQLEDLCSWV GQAERALAGH QGRTTQQDLS ALQKNQSDLK 3660
DLQDDIQNRA TSFATVVKDI EGFMEENQTK LSPRELTALR EKLHQAKEQY EALQEETRVA 3720
QKELEEAVTS ALQQETEKSK AAKELAENKK KIDALLDWVT SVGSSGGQLL TNLPGMEQLS 3780
GASLEKGALD TTDGYMGVNQ APEKLDKQCE MMKARHQELL SQQQNFILAT QSAQAFLDQH 3840
GHNLTPEEQQ MLQQKLGELK EQYSTSLAQS EAELKQVQTL QDELQKFLQD HKEFESWLER 3900
SEKELENMHK GGSSPETLPS LLKRQGSFSE DVISHKGDLR FVTISGQKVL DMENSFKEGK 3960
EPSEIGNLVK DKLKDATERY TALHSKCTRL GSHLNMLLGQ YHQFQNSADS LQAWMQACEA 4020
NVEKLLSDTV ASDPGVLQEQ LATTKQLQEE LAEHQVPVEK LQKVARDIME IEGEPAPDHR 4080
HVQETTDSIL SHFQSLSYSL AERSSLLQKA IAQSQSVQES LESLLQSIGE VEQNLEGKQV 4140
SSLSSGVIQE ALATNMKLKQ DIARQKSSLE ATREMVTRFM ETADSTTAAV LQGKLAEVSQ 4200
RFEQLCLQQQ EKESSLKKLL PQAEMFEHLS GKLQQFMENK SRMLASGNQP DQDITHFFQQ 4260
IQELNLEMED QQENLDTLEH LVTELSSCGF ALDLCQHQDR VQNLRKDFTE LQKTVKEREK 4320
DASSCQEQLD EFRKLVRTFQ KWLKETEGSI PPTETSMSAK ELEKQIEHLK SLLDDWASKG 4380
TLVEEINCKG TSLENLIMEI TAPDSQGKTG SILPSVGSSV GSVNGYHTCK DLTEIQCDMS 4440
DVNLKYEKLG GVLHERQESL QAILNRMEEV HKEANSVLQW LESKEEVLKS MDAMSSPTKT 4500
ETVKAQAESN KAFLAELEQN SPKIQKVKEA LAGLLVTYPN SQEAENWKKI QEELNSRWER 4560
ATEVTVARQR QLEESASHLA CFQAAESQLR PWLMEKELMM GVLGPLSIDP NMLNAQKQQV 4620
QFMLKEFEAR RQQHEQLNEA AQGILTGPGD VSLSTSQVQK ELQSINQKWV ELTDKLNSRS 4680
SQIDQAIVKS TQYQELLQDL SEKVRAVGQR LSVQSAISTQ PEAVKQQLEE TSEIRSDLEQ 4740
LDHEVKEAQT LCDELSVLIG EQYLKDELKK RLETVALPLQ GLEDLAADRI NRLQAALAST 4800
QQFQQMFDEL RTWLDDKQSQ QAKNCPISAK LERLQSQLQE NEEFQKSLNQ HSGSYEVIVA 4860
EGESLLLSVP PGEEKRTLQN QLVELKNHWE ELSKKTADRQ SRLKDCMQKA QKYQWHVEDL 4920
VPWIEDCKAK MSELRVTLDP VQLESSLLRS KAMLNEVEKR RSLLEILNSA ADILINSSEA 4980
DEDGIRDEKA GINQNMDAVT EELQAKTGSL EEMTQRLREF QESFKNIEKK VEGAKHQLEI 5040
FDALGSQACS NKNLEKLRAQ QEVLQALEPQ VDYLRNFTQG LVEDAPDGSD ASQLLHQAEV 5100
AQQEFLEVKQ RVNSGCVMME NKLEGIGQFH CRVREMFSQL ADLDDELDGM GAIGRDTDSL 5160
QSQIEDVRLF LNKIHVLKLD IEASEAECRH MLEEEGTLDL LGLKRELEAL NKQCGKLTER 5220
GKARQEQLEL TLGRVEDFYR KLKGLNDATT AAEEAEALQW VVGTEVEIIN QQLADFKMFQ 5280
KEQVDPLQMK LQQVNGLGQG LIQSAGKDCD VQGLEHDMEE INARWNTLNK KVAQRIAQLQ 5340
EALLHCGKFQ DALEPLLSWL ADTEELIANQ KPPSAEYKVV KAQIQEQKLL QRLLDDRKAT 5400
VDMLQAEGGR IAQSAELADR EKITGQLESL ESRWTELLSK AAARQKQLED ILVLAKQFHE 5460
TAEPISDFLS VTEKKLANSE PVGTQTAKIQ QQIIRHKALN EEIVNRKKNV DQAIKNGQAL 5520
LKQTTGEEVL LIQEKLDGIK TRYADITVTS SKALRTLEQA RQLATKFQST YEELTGWLRE 5580
VEEELATSGG QSPTGEQIPQ FQQRQKELKK EVMEHRLVLD TVNEVSRALL ELVPWRAREG 5640
LDKLVSDANE QYKLVSDTIG QRVDEIDAAI QRSQQYEQAA DAELAWVAET KRKLMALGPI 5700
RLEQDQTTAQ LQVQKAFSID IIRHKDSMDE LFSHRSEIFG TCGEEQKTVL QEKTESLIQQ 5760
YEAISLLNSE RYARLERAQV LVNQFWETYE ELSPWIEETR ALIAQLPSPA IDHEQLRQQQ 5820
EEMRQLRESI AEHKPHIDKL LKIGPQLKEL NPEEGEMVEE KYQKAENMYA QIKEEVRQRA 5880
LALDEAVSQS TQITEFHDKI EPMLETLENL SSRLRMPPLI PAEVDKIREC ISDNKSATVE 5940
LEKLQPSFEA LKRRGEELIG RSQGADKDLA AKEIQDKLDQ MVFFWEDIKA RAEEREIKFL 6000
DVLELAEKFW YDMAALLTTI KDTQDIVHDL ESPGIDPSII KQQVEAAETI KEETDGLHEE 6060
LEFIRILGAD LIFACGETEK PEVRKSIDEM NNAWENLNKT WKERLEKLED AMQAAVQYQD 6120
TLQAMFDWLD NTVIKLCTMP PVGTDLNTVK DQLNEMKEFK VEVYQQQIEM EKLNHQGELM 6180
