CYTSA_RAT
ID CYTSA_RAT Reviewed; 1118 AA.
AC Q2KN99;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; AY884296; AAX84187.1; -; mRNA.
DR RefSeq; NP_001034544.1; NM_001039455.1.
DR RefSeq; XP_006256401.1; XM_006256339.3.
DR AlphaFoldDB; Q2KN99; -.
DR SMR; Q2KN99; -.
DR BioGRID; 262991; 1.
DR IntAct; Q2KN99; 1.
DR MINT; Q2KN99; -.
DR STRING; 10116.ENSRNOP00000001764; -.
DR iPTMnet; Q2KN99; -.
DR PhosphoSitePlus; Q2KN99; -.
DR jPOST; Q2KN99; -.
DR PaxDb; Q2KN99; -.
DR PRIDE; Q2KN99; -.
DR Ensembl; ENSRNOT00000001764; ENSRNOP00000001764; ENSRNOG00000001303.
DR GeneID; 361828; -.
DR KEGG; rno:361828; -.
DR UCSC; RGD:1309570; rat.
DR CTD; 23384; -.
DR RGD; 1309570; Specc1l.
DR eggNOG; KOG4678; Eukaryota.
DR GeneTree; ENSGT00940000153592; -.
DR HOGENOM; CLU_009328_1_0_1; -.
DR InParanoid; Q2KN99; -.
DR OMA; FDSASQX; -.
DR OrthoDB; 854083at2759; -.
DR PhylomeDB; Q2KN99; -.
DR PRO; PR:Q2KN99; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000001303; Expressed in lung and 18 other tissues.
DR Genevisible; Q2KN99; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031941; C:filamentous actin; ISO:RGD.
DR GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0034332; P:adherens junction organization; ISO:RGD.
DR GO; GO:0061713; P:anterior neural tube closure; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; ISO:RGD.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISO:RGD.
DR GO; GO:0036032; P:neural crest cell delamination; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
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 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell junction; Coiled coil; Cytoplasm;
KW Cytoskeleton; Gap junction; Phosphoprotein; Reference proteome.
FT CHAIN 1..1118
FT /note="Cytospin-A"
FT /id="PRO_0000231021"
FT DOMAIN 1012..1117
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..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 916..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..281
FT /evidence="ECO:0000255"
FT COILED 395..450
FT /evidence="ECO:0000255"
FT COILED 488..808
FT /evidence="ECO:0000255"
FT COMPBIAS 11..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..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..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KN98"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KN98"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KN98"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YQ0"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YQ0"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1118 AA; 124338 MW; 063B4292C684D817 CRC64;
MKKANRSAGS VPKVSGISKP QTVEKSKSEN SSSAPTGGKP VKPGAAAALS KTKSNDDLLA
GMAGGVNVTN GVKAKKSNCS SAAPSAPAPA MTISESKSKS STGTSSSAKR STSAGNKESS
STRERLRERT RLNQSKKLPS VSQGANDVAL AKRSRSRTAT EGDIRMSKSK SDNQISDKAA
LEAKVKDLLT LAKTKDVEIL HLRNELRDMR AQLGISEDHC EGEDRSEEKE TIIAHQPTDV
ESTLLQLQEQ NTAIREELNQ LKNENRMLKD RLNALGFSLE QRLDNSEKLF GYQSLSPEIT
PGNQSDGGGT LTSSVEGSAP GSVEDLLSQD ENTLMAHQHS NSMDNLDSEC SEVYQPLTSS
DDALDAPSSS ESEGVPSIER SRKGSSGNAS EVSVACLTER IHQMEENQHS TSEELQATLQ
ELADLQQITQ ELNSENERLG EEKVILMESL CQQSDKLEHF GRQIEYFRSL LDEHHISYVI
DEDVKSGRYM ELEQRYMDLA ENARFEREQL LGVQQHLSNT LKMAEQDNKE AQEMIGALKE
RSHHMERIIE SEQKGKAALA ATLEEYKATV ASDQIEMNRL KAQLEKEKQK VAELYSIHNS
GDKSDIQDLL ESVRLDKEKA ETLASSLQED LAHTRNDANR LQDTIAKVED EYRAFQEEAK
KQIEDLNMTL EKLRSELEEK ETERSDMKET IFELEDEVEQ HRAVKLHDNL IISDLENTVK
KLQDQKHDLE RENKTLHRRL REESAEWRQF QADLQTAVVI ANDIKSEAQE EIGDLKRRLH
EAQEKNEKLT KELEEIKSRK QEEERGRVYN YMNAVERDLA ALRQGMGLSR RSSTSSEPTP
TVKTLIKSFD SASQVPNAAA AAIPRTPLSP SPMKTPPAAA VSPMQRHSIS GPVSTSKPLT
ALSDKRSNYG EIPGQEHLLR TSSTSRPASL PRVPAMESAK TISVSRRSSE EMKRDISASE
GASPASLMAM GTTSPQLSLS SSPTASVTPS TRSRIREERK DPLSALAREY GGSKRNALLK
WCQKKTEGYQ NIDITNFSSS WNDGLAFCAL LHTYLPAHIP YQELNSQEKK RNFTLAFQAA
ESVGIKSTLD INEMARTERP DWQNVMLYVT AIYKYFET
