K0754_MOUSE
ID K0754_MOUSE Reviewed; 3305 AA.
AC Q69ZZ9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 3.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Microtubule-actin cross-linking factor 1, isoforms 6/7 {ECO:0000305};
DE AltName: Full=Uncharacterized protein KIAA0754;
GN Name=Macf1 {ECO:0000312|MGI:MGI:108559}; Synonyms=Kiaa0754;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 177-3305 (ISOFORM 7).
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|PROSITE-
CC ProRule:PRU00792}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=6;
CC IsoId=Q69ZZ9-2; Sequence=Displayed;
CC Name=7;
CC IsoId=Q69ZZ9-1; Sequence=VSP_061508, VSP_061509;
CC Name=1; Synonyms=Macf1b;
CC IsoId=Q9QXZ0-1; Sequence=External;
CC Name=2; Synonyms=Macf1a;
CC IsoId=Q9QXZ0-2; Sequence=External;
CC Name=3;
CC IsoId=Q9QXZ0-3; Sequence=External;
CC Name=4;
CC IsoId=Q9QXZ0-4; Sequence=External;
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DR EMBL; AL606918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK173019; BAD32297.1; -; mRNA.
DR AlphaFoldDB; Q69ZZ9; -.
DR iPTMnet; Q69ZZ9; -.
DR PhosphoSitePlus; Q69ZZ9; -.
DR jPOST; Q69ZZ9; -.
DR MaxQB; Q69ZZ9; -.
DR PeptideAtlas; Q69ZZ9; -.
DR PRIDE; Q69ZZ9; -.
DR UCSC; uc012dkt.1; mouse. [Q69ZZ9-2]
DR MGI; MGI:108559; Macf1.
DR InParanoid; Q69ZZ9; -.
DR PRO; PR:Q69ZZ9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q69ZZ9; protein.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0051011; F:microtubule minus-end binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:MGI.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:MGI.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IMP:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0030334; P:regulation of cell migration; ISO:MGI.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0032886; P:regulation of microtubule-based process; ISO:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IBA:GO_Central.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 8.
DR Gene3D; 3.30.920.20; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR003108; GAR_dom.
DR InterPro; IPR036534; GAR_dom_sf.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR23169; PTHR23169; 4.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF02187; GAS2; 1.
DR Pfam; PF00435; Spectrin; 14.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00243; GAS2; 1.
DR SMART; SM00150; SPEC; 17.
DR SUPFAM; SSF143575; SSF143575; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51460; GAR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cytoplasm; Cytoskeleton; Metal-binding;
KW Reference proteome.
FT CHAIN 1..3305
FT /note="Microtubule-actin cross-linking factor 1, isoforms
FT 6/7"
FT /id="PRO_0000295723"
FT DOMAIN 2958..2993
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 2994..3029
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 3034..3106
FT /note="GAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792"
FT REGION 108..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2865..2891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3122..3305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..979
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3141..3215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3252..3305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2971
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2973
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2975
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2977
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2982
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 3007
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 3009
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 3011
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 3013
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 3018
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 1091..1115
