CYTSA_MOUSE
ID CYTSA_MOUSE Reviewed; 1118 AA.
AC Q2KN98; Q8CHF9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cytospin-A;
DE AltName: Full=SPECC1-like protein;
DE AltName: Full=Sperm antigen with calponin homology and coiled-coil domains 1-like;
GN Name=Specc1l; Synonyms=Cytsa, Kiaa0376;
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 [MRNA].
RA Huang C.-H., Ye T., Chen Y.;
RT "Characterization of cytospin A as a multiple coiled coil protein involved
RT in cytokinesis and spindle organization.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385; SER-386; SER-390 AND
RP SER-888, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=21703590; DOI=10.1016/j.ajhg.2011.05.023;
RA Saadi I., Alkuraya F.S., Gisselbrecht S.S., Goessling W., Cavallesco R.,
RA Turbe-Doan A., Petrin A.L., Harris J., Siddiqui U., Grix A.W. Jr.,
RA Hove H.D., Leboulch P., Glover T.W., Morton C.C., Richieri-Costa A.,
RA Murray J.C., Erickson R.P., Maas R.L.;
RT "Deficiency of the cytoskeletal protein SPECC1L leads to oblique facial
RT clefting.";
RL Am. J. Hum. Genet. 89:44-55(2011).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: May interact with both microtubules and actin cytoskeleton.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21703590}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250}. Cell junction, gap junction {ECO:0000250}.
CC Note=Colocalizes with beta-tubulin, acetylated alpha-tubulin and F-
CC actin. Also observed in a ring around gamma-tubulin containing
CC centrioles possibly in the microtubule organizing center (By
CC similarity). {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: At 9.5-10.5 dpc, expressed in the developing
CC maxillary prominence and the lateral nasal process, as well as in the
CC limbs and eye. {ECO:0000269|PubMed:21703590}.
CC -!- SIMILARITY: Belongs to the cytospin-A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41420.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY884297; AAX84188.1; -; mRNA.
DR EMBL; AB093236; BAC41420.1; ALT_INIT; mRNA.
DR CCDS; CCDS48599.1; -.
DR RefSeq; NP_001139298.1; NM_001145826.1.
DR RefSeq; NP_700455.3; NM_153406.3.
DR RefSeq; XP_006514315.1; XM_006514252.3.
DR RefSeq; XP_011241891.1; XM_011243589.2.
DR RefSeq; XP_017169616.1; XM_017314127.1.
DR AlphaFoldDB; Q2KN98; -.
DR SMR; Q2KN98; -.
DR BioGRID; 216715; 10.
DR IntAct; Q2KN98; 3.
DR STRING; 10090.ENSMUSP00000045099; -.
DR iPTMnet; Q2KN98; -.
DR PhosphoSitePlus; Q2KN98; -.
DR jPOST; Q2KN98; -.
DR MaxQB; Q2KN98; -.
DR PaxDb; Q2KN98; -.
DR PeptideAtlas; Q2KN98; -.
DR PRIDE; Q2KN98; -.
DR ProteomicsDB; 279140; -.
DR DNASU; 74392; -.
DR Ensembl; ENSMUST00000218766; ENSMUSP00000151322; ENSMUSG00000033444.
DR GeneID; 74392; -.
DR KEGG; mmu:74392; -.
DR UCSC; uc007fqe.2; mouse.
DR CTD; 23384; -.
DR MGI; MGI:1921642; Specc1l.
DR VEuPathDB; HostDB:ENSMUSG00000033444; -.
DR eggNOG; KOG4678; Eukaryota.
DR GeneTree; ENSGT00940000153592; -.
DR HOGENOM; CLU_009328_1_0_1; -.
DR InParanoid; Q2KN98; -.
DR OrthoDB; 854083at2759; -.
DR PhylomeDB; Q2KN98; -.
DR TreeFam; TF316716; -.
DR BioGRID-ORCS; 74392; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Specc1l; mouse.
DR PRO; PR:Q2KN98; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q2KN98; protein.
DR Bgee; ENSMUSG00000033444; Expressed in otolith organ and 223 other tissues.
