CYTSA_TAKRU
ID CYTSA_TAKRU Reviewed; 1118 AA.
AC Q2KN94;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 63.
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 Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
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; AY884301; AAX84192.1; -; mRNA.
DR RefSeq; NP_001072071.1; NM_001078603.1.
DR AlphaFoldDB; Q2KN94; -.
DR SMR; Q2KN94; -.
DR STRING; 31033.ENSTRUP00000039399; -.
DR PRIDE; Q2KN94; -.
DR GeneID; 777979; -.
DR KEGG; tru:777979; -.
DR CTD; 561775; -.
DR eggNOG; KOG4678; Eukaryota.
DR InParanoid; Q2KN94; -.
DR OrthoDB; 854083at2759; -.
DR Proteomes; UP000005226; 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; Reference proteome.
FT CHAIN 1..1118
FT /note="Cytospin-A"
FT /id="PRO_0000231024"
FT DOMAIN 1012..1117
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 225..264
FT /evidence="ECO:0000255"
FT COILED 384..438
FT /evidence="ECO:0000255"
FT COILED 475..796
FT /evidence="ECO:0000255"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..874
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 123319 MW; 42BE47003860DC59 CRC64;
MKKSVRPAVS RASGERGKPE VAGTTGTGKP VSKSSTAAPL SKVKSSDDLL AAMAGGNPTS
SNAVAKTKRT ASVGTTASTL DKPKTTSGTT SKRLTSSVTK ETNLTRDRLR TSRASANKKQ
SAAGTVVGDA ASGKRSRSQV LVESESRMSK SKSDGQISDK VALEAKVKDL LGLAKSKDVE
ILHLRSELRD MRVQLGLGGK ELQEGPEEEE EEEEEEKPHV SAITAADVES TLILLQEQNQ
AIREELNLLK SENRMLKDRL NALGFSLEQR LDGSDKLFSY ASLSPDLAAG SGQSDGGGTG
TLTSSVEGSA PGSLEDLLAG HQHGGSADNL DSESSEVYQA VTSSDDALDA PSGASSSSES
ECAPSRERSR RGSSGNASEV SVACLTERIH QMEENQHSTA EELQATLQEL ADLQQITQEL
NGENERLGEE KVILMDSLCQ QSDKLELYGR QIEYLRSLLD EHHVSYVLEE DIKSGRYMEL
EQRYADLAEN ARFEREQLLG VQQHLSNTLK MAEQDNAEAQ EMIGALKERN HQMERIMESE
RQGRAAVEAA LHEYKDAVSS EQAELSRCRA QLDQERQRVA ELYSLHTAGD KNDICQLLEG
VRLGKEEAEA KAAKLQEGLE QAHSDLGHLQ ETFSKLDREY REFREQAQRQ LSEQERALEK
QRMDLQEKET EIADMKETIF ELEDEVEQHR ALKLHDNLII TDLENSVKKL QDQKHDMERE
IKILHRRLRE ESMEWRQFQA DLQTAVVIAN DIKSEAQEEI GDLRRRLQEA QEKNEKLSKE
LEEVKSRKQD EERGRVYNYM NAVERDLAAL RQGMGLSRRS STSSEPSPTV KTLIKSFDSA
SQGPPSNGAS VTPTVSAAPL PRTPLSPSPM KTPPAAAVSP IQRHSISGSM SAAKPLSSLG
DKRPTYTDIT IPTEHLLRGS AASRPPSALQ RVSNMDSTKT ISVSRRSSEE MKRDMSASEG
ASSTSLMAMS AASAPLSLSS SSPTASVTPT TRSRLREERK DPLSALAREY GGSKRNALLK
WCQKKTEGYQ NIDITNFSSS WNDGLAFCAV LHTYLPAHIP YQELTSQEKR RNFTLAFQAA
ESVGIKCTLD INDMVHTERP DWQSVMTYVT AIYKYFET
