CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024724
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Microtubule-actin cross-linking factor 1 
Protein Synonyms/Alias
 Actin cross-linking family 7 
Gene Name
 Macf1 
Gene Synonyms/Alias
 Acf7; Aclp7; Macf 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
147QIALDFLKQRQVKLVubiquitination[1]
669ETQYCKLKETSSFRMacetylation[2]
684RHLQSLHKFVSKATAacetylation[2]
835LQDSMDEKEQLIQSKacetylation[2]
4252LWENLGEKIAHRQHKacetylation[2]
Reference
 [1] 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]
 [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 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 1579 1602 LRR 9.
 REPEAT 1629 1653 LRR 10.
 REPEAT 1816 1891 Spectrin 1.
 REPEAT 1869 1891 LRR 11.
 REPEAT 1933 2041 Spectrin 2.
 REPEAT 2058 2083 LRR 12.
 REPEAT 2194 2220 LRR 13.
 REPEAT 2399 2507 Spectrin 3.
 REPEAT 2444 2467 LRR 14.
 REPEAT 2534 2557 LRR 15.
 REPEAT 2702 2725 LRR 16.
 REPEAT 2733 2837 Spectrin 4.
 REPEAT 2842 2945 Spectrin 5.
 REPEAT 2984 3009 LRR 17.
 REPEAT 3105 3127 LRR 18.
 REPEAT 3169 3274 Spectrin 6.
 REPEAT 3214 3237 LRR 19.
 REPEAT 3281 3383 Spectrin 7.
 REPEAT 3388 3491 Spectrin 8.
 REPEAT 3714 3818 Spectrin 9.
 REPEAT 3737 3761 LRR 20.
 REPEAT 3825 3927 Spectrin 10.
 REPEAT 3846 3870 LRR 21.
 REPEAT 4047 4152 Spectrin 11.
 REPEAT 4157 4261 Spectrin 12.
 REPEAT 4267 4370 Spectrin 13.
 REPEAT 4375 4481 Spectrin 14.
 REPEAT 4486 4589 Spectrin 15.
 REPEAT 4538 4561 LRR 22.
 REPEAT 4594 4700 Spectrin 16.
 REPEAT 4707 4808 Spectrin 17.
 REPEAT 4812 4916 Spectrin 18.
 DOMAIN 5083 5118 EF-hand 1.
 DOMAIN 5119 5154 EF-hand 2.
 DOMAIN 5159 5231 GAR.
 REGION 5159 5430 C-terminal tail (By similarity).
 REGION 5355 5370 4 X 4 AA tandem repeats of [GS]-S-R-[AR].
 MOD_RES 280 280 Phosphoserine (By similarity).
 MOD_RES 1376 1376 Phosphoserine (By similarity).
 MOD_RES 1860 1860 Phosphoserine (By similarity).
 MOD_RES 2429 2429 Phosphoserine (By similarity).
 MOD_RES 2454 2454 Phosphoserine (By similarity).
 MOD_RES 2895 2895 Phosphoserine (By similarity).
 MOD_RES 4074 4074 Phosphoserine (By similarity).
 MOD_RES 4252 4252 N6-acetyllysine (By similarity).
 MOD_RES 5009 5009 Phosphoserine (By similarity).
 MOD_RES 5296 5296 Phosphothreonine (By similarity).
 MOD_RES 5334 5334 Phosphoserine (By similarity).
 MOD_RES 5372 5372 Phosphoserine (By similarity).
 MOD_RES 5375 5375 Phosphoserine (By similarity).  
