PSRC1_BOVIN
ID PSRC1_BOVIN Reviewed; 326 AA.
AC Q29RJ9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Proline/serine-rich coiled-coil protein 1;
GN Name=PSRC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for normal progression through mitosis. Required for
CC normal congress of chromosomes at the metaphase plate, and for normal
CC rate of chromosomal segregation during anaphase. Plays a role in the
CC regulation of mitotic spindle dynamics. Increases the rate of turnover
CC of microtubules on metaphase spindles, and contributes to the
CC generation of normal tension across sister kinetochores. Recruits KIF2A
CC and ANKRD53 to the mitotic spindle and spindle poles. May participate
CC in p53/TP53-regulated growth suppression (By similarity).
CC {ECO:0000250|UniProtKB:Q6PGN9}.
CC -!- SUBUNIT: Interacts with APC2 (By similarity). Interacts with KIF2A (By
CC similarity). Interacts with ANKRD53; recruits ANKRD53 to the spindle
CC during mitosis (By similarity). {ECO:0000250|UniProtKB:Q6PGN9,
CC ECO:0000250|UniProtKB:Q9D0P7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}.
CC Note=Detected at the mitotic spindle and spindle poles. Diffusely
CC distributed throughout the cell during interphase (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PSRC1 family. {ECO:0000305}.
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DR EMBL; BC114140; AAI14141.1; -; mRNA.
DR RefSeq; NP_001039966.1; NM_001046501.1.
DR RefSeq; XP_005204239.1; XM_005204182.3.
DR RefSeq; XP_005204240.1; XM_005204183.2.
DR RefSeq; XP_005204241.1; XM_005204184.3.
DR RefSeq; XP_010801525.1; XM_010803223.1.
DR RefSeq; XP_010801526.1; XM_010803224.2.
DR RefSeq; XP_010801527.1; XM_010803225.2.
DR AlphaFoldDB; Q29RJ9; -.
DR SMR; Q29RJ9; -.
DR STRING; 9913.ENSBTAP00000025034; -.
DR PaxDb; Q29RJ9; -.
DR PRIDE; Q29RJ9; -.
DR Ensembl; ENSBTAT00000025034; ENSBTAP00000025034; ENSBTAG00000018806.
DR Ensembl; ENSBTAT00000086609; ENSBTAP00000068159; ENSBTAG00000018806.
DR GeneID; 541250; -.
DR KEGG; bta:541250; -.
DR CTD; 84722; -.
DR VEuPathDB; HostDB:ENSBTAG00000018806; -.
DR VGNC; VGNC:33484; PSRC1.
DR eggNOG; ENOG502S467; Eukaryota.
DR GeneTree; ENSGT00940000154189; -.
DR HOGENOM; CLU_067830_0_0_1; -.
DR InParanoid; Q29RJ9; -.
DR OrthoDB; 1567239at2759; -.
DR TreeFam; TF338374; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000018806; Expressed in retina and 99 other tissues.
DR ExpressionAtlas; Q29RJ9; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
DR InterPro; IPR026658; DDA3.
DR InterPro; IPR026657; DDA3/GTSE-1.
DR InterPro; IPR032768; GTSE1_N.
DR PANTHER; PTHR21584; PTHR21584; 1.
DR PANTHER; PTHR21584:SF1; PTHR21584:SF1; 1.
DR Pfam; PF15259; GTSE1_N; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Mitosis;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..326
FT /note="Proline/serine-rich coiled-coil protein 1"
FT /id="PRO_0000273727"
FT REPEAT 38..41
FT /note="1"
FT REPEAT 68..71
FT /note="2"
FT REPEAT 213..216
FT /note="3"
FT REPEAT 223..226
FT /note="4"
FT REPEAT 233..236
FT /note="5"
FT REPEAT 301..304
FT /note="6"
FT REGION 38..304
FT /note="6 X 4 AA repeats of P-X-X-P"
FT REGION 39..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..94
FT /evidence="ECO:0000255"
FT COMPBIAS 94..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
SQ SEQUENCE 326 AA; 34326 MW; 382C692B4B389BFE CRC64;
MEDLEEDVKF IADETLDFGG LSPSDSREEE DVAVLVTPEK PLRRGLSHRS DPNAVAPTPQ
GLRLSLGPLS PEKLEEILHE ANRLAAQLEQ CALKERENTG EGSGPRRVKP SPRRETFVLK
DSPVRDLLPT VSSLARSTPS PSSLTPRLRS SDRKGSIRAL RATSGKKPSS VKRESPTCNL
FPASKSPASS PLARSAPPVR GKAGPSGRAT ASPPTPVRPV LAPQPPAGSS QRPSRPQGAA
AKPSSRLPVP SAVPRPGNRM PLASRSVPSS KGAPPSDSLS ARKGLPRPSA AGHRVPVSQR
PNLPISGAGR SNLQPPRKVA VPGSTR