FT /note="LFQKDQVDPLQVKLQQVNGLGQGLI -> VIVDHFIGRKGLEHKVRIASSLT
FT WC (in isoform 7)"
FT /id="VSP_061508"
FT VAR_SEQ 1116..3305
FT /note="Missing (in isoform 7)"
FT /id="VSP_061509"
SQ SEQUENCE 3305 AA; 369258 MW; 76642D9328CC2AC7 CRC64;
MGKPLSRPDC LRRNPTCLGK GEDEDGYIED CYVPQRSIYD TMRINEQIDQ GSKLNQTSKS
TMEKMEGSTI SSNGTLGASS NVFEARGPEG KKLDERIIFD ALKLSSDVQK SAPVPPRRRP
NAERKDNVNR RSWKSFMPPN FPEFAERMEA SLSEVSEAGA SNPSLQEKKE SSSALTESSG
HFDHREPQSE SVTLEHMSKS VDIPEVQNVK NLRDCQDFKF QQHSESSPHE FQPLGSEAAA
ASGNTDEMQE HRFSSATWPR AMKSSSKGGF SEKQYPLGDT ACAVELPPLS PCLSEELLDP
ELHMLITPSL REKTESELKF EEDERWIMME AEEEWEEEKL SEERKSLVTN EETSLADPLE
ESDQANSVPA VEDGSDRVAV SGTSDHLALH QMCCSVDLQP TRDQLASVPR GSPPDCTCVP
AGDTVISEVK NRPDQGLEGL TSGLQCPVEA EQLSDTDSVQ MFLELEKECL CEEGVTSSAE
LLSQASSEGL APTQDAEDSL LISHFPGAAL EQEQHVGFLS VRIKDPDTGL DGEYCNALDS
SQVPKAVELC AQPDSGRDAS TISKECEKVP FSPKIGGEFK LLADLEPHSE LDTGGLLNSN
LRASCEENLP VFIASELAKE NGNLSQVDCS QTEGNVEEYM ERIPLSFAFN YEQDVTSGPE
VEVFSSDSNL LTDEIHLESG KGALISQEDS NLASLGNVDL CELSMEKVCD KDGETKEPGC
QGKLLGNGAP AQFPTDFQRR SSESEVLSLH LLAGELRLNK AGAETMSDRE PQLSMALSQE
GELEMRDLDS TLNIFPEEQI SKASNTVPGL EEWISSQQRP VPAAVVPMVE NALDAVTPMP
GEDIPAVALT ASEGPAANAS ASDGTAAATP IVPIPEEDIP GASVVILVED VMTAAISAPE
QAAASSGAVP PVETVTVPII DEDVTSEEPD TQAAEMFLPE EPAIPTPAGP TAEEPDTPTV
PVSTAEEPSM PPPAGPTPEE SAAPTLKEPT PEKPDTQVVS SSIPEWSATP ATAVPAKEIF
SPDGPFLEGT THTDSVPISE ETPVLENASS PGMGIKECLD SSAFGIKEVP GTMIHGKVPL
AATDGLNSHE LFQKDQVDPL QVKLQQVNGL GQGLIQSAGK NCDVQGLEHD MDEINTRWNT
LNKKVAQRIA QLQEALLHCG KFQDALEPLL SWLTDTEELI ANQKPPSAEY KVVKAQIQEQ
KLLQRLLDDR KATVDMLQAE GGRIAQSAEL ADREKITGQL ESLERRWTDL LSKAAARQKQ
LEDILVLAKQ FHETAEPISD FLSVTEKKLA NSEPVGTQTA KIHQQIIRHK ALEEEIENHA
TDVHQAVKIG QSLSSLTCPA EQGIMSEKLD SLQARYSEIQ DRCCRKASLL EQALFNARLF
GEDEVEVLNW LAEVEDKLST VFVKDYRQDV LQKQHADHLA LNEEIINRKK NVDQAIKNGQ
ALLKQTTGEE VLLIQEKLDG IKTRYADITL TSSKALRTLE QARQLATKFH STYEELTGWL
REAEEELAAS GGQSPTGEQI PQFQQRQKEL KKEVMEHRLV LDTVNEVSHA LLELVPWRAR
EGLDKLVSDA NEQYKLISDT VGQRVDEIDA AIQRSQQYEQ AADAELAWVA ETKRKLMALG
PIRLEQDQTT AQLQVQKAFS IDIIRHKDSM DELFSHRGEI FSTCGEEQKA VLQEKTECLI
QQYEAVSLLN SERYARLERA QVLVNQFWET YEELSPWAEE TLALIAQLPP PAVDHEQLRQ
QQEEMRQLRE SIAEHKPHID KILKIGPQLK ELNPEEGKMV EEKYQKAENM YAQIKDEVRQ
RALALDEAVS QSAQFHDKIE PMLETLENLS SRLRMPPLIP AEVDKIRECI SDNKSATVEL
EKLQPSFEAL KRRGEELIGR SQGADKDLAA KEIQDKLDQM VFFWEDIKAR SEEREIKFLD
VLELAEKFWY DMAALLTTIK DTQDIVHDLE SPGIDPSIIK QQVEAAETIK EETDGLHEEL
EFIRILGADL IFACGETEKP EVKKSIDEMN NAWENLNKTW KERLEKLEDA MQAAVQYQDT
LQAMFDWLDN TVIKLCTMPP VGTDLNTVKD QLNEMKEFKV EVYQQQIEME KLNHQGELML
KKATDETDRD IIREPLTELK HLWENLGEKI AHRQHKLEGA LLALGQFQHA LEELMSWLTH
TEELLDAQRP ISGDPKVIEV ELAKHHVLKN DVLAHQATVA TVNKAGSELL ESSAGDDASS
LRSRLETMNQ CWESVLQKTE EREQQLQSTL QQAQGFHSEI EDFLLELNRM ENQLSASKPT
GGLPETAREQ LDTHMELHSQ LRAKEEIYNQ LLDKGRLMLL SRGDSGSGSK TEQSVALLEQ
KWHAVSSKVE ERKLEEALSL ATEFQNSLQE FINWLTLAEQ SLNIASPPSL ILNTVLSQIE
EHKVFANEVN DHRDQIIELD QTGNQLKFLS QKQDVVLIKN LLVSVQSRWE KVVQRSIERG
RSLDDARKRA KQFHEAWKKL IDWLEDAESH LDSELEISND PDKIKLQLSK HKEFQKTLGG
KQPVYDTTIR TGRALKEKTL LAGDTQKLDN LLGEVRDKWD TVCGKSVERQ HKLEEALLFS
GQFMDALQAL VDWLYKVEPQ LAEDQPVHGD LDLVMNLMDA HKVFQKELGK RTGTVQVLKR
SGRELIEGSR DDTTWVKGQL QELSTRWDTV CKLSVSKQSR LEQALKQAEE FRDTVHMLLE
WLSEAEQTLR FRGALPDDTE ALQSLIDTHK EFMKKVEEKR VDVNTAVAMG EAILAVCHPD
CITTIKHWIT IIRARFEEVL TWAKQHQQRL ETALSELVAN AELLEELLAW IQWAETTLIQ
RDQEPIPQNI DRVKALITEH QSFMEEMTRK QPDVDRVTKT YKRKSVEPTH APFMEKSRSG
SRKSLNQPTP PPMPILSQSE AKNPRINQLS ARWQQVWLLA LERQRKLNDA LDRLEELKEF
ANFDFDVWRK KYMRWMNHKK SRVMDFFRRI DKDQDGKITR QEFIDGILAS KFPTTKLEMT
AVADIFDRDG DGYIDYYEFV AALHPNKDAY RPTTDADKIE DEVTRQVAQC KCAKRFQVEQ
IGENKYRFGD SQQLRLVRIL RSTVMVRVGG GWMALDEFLV KNDPCRARGR TNIELREKFI
LPEGASQGMT PFRSRGRRSK PSSRAASPTR SSSSASQSNH SCTSMPSSPA TPASGTKVIS
SSGSKLKRPT PAFHSSRTSL AGDTSNSSSP ASTGAKANRA DPKKSASRPG SRAGSRAGSR
ASSRRGSDAS DFDLLETQSA CSDTSESSAA GGQGSSRRGL TKPSKIPTMS KKTTTASPRT
PGPKR