Keyword
 Acetylation; Actin-binding; Calcium; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Leucine-rich repeat; Membrane; Metal-binding; Microtubule; Phosphoprotein; Reference proteome; Repeat; SH3 domain; Wnt signaling pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 5430 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 RQHTILMSDK SFPQNPVELK ALYNQYIHFK 360
ETEILAKERE KGRIKELYKL LEVWIEFGRI KLPQGYHPNH VEEEWGKLIV EMLEREKSLR 420
PAVERLELLL QIANKIQNGA LNCEEKLTLA KNTLQADAAH LESGQPVQCE SDVIMYIQEC 480
EGLIRQLQVD LQILRDEKYY QLEELAFRVM RLQDELVTLR LECTNLYRKG HFTSLELVPP 540
STLTTTHLKA EPLNKTTHSS STSWFRKPMT RTELVAISSS EDEGSLRFVY ELLSWVEEMQ 600
MKLERAEWGN DLPSVELQWE TQQHIHTSVE ELGSSVKEAR LYEGKMSQNF HTSYVETLGK 660
LETQYCKLKE TSSFRMRHLQ SLHKFVSKAT AELIWLNGKE EEELACDWSD SNPNISAKKA 720
YFSELTMELE GKQDVFRSLQ DTAELLSLEN HPAKQTVEAY SAAVQSQLQW MKQLCLCVEQ 780
HIKENAAYFQ FFSDARDLES FLRNLQDSIK RKYTCDHNTS LSRLEDLLQD SMDEKEQLIQ 840
SKSSVASLVG RSKTIVQLKP RNPDHVLKST LSVKAICDYR QIEITICKND ECVLEDNSQR 900
TKWKVISPTG NEAMVPSVCL LIPPPNTEAI DVASRVEQSY QKVMALWHQL HINTKSLISW 960
NYLRKDIDAV QTWNLEKLRS SAPGECHQVM KNLQAHYEDF LQDSHDSALF SVADRLRIEE 1020
EVEACKTHFQ QLMESMENED KEETLAKVYI SELKNIRLRL EECEQRLLKQ IQSSASSKTD 1080
RDARQDVALR IAEQEHVQED LKHLRSDLDA VSVKCTTFLQ QSPSGSSATT LRSELNLMVE 1140
KMDHVYGLSI VCLNKLKTID VIVRSIQDAE LLVKGYEIKL SQEEAVPADL SALESHRTTL 1200
QHWLSDVKDK NSVFSVLDEE ISKAKAVAEQ LHHRAAEPNL DLERYQEKGS QLQERWHRVI 1260
AQLETRQSEV ESIQEVLRDY RACHGTLIKW IEETTAQQEM MKPGQAEDSR VLSEQLSQQT 1320
ELFAEIERNQ TKLDQCQKLS QQYSTTVKDY ELQLMTYKAF VESQQKSPGK RRRMISSSDA 1380
ITQEFMDLRT RYTALVTLTT QHVKYISDAL RRLEEEEKVV EEEKQEHVEK VKDLLGWVST 1440
LARNTQGTTT SSRTSASTDI EKAILEQQVL AEELTTKKEQ VSEAIKTSQI FLAKHGHKLS 1500
EREKEQISEQ LCALNKTYHD LCDGSANQLQ QLQSELAQQT EQKTLQKQQD TCHKKLEDLR 1560
SWVRQAERAL ERHRGRASQQ ELSALQQNQS DLKDLQGDIQ NHSTSFATAV KDIEGFLEEN 1620
QNKLSPQELT ALREKLYQAK EQYEGLQDRT REAQKELEEA VTSALQQETE KSKAATELAE 1680
NRRKIDALLD WVTSVGSSDR QPQTSLPGTE QFSGACLEKQ TLDATDGCVD VNQVPEKLDR 1740
QYELMKARHQ ELLSQQQNFI VATQSAQSFL DQHSHNLTPE ERQMLQEKLG ELKEQYAASL 1800
AQSEAKLRQT QTLRDELQKF LQDHREFENW LERSENELDG MHTGGSSPEA LNSLLKRQGS 1860
FSEDVISHKG DLRFVTISGQ KVLETENNFE EGQEPSPTRN LVNEKLKDAT ERYTTLHSKC 1920
TRLGSHLNML LGQYQQFQSS ADSLQAWMLT CEASVEKLLS DTVASDPGIL QQQLATTKQL 1980
QEELAEHQVP VEKLQKAAHD LMDIEGEPSL DCTPIRETTE SIFSRFQSLS CSLAERSALL 2040
QKAIAQSQSV QESMESLLQS MKEVEQNLEG EQVAALSSGL IQEALANNMK LKQDIARQKS 2100
