ID A0AA88S9X2_TACVA Unreviewed; 1750 AA.
AC A0AA88S9X2;
DT 27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT 27-MAR-2024, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE RecName: Full=Centrosomal protein of 164 kDa {ECO:0000256|ARBA:ARBA00067900};
GN ORFNames=Q7C36_016217 {ECO:0000313|EMBL:KAK2831131.1};
OS Tachysurus vachellii (Darkbarbel catfish) (Pelteobagrus vachellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Bagridae; Tachysurus.
OX NCBI_TaxID=175792 {ECO:0000313|EMBL:KAK2831131.1, ECO:0000313|Proteomes:UP001187315};
RN [1] {ECO:0000313|EMBL:KAK2831131.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PRFRI_2022a {ECO:0000313|EMBL:KAK2831131.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK2831131.1};
RA Liu H.;
RT "Pelteobagrus vachellii genome.";
RL Submitted (AUG-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in microtubule organization and/or maintenance
CC for the formation of primary cilia (PC), a microtubule-based structure
CC that protrudes from the surface of epithelial cells. Plays a critical
CC role in G2/M checkpoint and nuclear divisions. A key player in the DNA
CC damage-activated ATR/ATM signaling cascade since it is required for the
CC proper phosphorylation of H2AX, RPA, CHEK2 and CHEK1. Plays a critical
CC role in chromosome segregation, acting as a mediator required for the
CC maintenance of genomic stability through modulation of MDC1, RPA and
CC CHEK1. {ECO:0000256|ARBA:ARBA00056906}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Interacts (via N-terminus) with ATRIP. Interacts with ATM, ATR
CC and MDC1. Interacts with XPA (via N-terminus) upon UV irradiation.
CC Interacts with CEP83, CCDC92, TTBK2, DVL3, NPHP3 and weakly with NPHP4.
CC Interacts with DZIP1. {ECO:0000256|ARBA:ARBA00061715}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK2831131.1}.
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DR EMBL; JAVHJS010000017; KAK2831131.1; -; Genomic_DNA.
DR Proteomes; UP001187315; Unassembled WGS sequence.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0097539; C:ciliary transition fiber; IEA:UniProtKB-ARBA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IEA:TreeGrafter.
DR GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IEA:TreeGrafter.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:TreeGrafter.
DR CDD; cd00201; WW; 1.
DR FunFam; 3.30.1470.10:FF:000001; Centrosomal protein of 164 kDa; 1.
DR FunFam; 3.30.505.10:FF:000028; Suppressor of cytokine signaling 5; 1.
DR Gene3D; 3.30.1470.10; Photosystem I PsaD, reaction center subunit II; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR022252; SOCS4/SOCS5_dom.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10155; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10155:SF18; SUPPRESSOR OF CYTOKINE SIGNALING 9 ISOFORM X1; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF12610; SOCS; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF158235; SOCS box-like; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50225; SOCS; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cilium biogenesis/degradation {ECO:0000256|ARBA:ARBA00022794};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP001187315};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191};
KW Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 385..480
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 475..524
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
FT DOMAIN 611..644
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1328..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1388..1432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1593..1630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1498..1525
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..45
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..683
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..904
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1593..1625
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1750 AA; 201017 MW; 98B4758EC910A734 CRC64;
MSTEDAGDRG KERERGARPK VRQSRSEERQ DGGRRKGGRG KRKGRLAHEA ISDRPVSDGF
EYGDLLNGLE PRNGSVFRER RWRQVLSSPA SSLTEKVSAR ISQNTPSDDQ SVAETSSKSS
SGSRTLRQKI QDAVGQCFPI KTHSGPSASE QGISESPAPA SSRRKIHLSE LMLDSCPFPP
GSELAQKWNL IKQHTAPISQ PPILDTLSGT GASMSVGTIS AATVVEDEDD RLRERRRISI
EQGVDPPPNA QIHTFEVTAQ INPLYKLGPK LAHGMNELAG DDRATLQQQQ HMLQMQQQHH
QMLLQSCLDT LDEVVASSSG SAPSFSTESH PDSDSSSSSP CSMTRGSLVT AEHFKPQDGH
HRAHTQIDYI HCLVPDLLQI TNLPCYWGVM DRYEAETLLE GKPEGTFLLR DSAQEDYLFS
VSFRRYGRSL HARIEQWNHN FSFDVHDPSV FHAPTVTGLL EHYKDPNSCM FFEPLLSNPI
HRTRPFSLQH VCRAVISSCT TYDGISALPI PNALKEHLKE YHYKQRVRVR RLDTGWEVKS
SHNCGLLTVG QKAVSMSASA LKIGDQLILE EDYDENYIPS EQEIHEYARE IGIDPEREPE
LLWLAREGIV APLPAEWKPC QDVTGDVYYF NFTTGQSTWD HPCDEQYRRL VTQERERSSG
SAHVRNDKEK KKKKEKKEKK KERKKSEPEG PKASGPLGPL APLRSVCDTA VPALRGSLGS
SSGPQLKTPL GGSRMNSGLH RGRQEERPSL APPKRYSDDE EDEEEVQKKI SIPPSLCGTS
RLLQNLHLDL DALGGGLQYE DSEVSRTAPA EEKTEPELQD LALSGEISGN PPSPSQESEI
SEHVEVVSSH SVGMKVRFRS NFSENVLDLS DLCLADPKAA PEEKEKYDRR EAYEDDYEKE
EEEIRGEATK SGHRKSSGLD KWLPDHTQET PSSSSVSKHE DVEGERRMRV DKEEKERKHE
TKDRTKKGQE ESKEVKDRRR HDEELRTRRE EEEKETQRQV EEERLRAVEE RDKKLQLLRD
QMRREEEEEE RRIREENEKR IRALKERLQR EREEEEERLD QETRTKLQQL REHALRDRDT
HLHKLREENE KRASEVRAEL EAERERLEAQ RRRELEKMTE ESEEELKAEK RRLQEKWEEQ
LSSLRAEETT SNRKQDLRSP QPQQQLLDYK RELSEVLQEV RDEVQREHSR KLEQLKEEHR
NQLQTMREMH LEEESNERER VTRALEEERA QLLTSHTAQV EQLRLQLDTQ LYNVRRTHTQ
KEAEVQGLIE KLELKTKELK IQDSRLLAQA ADLEKRRKQL DKDERGLETL PHLLEERERL
LVDLERARQA SDREREERMR EREEMERERK REWEENRNMK DERERLQIKV TLLQEKCDQL
TRRVRELEQR ESADCKEEEK KEQEDVRRNR ESEESLRVED LEPSPSHGTH SNIEELRDFI
SSENVSLQRA RQFLDRHNGN LRDRQTMLKA ARTTLQDPSP GGVAHLLPEN IQQEASRLEE
LKQTVQKGHK LLRKKEERLS QLENSLVEEL SCDDAERTEA ERRVTFDVTD SEASSVYSQD
GAVPVKVQHL ADSLQQISSQ LNMVLGALGS LAPKTSSSTS TSLPRTSSFP PASSWAWPSN
TASSSGAKQN GFTHSSMNGV TALRGSDLLL NSSWRNLLPG VSMDTTFSTR AHTAHSGYMP
TSLSSMMQSK SSELDSLRLR GLIEGNKRWL ETRRKDTNVP LFTRYQVPPS SNGLVQLSLD
ENNQIRVHHY
//
