CYTSA_XENTR
ID CYTSA_XENTR Reviewed; 1101 AA.
AC Q2KN96;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
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; AY884299; AAX84190.1; -; mRNA.
DR RefSeq; NP_001037875.1; NM_001044410.1.
DR AlphaFoldDB; Q2KN96; -.
DR SMR; Q2KN96; -.
DR STRING; 8364.ENSXETP00000032135; -.
DR PaxDb; Q2KN96; -.
DR GeneID; 733457; -.
DR KEGG; xtr:733457; -.
DR CTD; 23384; -.
DR Xenbase; XB-GENE-5937736; specc1l.
DR eggNOG; KOG4678; Eukaryota.
DR HOGENOM; CLU_009328_1_0_1; -.
DR InParanoid; Q2KN96; -.
DR OrthoDB; 854083at2759; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
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..1101
FT /note="Cytospin-A"
FT /id="PRO_0000231026"
FT DOMAIN 995..1100
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 162..254
FT /evidence="ECO:0000255"
FT COILED 373..427
FT /evidence="ECO:0000255"
FT COILED 492..785
FT /evidence="ECO:0000255"
FT COMPBIAS 14..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 121701 MW; F290C2ADE48B5272 CRC64;
MRKASRSVGA APKVPANNKS QATERSKSES SAPTASKVSR PGSSLSKAKS NDDLLAGMAG
GLPASNSVKV KKNSTTSYPN SGTAMSGQEG RTRSSAGSSS NTKRSGSSGA KEVGSSRERL
RERSRLTANK KPQGLGVGTG EVSAPSKRSR GRTDSDMIRM SKSKSDNQIS DRAALEAKVK
ELMNLAKNKD AEILLLRTEL RDTRSQLGQD VSDKSPDDLP LIHLQEQNTT VCEELQQLKS
ENRMLKDRLN ALGFSLGQQP DDPDKLYGFQ SLGINPGSHS DCGGGTLTSS VEGSAPGSME
DLLSQDESTL TGERRSSSMD NLDSECSEVY QPLTSSDDAL DAPSSSSESE GLPSTERSRK
GSSGNASEVS VACLTERIHQ MEENQHSTAE ELQATLQELA DLQQITQELN SENERLGEEK
VILMDSLCQQ SDKLELFSRQ LEYAQALLDE HHIAYSLDED LKSSRYLDLE QRYMDLAENG
RFEREQLLGV QQHLSNSLKM AEQDNKDAQD VIRALKERNH HMERIAEAEQ LSKQALAATL
EEYKATLNSE QGECARLKAL LEQEKQRVAE LYSIHSSGDA SHIQNLLESV RSDKEKAESL
ASSLQEELLH ARTDVNRMQD AFGKLEDEYR AFREEAQKQV SELTLALEKV RHELEEKETE
LSDMKETIFE LEDEVEQHRA VKLHDNLIIS DVENAVKKLQ DQKHDMEREI KILNRKLREE
SAEWRQFQAD LQTAVVIAND IKSEAQEEIG ELKRQLQEAL EKNEKLAKEM ENATSRKQEE
ERGRVYNYMN AVERDLAALR QGMGLNRRSS TSSDPAPTVK TLIKSFDNAS SQAAAVAAAA
ATPISRTPLS PSPMKTPPAA AVSPMQRHSI SGPISVAKSL PGLSEKRPSY AEIPVQEHML
RSSSSSRSAA SLPRVPAIDN AKSISVSRRS SEELKRDISV PDGSSAPSLM VMTSPSPQLS
LSSSSPTASV TPTARSRIRE ERKDPLAALA REYGGSKRNA LLKWCQKKTE GYPNIDITNF
SSSWNDGLAF CALLHTYLPA HIPYQELTNQ DKRRNFTLAF QAAESVGIKS TLDINEMVRT
ERPDWQCLMT YVTSIYKYFE T