LKKATDETDR DIIREPLTEL KHLWENLGEK IAHRQHKLEG ALLALGQFQH ALEELMSWLT 6240
HTEELLDAQR PISGDPKVIE VELAKHHVLK NDVLAHQATV ETVNKAGNEL LESSAGDDAS 6300
SLRSRLEAMN QCWESVLQKT EEREQQLQST LQQAQGFHSE IEDFLLELTR MESQLSASKP 6360
TGGLPETARE QLDTHMELYS QLKAKEETYN QLLDKGRLML LSRDDSGSGS KTEQSVALLE 6420
QKWHVVSSKM EERKSKLEEA LNLATEFQNS LQEFINWLTL AEQSLNIASP PSLILNTVLS 6480
QIEEHKVFAN EVNAHRDQII ELDQTGNQLK FLSQKQDVVL IKNLLVSVQS RWEKVVQRSI 6540
ERGRSLDDAR KRAKQFHEAW KKLIDWLEDA ESHLDSELEI SNDPDKIKLQ LSKHKEFQKT 6600
LGGKQPVYDT TIRTGRALKE KTLLPEDSQK LDNFLGEVRD KWDTVCGKSV ERQHKLEEAL 6660
LFSGQFMDAL QALVDWLYKV EPQLAEDQPV HGDLDLVMNL MDAHKVFQKE LGKRTGTVQV 6720
LKRSGRELIE NSRDDTTWVK GQLQELSTRW DTVCKLSVSK QSRLEQALKQ AEVFRDTVHM 6780
LLEWLSEAEQ TLRFRGALPD DTEALQSLID THKEFMKKVE EKRVDVNSAV AMGEVILAVC 6840
HPDCITTIKH WITIIRARFE EVLTWAKQHQ QRLETALSEL VANAELLEEL LAWIQWAETT 6900
LIQRDQEPIP QNIDRVKALI AEHQTFMEEM TRKQPDVDRV TKTYKRKNIE PTHAPFIEKS 6960
RSGGRKSLSQ PTPPPMPILS QSEAKNPRIN QLSARWQQVW LLALERQRKL NDALDRLEEL 7020
KEFANFDFDV WRKKYMRWMN HKKSRVMDFF RRIDKDQDGK ITRQEFIDGI LASKFPTTKL 7080
EMTAVADIFD RDGDGYIDYY EFVAALHPNK DAYRPTTDAD KIEDEVTRQV AQCKCAKRFQ 7140
VEQIGENKYR FGDSQQLRLV RILRSTVMVR VGGGWMALDE FLVKNDPCRA RGRTNIELRE 7200
KFILPEGASQ GMTPFRSRGR RSKPSSRAAS PTRSSSSASQ SNHSCTSMPS SPATPASGTK 7260
VIPSSGSKLK RPTPTFHSSR TSLAGDTSNS SSPASTGAKT NRADPKKSAS RPGSRAGSRA 7320
GSRASSRRGS DASDFDLLET QSACSDTSES SAAGGQGNSR RGLNKPSKIP TMSKKTTTAS 7380
PRTPGPKR 7388 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:Compara.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0032587; C:ruffle membrane; IDA:UniProtKB.
 GO:0051015; F:actin filament binding; NAS:UniProtKB.
 GO:0016887; F:ATPase activity; ISS:UniProtKB.
 GO:0005509; F:calcium ion binding; NAS:UniProtKB.
 GO:0008017; F:microtubule binding; NAS:UniProtKB.
 GO:0007050; P:cell cycle arrest; IEA:InterPro.
 GO:0006928; P:cellular component movement; IEA:Compara.
 GO:0007163; P:establishment or maintenance of cell polarity; IEA:Compara.
 GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB.
 GO:0001707; P:mesoderm formation; IEA:Compara.
 GO:0030177; P:positive regulation of Wnt receptor signaling pathway; ISS:UniProtKB.
 GO:0006620; P:posttranslational protein targeting to membrane; IEA:Compara.
 GO:0010632; P:regulation of epithelial cell migration; ISS:UniProtKB.
 GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
 GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB.
 GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
 GO:0042060; P:wound healing; ISS:UniProtKB. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR001715; CH-domain.
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR003108; GAS2_dom.
 IPR001101; Plectin_repeat.
 IPR018159; Spectrin/alpha-actinin.
 IPR002017; Spectrin_repeat. 
Pfam
 PF00307; CH
 PF13499; EF_hand_5
 PF02187; GAS2
 PF00681; Plectin
 PF00435; Spectrin 
SMART
 SM00033; CH
 SM00054; EFh
 SM00243; GAS2
 SM00250; PLEC
 SM00150; SPEC 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS51460; GAR
 PS50002; SH3 
PRINTS