PSRC1_RAT
ID PSRC1_RAT Reviewed; 329 AA.
AC Q3KR66;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Proline/serine-rich coiled-coil protein 1;
GN Name=Psrc1; Synonyms=Dda3;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC105874; AAI05875.1; -; mRNA.
DR RefSeq; NP_001037767.1; NM_001044302.1.
DR RefSeq; XP_006233238.1; XM_006233176.3.
DR RefSeq; XP_006233239.1; XM_006233177.2.
DR RefSeq; XP_006233240.1; XM_006233178.3.
DR RefSeq; XP_006233241.1; XM_006233179.2.
DR AlphaFoldDB; Q3KR66; -.
DR STRING; 10116.ENSRNOP00000052733; -.
DR PaxDb; Q3KR66; -.
DR Ensembl; ENSRNOT00000055880; ENSRNOP00000052733; ENSRNOG00000020013.
DR GeneID; 691380; -.
DR KEGG; rno:691380; -.
DR UCSC; RGD:1585037; rat.
DR CTD; 84722; -.
DR RGD; 1585037; Psrc1.
DR eggNOG; ENOG502S467; Eukaryota.
DR GeneTree; ENSGT00940000154189; -.
DR HOGENOM; CLU_067830_0_0_1; -.
DR InParanoid; Q3KR66; -.
DR OMA; PCDSREE; -.
DR OrthoDB; 1567239at2759; -.
DR PhylomeDB; Q3KR66; -.
DR TreeFam; TF338374; -.
DR PRO; PR:Q3KR66; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000020013; Expressed in ovary and 18 other tissues.
DR Genevisible; Q3KR66; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0030496; C:midbody; ISO:RGD.
DR GO; GO:0005819; C:spindle; ISO:RGD.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001578; P:microtubule bundle formation; ISO:RGD.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
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..329
FT /note="Proline/serine-rich coiled-coil protein 1"
FT /id="PRO_0000273730"
FT REPEAT 38..41
FT /note="1"
FT REPEAT 68..71
FT /note="2"
FT REPEAT 103..106
FT /note="3"
FT REPEAT 194..197
FT /note="4"
FT REPEAT 212..215
FT /note="5"
FT REGION 68..215
FT /note="5 X 4 AA repeats of P-X-X-P"
FT REGION 94..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..94
FT /evidence="ECO:0000255"
FT COMPBIAS 135..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..304
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 124
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 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
SQ SEQUENCE 329 AA; 34577 MW; BD0B4B971591357E CRC64;
MEDLKEDIKF IVDETLDFGG LSPSDSHEEE DITVLVSPEK PLRRGLSHRS NPNAVAPALQ
GVRFSLGPLS PEKLEEILDE ANRLAAQLEE CALKDSENAA AGPGRPSPRG KPSPRRETFV
LKDSPVRDLL PTVSSWSAPP PSNLTGLRSS DKKGSARAGR VTAGKKPSSI KKESPTCNLF
SASKNPGRSP LAQPTLPPRR KTGSGARTVA SPPIPVRPAP QSSASNSQCS SWLQGAAAKS
SSRLPFPSAI PKPAIRMPLT GRSIPAGKGA LAPDPLPTQK GHPSTVGHRA PVSQRTNLPT
IGAARGRTSS AARGRVQPLR KAAVPGPTR
