CYTSA_PANTR
ID CYTSA_PANTR Reviewed; 1117 AA.
AC Q2KNA1;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 75.
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;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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.
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 {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Cell junction, gap junction
CC {ECO:0000250}. Note=Colocalizes with beta-tubulin, acetylated alpha-
CC tubulin and F-actin. Also observed in a ring around gamma-tubulin
CC containing centrioles possibly in the microtubule organizing center (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytospin-A family. {ECO:0000305}.
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DR EMBL; AY884294; AAX84185.1; -; mRNA.
DR RefSeq; NP_001035052.1; NM_001039963.1.
DR AlphaFoldDB; Q2KNA1; -.
DR SMR; Q2KNA1; -.
DR STRING; 9598.ENSPTRP00000059318; -.
DR PaxDb; Q2KNA1; -.
DR PRIDE; Q2KNA1; -.
DR GeneID; 458713; -.
DR KEGG; ptr:458713; -.
DR CTD; 23384; -.
DR eggNOG; KOG4678; Eukaryota.
DR InParanoid; Q2KNA1; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell junction; Coiled coil; Cytoplasm;
KW Cytoskeleton; Gap junction; Phosphoprotein; Reference proteome.
FT CHAIN 1..1117
FT /note="Cytospin-A"
FT /id="PRO_0000231020"
FT DOMAIN 1011..1116
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
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 919..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..280
FT /evidence="ECO:0000255"
FT COILED 394..449
FT /evidence="ECO:0000255"
FT COILED 487..807
FT /evidence="ECO:0000255"
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"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KN98"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KN98"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KN98"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YQ0"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YQ0"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YQ0"
SQ SEQUENCE 1117 AA; 124561 MW; A30D1EDEBF8D7AC6 CRC64;
MKKASRSVGS VPKVSAISKT QTAEKIKPEN SSSASTGGKL VKPGTAASLS KTKSSDDLLA
GMAGGVTVTN GVKGKKSTCP SAAPSASAPA MTTVENKSKI STGTASSTKR NTSTGNKESS
STRERLRERT RLNQSKKLPS AGQGANDMAL AKRSRSRTAT ECDVRMSKSK SDNQISDRAA
LEAKVKDLLT LAKTKDVEIL HLRNELRDMR AQLGINEDHS EGDEKSEKET IMAHQPTDVE
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 AELYSIHNSG
DKSDIQDLLE SVRLDKEKAE TLASSLQEDL AHTRNDANRL QDAIAKVEDE YRAFQEEAKK
QIEDLNMTLE KLRSDLDEKE TERSDMKETI FELEDEVEQH RAVKLHDNLI ISDLENTVKK
LQDQKHDMER EIKTLHRRLR EESAEWRQFQ ADLQTAVVIA NDIKSEAQEE IGDLKRRLHE
AQEKNEKLTK ELEEIKSRKQ EEERGRVYNY MNAVERDLAA LRQGMGLSRR SSTSSEPTPT
VKTLIKSFDS ASQVPNPAAA AIPRTPLSPS PMKTPPAAAV SPMQRHSISG PISTSKPLTA
LSDKRPNYGE IPVQEHLLRT SSASRPASLP RGPAMESAKT LSVSRRSSEE MKRDISAQEG
ASPASLMAMG TTSPQLSLSS SPTASVTPTT RSRIREERKD PLSALAREYG GSKRNALLKW
CQKKTEGYQN IDITNFSSSW NDGLAFCALL HTYLPAHIPY QELNSQDKRR NFMLAFQAAE
SVGIKSTLDI NEMVRTERPD WQNVMLYVTA IYKYFET