SLEATREMVT RFMETADGNS AAVLQDRLAE LSQRFHRLQL QQQEKESGLK KLLPQAETFE 2160
QLSSKLQQFV EHKNRLLASG NQPDQDIAHF SQHIQELTLE MEDQKENLGT LEHLVTALGS 2220
CGFALDLSQH QEKIQNLKKD FTELQKTVQE REKDASNCQE QLDEFRKLIR TFQKWLKETE 2280
GNVPPAETFV SAKELEKQIE HLKGLLDDWA GKGVLVEEIN TKGTALESLI MDITAPDSQA 2340
KTGSVLPSVG SSVGSVNGYH TCKDLTEIQC DMSDVNSKYD KLGDALRERQ ESLQTVLSRM 2400
EEVQKEASSV LQWLESKEEV LKGMDASLSP TKTETVKAQA ESNKAFLAEL EQNSPKIQKV 2460
KEALAGLLEA YPNSQEAENW RKMQEDLNSR WEKATEVTVA RQKQLEESAS HLACFQAAES 2520
QLRPWLMEKE LMMGVLGPLS IDPNMLNAQK QQVQFMLKEF EARRQQHEQL TEAAQGILTG 2580
PGDVSPSASQ VHKDLQSISQ KWVELTDKLN SRSTQIDQAI VKSTQYQDLL QDLSEKVKAV 2640
GQRLSGQSAI STQPDAVKQQ LEETSEIRSD LGQLDDEMKE AQTLCQELSL LIGEQYLKDE 2700
LKKRLETVAL PLQGLEDLAA DRMNRLQAAL ASTQQFQQMF DELRTWLDEK QSQQAKNCPI 2760
SAKLERLQSQ LQENEEFQKN LNQHSGSYEV IVAEGESLLL SVPPGEEKKT LQNQLVELKS 2820
HWEDLNKKTV DRQSRLKDCM QKAQKYQWHV EDLVPWIKDC KSKMSELQVT LDPVQLESSL 2880
LRSKAMLNEA EKRRSLLEIL NSAADILINS SEIDEDEIRD EKAGLNQNMD AITEELQAKT 2940
GSLEEMTQRL KEFQESFKNI EKKVEGAKHQ LEIFDALGSQ ACSNKNLEKL KAQREVLQAL 3000
DPQVDYLRDF TRGLVEDAPD GSDASPLVHQ AELAQQEFLE VKQRVNSSCL TMENKLEGIG 3060
QFHCRVREMF SQLADLDDEL DGMGAIGRDT DSLQSQIEDI RLFLNKIQAL RLDIEDSEAE 3120
CRKMLEEEGT LDLLGLKREL EALNKQCGKL TERGKARQEQ LELTLGRVED FYSKLKALND 3180
AATAAEEGEA LQWIVGTEVD VINQQLADFK MFQKEQVDPL QVKLQQVNGL GQGLIQSAGK 3240
TCDVQGLEHD MEEVNTRWNT LNKKVAQRIA QLQEALLHCG KFQDALEPLL SWLTDTEELI 3300
ANQKPPSAEY KVVKAQIQEQ KLLQRLLDDR KATVDMLQAE GGRIAQAAEL ADREKITGQL 3360
ESLECRWTEL LSKAAARQKQ LEDILVLAKQ FHETAEPISD FLSVTEKKLA NSEPVGTQTA 3420
KIHQQIIRHK ALEEEIENHA ADVQQAVKIG QSLSSLICPA EQGIMSEKLD SLQARYSEIQ 3480
DRCCRKASLL EQALFNARLF GEDEVEVLNW LAEVEDKLSA VFVKDYRQDV LQKQHADHLA 3540
LNEEIINRKK NVDQAIKNGQ ALLKQTTGEE VLLIQEKLDG IKTRYADITV TSSKALRTLE 3600
QARQLATKFH STYEELTGWL REVEEELAAS GGQSPTGEQI PQFQQRQKEL KKEVMEHRLV 3660
LDTVNEVSHA LLELVPWRAR EGLDKLVSDA NEQYKLVSDT VGQRVDEIDA AIQRSQQYEQ 3720
AADAELAWVA ETKRKLMALG PIRLEQDQTT AQLQVQKAFS IDIIRHKDSM DELFSHRGEI 3780
FSTCGEEQKA VLQEKTECLI QQYEAVSLLN SERYARLERA QVLVNQFWET YEELSPWAEE 3840
TLALIAQLPP PAVDHEQLRQ QQEEMRQLRE SIAEHKPHID KILKIGPQLK ELNPEEGKMV 3900
EEKYQKAENM YAQIKDEVRQ RALALDEAVS QSAQIAEFHD KIEPMLETLE NLSSRLRMPP 3960
LIPAEVDKIR ECISDNKSAT MELEKLQPSF EALKRRGEEL IGRSQGADKD LAAKEIQDKL 4020
DQMVFFWEDI KARSEEREIK FLDVLELAEK FWYDMAALLT TIKDTQEIVH DLESPGIDPS 4080
IIKQQVEAAE TIKEETDGLH EELEFIRILG ADLIFACGET EKPEVKKSID EMNNAWENLN 4140
