CYTSA_CHICK
ID CYTSA_CHICK Reviewed; 1118 AA.
AC Q2KN97;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 91.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX84189.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY884298; AAX84189.1; ALT_INIT; mRNA.
DR RefSeq; NP_001038102.1; NM_001044637.1.
DR RefSeq; XP_015130808.1; XM_015275322.1.
DR RefSeq; XP_015130809.1; XM_015275323.1.
DR RefSeq; XP_015130810.1; XM_015275324.1.
DR RefSeq; XP_015130811.1; XM_015275325.1.
DR RefSeq; XP_015130812.1; XM_015275326.1.
DR AlphaFoldDB; Q2KN97; -.
DR SMR; Q2KN97; -.
DR STRING; 9031.ENSGALP00000033238; -.
DR PaxDb; Q2KN97; -.
DR Ensembl; ENSGALT00000033880; ENSGALP00000033238; ENSGALG00000006648.
DR GeneID; 416950; -.
DR KEGG; gga:416950; -.
DR CTD; 23384; -.
DR VEuPathDB; HostDB:geneid_416950; -.
DR eggNOG; KOG4678; Eukaryota.
DR GeneTree; ENSGT00940000153592; -.
DR HOGENOM; CLU_009328_1_0_1; -.
DR InParanoid; Q2KN97; -.
DR OMA; FDSASQX; -.
DR OrthoDB; 854083at2759; -.
DR PhylomeDB; Q2KN97; -.
DR PRO; PR:Q2KN97; -.
DR Proteomes; UP000000539; Chromosome 15.
DR Bgee; ENSGALG00000006648; Expressed in cerebellum and 13 other tissues.
DR ExpressionAtlas; Q2KN97; baseline and differential.
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; Reference proteome.
FT CHAIN 1..1118
FT /note="Cytospin-A"
FT /id="PRO_0000231022"
FT DOMAIN 1012..1117
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 299..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 856..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 193..281
FT /evidence="ECO:0000255"
FT COILED 396..450
FT /evidence="ECO:0000255"
FT COILED 488..808
FT /evidence="ECO:0000255"
FT COMPBIAS 14..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..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 136..153
FT /note="Polar 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 299..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..877
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 124909 MW; 8BADEFEFCCF8096A CRC64;
MKKASRSVGS VPKVPGVNKT QTTEKTKPES GSSLSAVTKL SKPGTSASLL KTKSNDDLLA
GMASGGGVTM TNGVKAKKST CASTVSSTTG TTMSTLENKP RTVAGSTARR STSSGTKESS
SSRERIRDRS RLSQSKKLPL AGQGSNDTVL AKRSRSRTNP ESDIRMSKSK SDNQISDKAA
LEAKVNDLLT LAKTKDVEIL HLRNELRDMR AQLGLNEDQV EGDEKSEEKE AIVVHQPTDV
ESTLLQLQEQ NTAIREELNQ LKNENRMLKD RLNALGFSLE QRLDNSEKLF GYQSLSPEIT
AGNHSDGGGT LTSSVEGSAP GSMEDLLSQD EHTLMDNQHS NSMDNLDSEC SEVYQPLTSS
DDALDAPSSS ESEGVPSIER SRKGSSGNAS EVSVACLTER IHQMEENQHS TAEELQATLQ
ELADLQQITQ ELNSENERLG EEKVILMESL CQQSDKLEHF SRQIEYFRSL LDEHHISYVI
DEDMKSGRYM ELEQRYMDLA ENARFEREQL LGVQQHLSNT LKMAEQDNKE AQEMIGALKE
RNHHMERIIE SEQKSKTAIA STLEEYKATV ASDQIEMNRL KAQLEHEKQK VAELYSIHNS
GDKSDIQDLL ESVRLDKEKA ETLASSLQEE LAHTRNDANR LQDAIAKVED EYRVFQEEAK
KQIEDLNVTL EKLRAELDEK ETERSDMKET IFELEDEVEQ HRAVKLHDNL IISDLENTVK
KLQDQKHDME REIKNLHRRL REESAEWRQF QADLQTAVVI ANDIKSEAQE EIGDLKRRLH
EAQEKNEKLT KELEEIKSRK QEEERGRVYN YMNAVERDLA ALRQGMGLSR RSSTSSEPTP
TVKTLIKSFD SASQVPSPAA ATIPRTPLSP SPMKTPPAAA VSPMQRHSIS GPISASKPLA
TLTDKRPSYA EIPVQEHLLR TSSTSRPASL PRVPAMESAK SISVSRRSSE EIKRDISAPD
GASPASLMAM GTTSPQLSLS SSPTASVTPT TRSRIREERK DPLSALAREY GGSKRNALLK
WCQKKTEGYQ NIDITNFSSS WNDGLAFCAV LHTYLPAHIP YQELNSQDKR RNFTLAFQAA
ESVGIKSTLD INEMVRTERP DWQNVMLYVT AIYKYFET
