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Database: UniProt
Entry: U3B8P4_CALJA
LinkDB: U3B8P4_CALJA
Original site: U3B8P4_CALJA 
ID   U3B8P4_CALJA            Unreviewed;      1117 AA.
AC   U3B8P4; F7I558;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Cytospin-A {ECO:0000256|ARBA:ARBA00015657, ECO:0000256|RuleBase:RU367063};
GN   Name=SPECC1L {ECO:0000313|EMBL:JAB02502.1,
GN   ECO:0000313|Ensembl:ENSCJAP00000093948.1};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB02502.1};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000093948.1, ECO:0000313|Proteomes:UP000008225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB02502.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Bladder {ECO:0000313|EMBL:JAB02502.1}, Cerebellum
RC   {ECO:0000313|EMBL:JAB51856.1}, Cerebral cortex
RC   {ECO:0000313|EMBL:JAB28261.1}, Hippocampus
RC   {ECO:0000313|EMBL:JAB19027.1}, and Skeletal muscle
RC   {ECO:0000313|EMBL:JAB36927.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
RN   [3] {ECO:0000313|Ensembl:ENSCJAP00000093948.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Involved in cytokinesis and spindle organization. May play a
CC       role in actin cytoskeleton organization and microtubule stabilization
CC       and hence required for proper cell adhesion and migration.
CC       {ECO:0000256|ARBA:ARBA00025131, ECO:0000256|RuleBase:RU367063}.
CC   -!- SUBUNIT: May interact with both microtubules and actin cytoskeleton.
CC       {ECO:0000256|ARBA:ARBA00011235, ECO:0000256|RuleBase:RU367063}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000256|ARBA:ARBA00004186, ECO:0000256|RuleBase:RU367063}.
CC       Cytoplasm, cytoskeleton {ECO:0000256|RuleBase:RU367063}. Cell junction,
CC       gap junction {ECO:0000256|RuleBase:RU367063}.
CC   -!- SIMILARITY: Belongs to the cytospin-A family.
CC       {ECO:0000256|ARBA:ARBA00009452, ECO:0000256|RuleBase:RU367063}.
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DR   EMBL; GAMT01009359; JAB02502.1; -; mRNA.
DR   EMBL; GAMS01004109; JAB19027.1; -; mRNA.
DR   EMBL; GAMR01005671; JAB28261.1; -; mRNA.
DR   EMBL; GAMQ01004924; JAB36927.1; -; mRNA.
DR   EMBL; GAMP01000899; JAB51856.1; -; mRNA.
DR   STRING; 9483.ENSCJAP00000017790; -.
DR   Ensembl; ENSCJAT00000118013.1; ENSCJAP00000093948.1; ENSCJAG00000009691.5.
DR   GeneTree; ENSGT00940000153592; -.
DR   OrthoDB; 5393863at2759; -.
DR   Proteomes; UP000008225; Chromosome 1.
DR   Bgee; ENSCJAG00000009691; Expressed in cerebellum and 6 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-UniRule.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR   CDD; cd21199; CH_CYTS; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   PANTHER; PTHR23167; CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED; 1.
DR   PANTHER; PTHR23167:SF18; CYTOSPIN-A; 1.
DR   Pfam; PF00307; CH; 1.
DR   SMART; SM00033; CH; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   PROSITE; PS50021; CH; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle {ECO:0000256|RuleBase:RU367063};
KW   Cell division {ECO:0000256|RuleBase:RU367063};
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949,
KW   ECO:0000256|RuleBase:RU367063}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|RuleBase:RU367063};
KW   Cytoskeleton {ECO:0000256|RuleBase:RU367063};
KW   Gap junction {ECO:0000256|ARBA:ARBA00022868,
KW   ECO:0000256|RuleBase:RU367063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT   DOMAIN          1011..1116
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   REGION          1..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          920..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          243..270
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          400..441
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          488..805
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        11..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..990
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1117 AA;  124515 MW;  F33445AE500A70A6 CRC64;
     MRKASRSVGS VPKVSGISKT QTAEKIKPEN SSSASTGGKP VKPGTAASLS KTKSSDDLLA
     GMAGGVTVTN GVKGKKSTCP SAAPSASAPA MTTVENKSKI STGTASSTKR STSTGNKESS
     STRERLRERT RLNQSKKLPS AGQGANDVAL AKRSRSRTAT ECDVRMSKSK SDNQISDKAA
     LEAKVKDLLT LAKTKDVEIL HLRNELRDMR AQLGISEEHS EGDEKSEKET IIAHQPTDVE
     STLLQLQEQN TAIREELNQL KNENRMLKDR LNALGFSLEQ RLDNSEKLFG YQSLSPEITP
     GNQSDGGGTL TSSVEGSAPG SVEDLLSQDE NTLMDHQHSN SMDNLDSECS EVYQPLTSSD
     DALDAPSSSE SEGIPSIERS RKGSSGNASE VSVACLTERI HQMEENQHST SEELQATLQE
     LADLQQITQE LNSENERLGE EKVILMESLC QQSDKLEHFS RQIEYFRSLL DEHHISYVID
     EDVKSGRYME LEQRYMDLAE NARFEREQLL GVQQHLSNTL KMAEQDNKEA QEMIGALKER
     SHHMERIIES EQKGKAALAA TLEEYKATVA SDQIEMNRLK AQLENEKQKV TELYSIHNSG
     DKSDIQDLLE SVRLDKEKAE TLASSLQEDL AHTQNDANRL QDALAKVEDE YRAFQEDAKK
     QIEDLNMTLE KLRSELDEKE TERSDMKETI FELEDEVEQH RAVKLHDNLI ISDLENTVKK
     LQDQKHDMER EIKTLHRRLR EESAEWRQFQ ADLQTAVVIA NDIKSEAQEE IGDLKRRLHE
     AQEKNEKLTK ELEEIKSRKQ EEERGRVYNY MNAVERDLAA LRQGMGLSRR SSTSSEPTPT
     VKTLIKSFDS ASQVPNPAAA AIPRTPLSPS PMKTPPAAAV SPMQRHSISG PISTSKPLTA
     LSDKRPNYGE IPVQEHLLRT SSTSRPASLP RVPAMESAKT LSVSRRSSEE MKRDISAQEG
     ASPASLMAMG TTSPQLSLSS SPTASVTPTT RSRIREERKD PLSALAREYG GSKRNALLKW
     CQKKTEGYQN IDITNFSSSW NDGLAFCALL HTYLPAHIPY QELNSQDKRR NFMLAFQAAE
     SVGIKSTLDI NEMVRTERPD WQNVMLYVTA IYKYFET
//
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