CYTSA_DANRE
ID CYTSA_DANRE Reviewed; 1132 AA.
AC Q2KN93; B0UYP9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 87.
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=specc1la; Synonyms=cytsa, cytsaa, specc1l;
GN ORFNames=im:7159316, si:dkey-118g10.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
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 GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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; AY884302; AAX84193.1; -; mRNA.
DR EMBL; CR547121; CAQ15300.1; -; Genomic_DNA.
DR RefSeq; NP_001034905.1; NM_001039816.1.
DR RefSeq; XP_005167234.1; XM_005167177.3.
DR AlphaFoldDB; Q2KN93; -.
DR SMR; Q2KN93; -.
DR STRING; 7955.ENSDARP00000010292; -.
DR PaxDb; Q2KN93; -.
DR PRIDE; Q2KN93; -.
DR Ensembl; ENSDART00000014046; ENSDARP00000010292; ENSDARG00000006719.
DR Ensembl; ENSDART00000164976; ENSDARP00000135296; ENSDARG00000006719.
DR GeneID; 561775; -.
DR KEGG; dre:561775; -.
DR CTD; 561775; -.
DR ZFIN; ZDB-GENE-060810-139; specc1la.
DR eggNOG; KOG4678; Eukaryota.
DR GeneTree; ENSGT00940000153592; -.
DR InParanoid; Q2KN93; -.
DR OMA; FDSASQX; -.
DR OrthoDB; 854083at2759; -.
DR PhylomeDB; Q2KN93; -.
DR TreeFam; TF316716; -.
DR PRO; PR:Q2KN93; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000006719; Expressed in spleen and 20 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060325; P:face morphogenesis; IDA: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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell junction; Coiled coil; Cytoplasm;
KW Cytoskeleton; Gap junction; Reference proteome.
FT CHAIN 1..1132
FT /note="Cytospin-A"
FT /id="PRO_0000231023"
FT DOMAIN 1026..1131
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 226..268
FT /evidence="ECO:0000255"
FT COILED 385..440
FT /evidence="ECO:0000255"
FT COILED 478..798
FT /evidence="ECO:0000255"
FT COMPBIAS 25..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..891
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 40
FT /note="P -> S (in Ref. 1; AAX84193)"
FT /evidence="ECO:0000305"
FT CONFLICT 1106
FT /note="T -> N (in Ref. 1; AAX84193)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1132 AA; 123627 MW; D981C97E55FFF321 CRC64;
MKKAGRPVGN KAASGGGKGD SVTAGNCAGK NTVKSPTSAP LSKVKSNDDL LAAMAGSSAG
TNNSVAKGKK STSTHSTSCG TNTNNPDTKT KTTSGPSGKR TTSMTSKESN SSRERLRNSR
NSSSKKQSST GASDRAQPKH SRALAQTSDS ESRMSKSKSD GQLSDKVALE AKVKNLLGLA
KSKDVEILQL RGELRDMRVQ LGLPEEDEEE ERPPEREAAA VITAADVEST LLLLQEQNQA
IRGELNLLKN ENRMLKDRLN ALGFSLEQRL DGADKTFGFP STSPELSSGG AGAHGDCATV
ASSVEGSAPG SMEDLLTGGQ RSGSTDNLDS ESSEVYQAVT SSDDALDAPS GCGSSSSSES
EGGPPACRSS SRKGSSGNTS EVSVACLTER IHQMEENQHS TSEELQATLQ ELADLQQITQ
ELNGENERLG EEKVLLMDSL CQQSDKLEHC GRQIEYFRSL LDEHGVAYSV DEDIKSGRYM
ELEQRYVELA ENARFEREQL LGVQQHLSNT LKMAEQDNAE AQNVIAALKE RNHHMERLLD
VERQERASMA AVLEECKAAV NNDQAELSRC RVLLEQERQK VAELYSIHNA GDKSDIHQLL
EGVRLDKEEA EAKASKLQDD LGHARSEVAC LQDTLNKLDA EYRDFQSVVQ KELAEQKRAI
EKQREDLQEK ETEIGDMKET IFELEDEVEQ HRAVKLHDNL IISDLENSMK KLQDQKHDME
REIKILHRRL REESAEWRQF QADLQTAVVI ANDIKSEAQE EIGDLRRRLQ EAQEKNEKLG
KEIEEVKNRK QDEERGRVYN YMNAVERDLA ALRQGMGLSR RPSTSSEPSP TVKTLIKSFD
SASQGPGANA TAVAAAAAAA AAAAAVTVTS TTPTAPLPRT PLSPSPMKTP PAAAVSPIQR
HSITGSMAAA KPLSSLADKR PSYTDISMPA EHLLRAANSR PASALQRVSN MDTSKTITVS
RRSSEEPKRD ISTPDGGPAS SLISMSSAAA LSSSSSPTAS VNPTARSRLR EERKDPLSAL
AREYGGSKRN ALLRWCQKKT EGYQNIDITN FSSSWNDGLA FCAVLHTYLP AHIPYQELNS
QDKRRNFTLA FQAAESVGIK STLDITDMVH TERPDWQSVM TYVTSIYKYF ET