RTWKERLEKL EDAMQAAVQY QDTLQAMFDW LDNTVIRLCT MPPVGTDLNT VKDQLNEMKE 4200
FKVEVYQQQI EMEKLNHQGE LMLKKATDET DRDIIREPLT ELKHLWENLG EKIAHRQHKL 4260
EGALLALGQF QHALEELMGW LTHTEELLDA QRPISGDPKV IEVELAKHHV LKNDVLAHQA 4320
TVETVNKAGN ELLESSAGDD ASSLRSRLET MNQCWESVLQ KTEEREQQLQ STLQQAQGFH 4380
SEIEEFLLEL NRMESQLSAS KPTGGLPETA REQLDAHMEL HSQLRAKEEI YNQLLDKGRL 4440
MLLSRGDSGS GSKTEQSVAL LEQKWHVVSS KVEERKSKLE EALSLATEFQ NSLQEFINWL 4500
TLAEQSLNIA SPPSLILNTV LSQIEEHKVF ANEVNAHRDQ IIELDQTGNQ LKFLSQKQDV 4560
VLIKNLLVSV QSRWEKVVQR SIERGRSLDD ARKRAKQFHE AWKKLIDWLE DAESHLDSEL 4620
EISNDPDKIK LQLSKHKEFQ KTLGGKQPVY DTTIRTGRAL KEKTLLADDA QKLDNLLGEV 4680
RDKWDTVCGK SVERQHKLEE ALLFSGQFMD ALQALVDWLY KVEPQLAEDQ PVHGDLDLVM 4740
NLMDAHKVFQ KELGKRTGTV QVLKRSGREL IESSRDDTTW VKGQLQELST RWDTVCKLSV 4800
SKQSRLEQAL KQAEEFRDTV HMLLEWLSEA EQTLRFRGAL PDDTEALQSL IDTHKEFMKK 4860
VEEKRVDVNA AVAMGEVILA VCHPDCITTI KHWITIIRAR FEEVLTWAKQ HQQRLETALS 4920
ELVANAELLE ELLAWIQWAE TTLIQRDQEP IPQNIDRVKA LITEHQSFME EMTRKQPDVD 4980
RVTKTYKRKN IEPTHAPFIE KSRSGSRKSL NQPTPPPMPI LSQSEAKNPR INQLSARWQQ 5040
VWLLALERQR KLNDALDRLE ELKEFANFDF DVWRKKYMRW MNHKKSRVMD FFRRIDKDQD 5100
GKITRQEFID GILASKFPTT KLEMTAVADI FDRDGDGYID YYEFVAALHP NKDAYRPTTD 5160
ADKIEDEVTR QVAQCKCAKR FQVEQIGENK YRFGDSQQLR LVRILRSTVM VRVGGGWMAL 5220
DEFLVKNDPC RARGRTNIEL REKFILPEGA SQGMTPFRSR GRRSKPSSRA ASPTRSSSSA 5280
SQSNHSCTSM PSSPATPASG TKVISSTGSK LKRPTPTFHS SRTSLAGDTS NSSSPASTGA 5340
KTNRADPKKS ASRPGSRAGS RAGSRASSRR GSDASDFDLL ETQSACSDTS ESSAAGGQGS 5400
SRRGLTKPSK IPTMSKKTTT ASPRTPCPKR 5430 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:Compara.
 GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
 GO:0005874; C:microtubule; ISS:UniProtKB.
 GO:0032587; C:ruffle membrane; ISS:UniProtKB.
 GO:0016887; F:ATPase activity; ISS:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 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; ISS:UniProtKB.
 GO:0001707; P:mesoderm formation; IEA:Compara.
 GO:0030177; P:positive regulation of Wnt receptor signaling pathway; IMP: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; ISS: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.
 IPR001452; SH3_domain.
 IPR018159; Spectrin/alpha-actinin.
 IPR002017; Spectrin_repeat. 
Pfam
 PF00307; CH
 PF13499; EF_hand_5
 PF02187; GAS2
 PF00435; Spectrin 
SMART
 SM00033; CH
 SM00054; EFh
 SM00243; GAS2
 SM00326; SH3
 SM00150; SPEC 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS51460; GAR
 PS50002; SH3 
PRINTS