CYTSA_CANLF
ID CYTSA_CANLF Reviewed; 1117 AA.
AC Q2KNA0;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
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; AY884295; AAX84186.1; -; mRNA.
DR RefSeq; NP_001041579.1; NM_001048114.1.
DR RefSeq; XP_005636591.1; XM_005636534.1.
DR RefSeq; XP_005636592.1; XM_005636535.1.
DR RefSeq; XP_005636594.1; XM_005636537.1.
DR RefSeq; XP_013963585.1; XM_014108110.1.
DR AlphaFoldDB; Q2KNA0; -.
DR SMR; Q2KNA0; -.
DR STRING; 9615.ENSCAFP00000020373; -.
DR PaxDb; Q2KNA0; -.
DR Ensembl; ENSCAFT00040033613; ENSCAFP00040029250; ENSCAFG00040018176.
DR Ensembl; ENSCAFT00845039043; ENSCAFP00845030582; ENSCAFG00845022108.
DR GeneID; 486397; -.
DR KEGG; cfa:486397; -.
DR CTD; 23384; -.
DR VEuPathDB; HostDB:ENSCAFG00845022108; -.
DR eggNOG; KOG4678; Eukaryota.
DR GeneTree; ENSGT00940000153592; -.
DR HOGENOM; CLU_009328_1_0_1; -.
DR InParanoid; Q2KNA0; -.
DR OMA; FDSASQX; -.
DR OrthoDB; 854083at2759; -.
DR TreeFam; TF316716; -.
DR Proteomes; UP000002254; Chromosome 26.
DR Bgee; ENSCAFG00000013823; Expressed in lung and 48 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 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_0000231017"
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 852..878
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 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..55
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 862..876
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..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; 124639 MW; 6846AA7DE50499D4 CRC64;
MKKASRSVGS VPKVSGISKT QTVEKTKPEN SSSASTGGKV IKTGTTASLS KTKSSDDLLA
GMAGGVTVTN GVKGKKSTCP STGSSASAPA MTTVENKSKI STGTSSSTKR STSIGNKESS
STRERLRERT RLNQSKKLPS AGQGANDVAL AKRSRSRTTT ECDVRMSKSK SDNQISDKAA
LEAKVKDLLT LAKTKDVEIL HLRNELRDMR AQLGINEDHS EGDEKSEKEA 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
NHHMERIIES EQKGKAALAA TLEEYKATVA SDQIEMNRLK AQLENEKQKV AELYSIHNSG
DKSDIQDLLE SVRLDKEKAE TLASSLQEDL AHTRNDANRL QDTIAKVEDE YRAFQEEAKK
QIEELNMTLE KLRSELEEKE TERSDMKETI FELEDEVEQH RAVKLHDNLI ISDLENTVKK
LQDQKHDMER EIKTLHRRLR EESAEWRQFQ ADLQTAVVIA NDIKSEAQEE IGDLKRRLHE
AQEKNEKLTK ELEEIKSRKQ EEERGRVYNY MNAVERDLAA LRQGMGLSRR SSTSSEPTPT
VKTLIKSFDS ASQVPNPTAA AIPRTPLSPS PMKTPPAAAV SPMQRHSISG PISTSKPLTA
LSDKRPNYGE IPVQEHLLRT SSTSRPASLP RVPAMESAKT ISVSRRSSEE MKRDISAPEG
ASPASLMAMG TTSPQLSLSS SPTASVTPTT RSRIREERKD PLSALAREYG GSKRNALLKW
CQKKTEGYQN IDITNFSSSW NDGLAFCALL HTYLPAHIPY QELNSQDKRR NFTLAFQAAE
SVGIKSTLDI NEMVRTERPD WQSVMLYVTA IYKYFET