DR ExpressionAtlas; Q2KN98; baseline and differential.
DR Genevisible; Q2KN98; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031941; C:filamentous actin; IDA:MGI.
DR GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IDA:MGI.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008013; F:beta-catenin binding; IPI:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0034332; P:adherens junction organization; IMP:MGI.
DR GO; GO:0061713; P:anterior neural tube closure; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IMP:MGI.
DR GO; GO:0060325; P:face morphogenesis; ISO:MGI.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IDA:MGI.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR GO; GO:0036032; P:neural crest cell delamination; IMP:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:MGI.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR040166; CYTSA.
DR PANTHER; PTHR23167:SF18; PTHR23167:SF18; 1.
DR Pfam; PF00307; CH; 1.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell junction; Coiled coil; Cytoplasm;
KW Cytoskeleton; Gap junction; Phosphoprotein; Reference proteome.
FT CHAIN 1..1118
FT /note="Cytospin-A"
FT /id="PRO_0000231019"
FT DOMAIN 1012..1117
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..281
FT /evidence="ECO:0000255"
FT COILED 395..450
FT /evidence="ECO:0000255"
FT COILED 488..808
FT /evidence="ECO:0000255"
FT COMPBIAS 11..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..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 966..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YQ0"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YQ0"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1118 AA; 124488 MW; 1670E69840146D8F CRC64;
MKKANRSAGS VPKVSGISKP QTVEKSKPEN SSSAPTGVKP VRPGAAAALS KTKSNDDLLA
GMAGGVNVTN GIKAKKSTCS SAAPSAPAPA MTISENKSKI STGTSSSAKR STSAGNKESS
STRERLRERT RLNQSKKLPS VSQGANDVAL AKRSRSRTAA EGDIRMSKSK SDNQISDKAA
LEAKVKDLLT LAKTKDVEIL HLRNELRDMR AQLGISEDHC EGEDRSEVKE TIIAHQPTDV
ESTLLQLQEQ NTAIREELNQ LKNENRMLKD RLNALGFSLE QRLDNSEKLF GYQSLSPEIT
PGNQSDGGGT LTSSVEGSAP GSVEDLLSQD ENTLMDHQHS NSMDNLDSEC SEVYQPLTSS
DDALDAPSSS ESEGVPSIER SRKGSSGNAS EVSVACLTER IHQMEENQHS TSEELQATLQ
ELADLQQITQ ELNSENERLG EEKVILMESL CQQSDKLEHF GRQIEYFRSL LDEHHISYVI
DEDVKSGRYM ELEQRYMDLA ENARFEREQL LGVQQHLSNT LKMAEQDNKE AQEMIGALKE
RSHHMERIIE SEQKGKAALA ATLEEYKATV ASDQIEMNRL KAQLENEKQK VAELYSIHNS
GDKSDIQDLL ESVRLDKEKA ETLASSLQED LAHTRNDANR LQDTIAKVED EYRAFQEEAK
KQIEDLNMTL EKLRSELEEK DTERSDMKET IFELEDEVEQ HRAVKLHDNL IISDLENTVK
KLQDQKHDME REIKTLHRRL REESAEWRQF QADLQTAVVI ANDIKSEAQE EIGDLKRRLH
EAQEKNEKLT KELEEIKSRK QEEERGRVYN YMNAVERDLA ALRQGMGLSR RSSTSSEPTP
TVKTLIKSFD SASQVPNAAA AAIPRTPLSP SPMKTPPAAA VSPMQRHSIS GPISTSKPLT
ALSDKRSNYG ELPVQEHLLR TSSTSRPASL PRVPAMESAK TISVSRRSSE EMKRDISASE
GASPASLMAM GTTSPQLSLS SSPTASVTPS TRSRIREERK DPLSALAREY GGSKRNALLK
WCQKKTEGYQ NIDITNFSSS WNDGLAFCAL LHTYLPAHIP YQELNSQDKK RNFTLAFQAA
ESVGIKSTLD INEMARTERP DWQNVMLYVT AIYKYFET
