ID WDR62_PIG Reviewed; 1541 AA.
AC Q8HXL3;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 118.
DE RecName: Full=WD repeat-containing protein 62;
GN Name=WDR62;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11856879; DOI=10.1159/000048814;
RA Droegemueller C., Kuiper H., Voss-Nemitz R., Brenig B., Distl O., Leeb T.;
RT "Molecular characterization and chromosome assignment of the porcine gene
RT COX7A1 coding for the muscle specific cytochrome c oxidase subunit VIIa-
RT M.";
RL Cytogenet. Cell Genet. 94:190-193(2001).
CC -!- FUNCTION: Required for cerebral cortical development. Plays a role in
CC neuronal proliferation and migration (By similarity). Plays a role in
CC mother-centriole-dependent centriole duplication; the function seems
CC also to involve CEP152, CDK5RAP2 and CEP63 through a stepwise assembled
CC complex at the centrosome that recruits CDK2 required for centriole
CC duplication (By similarity). {ECO:0000250|UniProtKB:O43379}.
CC -!- SUBUNIT: Can form homodimers (via C-terminus). Interacts (via C-
CC terminus) with MAPKBP1 (via C-terminus). Interacts with CDK5RAP2,
CC CEP152, CEP63 and KIAA0753. CEP63, CDK5RAP2, CEP152, WDR62 are proposed
CC to form a stepwise assembled complex at the centrosome forming a ring
CC near parental centrioles. {ECO:0000250|UniProtKB:O43379}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43379}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O43379}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:O43379}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:O43379}. Note=Shows cell cycle-dependent
CC localization. Accumulates to the spindle pole during mitosis (By
CC similarity). Colocalizes with CDK5RAP2, CEP152 and WDR62 in a discrete
CC ring around the proximal end of the parental centriole. At this site, a
CC cohesive structure is predicted to engage parental centrioles and
CC procentrioles (By similarity). {ECO:0000250|UniProtKB:O43379}.
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DR EMBL; AJ410870; CAD56046.1; -; Genomic_DNA.
DR RefSeq; NP_001121933.1; NM_001128461.1.
DR AlphaFoldDB; Q8HXL3; -.
DR SMR; Q8HXL3; -.
DR STRING; 9823.ENSSSCP00000003147; -.
DR PaxDb; 9823-ENSSSCP00000003147; -.
DR PeptideAtlas; Q8HXL3; -.
DR Ensembl; ENSSSCT00015041621.1; ENSSSCP00015016445.1; ENSSSCG00015031458.1.
DR Ensembl; ENSSSCT00015041803.1; ENSSSCP00015016497.1; ENSSSCG00015031458.1.
DR Ensembl; ENSSSCT00025082695.1; ENSSSCP00025035922.1; ENSSSCG00025060081.1.
DR Ensembl; ENSSSCT00035043166.1; ENSSSCP00035017267.1; ENSSSCG00035032586.1.
DR Ensembl; ENSSSCT00040102629.1; ENSSSCP00040046405.1; ENSSSCG00040074223.1.
DR Ensembl; ENSSSCT00045041551.1; ENSSSCP00045028833.1; ENSSSCG00045024235.1.
DR Ensembl; ENSSSCT00045041863.1; ENSSSCP00045029063.1; ENSSSCG00045024235.1.
DR Ensembl; ENSSSCT00060093174.1; ENSSSCP00060040297.1; ENSSSCG00060068255.1.
DR GeneID; 100144885; -.
DR KEGG; ssc:100144885; -.
DR CTD; 284403; -.
DR eggNOG; KOG1408; Eukaryota.
DR InParanoid; Q8HXL3; -.
DR OrthoDB; 1220745at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; Unplaced.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0007099; P:centriole replication; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 4.
DR InterPro; IPR024977; Apc4-like_WD40_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR45589; WD REPEAT DOMAIN 62, ISOFORM G; 1.
DR PANTHER; PTHR45589:SF3; WD REPEAT-CONTAINING PROTEIN 62; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 12.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 3: Inferred from homology;
KW Acetylation; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT CHAIN 2..1541
FT /note="WD repeat-containing protein 62"
FT /id="PRO_0000281881"
FT REPEAT 109..150
FT /note="WD 1"
FT REPEAT 153..194
FT /note="WD 2"
FT REPEAT 196..234
FT /note="WD 3"
FT REPEAT 291..330
FT /note="WD 4"
FT REPEAT 357..396
FT /note="WD 5"
FT REPEAT 402..450
FT /note="WD 6"
FT REPEAT 490..529
FT /note="WD 7"
FT REPEAT 532..574
FT /note="WD 8"
FT REPEAT 578..618
FT /note="WD 9"
FT REPEAT 626..665
FT /note="WD 10"
FT REPEAT 671..713
FT /note="WD 11"
FT REPEAT 714..752
FT /note="WD 12"
FT REPEAT 803..846
FT /note="WD 13"
FT REPEAT 1138..1180
FT /note="WD 14"
FT REGION 762..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1185..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1023
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U3T8"
FT MOD_RES 1050
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 1095
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 1125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 1151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 1235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 1255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 1275
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
SQ SEQUENCE 1541 AA; 168899 MW; 81B8882854AF4F1E CRC64;
MAALGTGGYV RNDAVEKLPT IMAGVPARRA QSSPPPAPPL CLRRRTRLTA APEDAVQNRV
SLEKVLGITA QNSSGLTCDP GTGHVAYLAG CVVVILNPKE NKQQHILNTA RKSLSALAFS
PDGKYIVTGE NGHRPAVRIW DVEEKNQVAE MLGHKYGVAC VAFSPNMKHI VSMGYQHDMV
LNVWDWKKDI VVASNKVSCR VIALSFSEDS SYFVTVGNRH VRFWFLEVST EAKVTGTVPL
VGRSGILGEL HDNVFCGVAC GRGQMAGSTF CVSYSGLLCQ FNEKRVLEKW INLKVSLSSC
LCVSQELIFC GCTDGIVRIF QAHSLHYLAN LPKPHYLGVD VAQGLEPSFL FHRKAEAVYP
DTVALTFDPN HQWLSCVYKD HSIYIWDVKD INKVGKMWSE LFHSSYVWNV EVYPEFEDQR
ACLPSGSFLT CSSDNTIRFW NLDSNPDSHW QKNIFSDTLL KVVYVESDIQ HLQDMSHFPD
RGSENGMAVD MKAGVRVMQV SPDGQHLASG DRSGNLRIHE LHFMDELVRV EAHDAEVLCL
EYSKPETGLT LLASASRDRL IHVLNVEKNY SLEQTLDDHS SSITAVKFTG SRDIQMISCG
ADKSIYFRSA QQASDGLHFV RTHHVAEKTT LYDMDIDITQ KYVAVACQDR NVRVYNTVNG
KQKKCYKGSQ GDEGSLLKVH VDPSGTFLAT SCSDKSISVI DFYSGECVAK MFGHSEIITG
MKFTYDCRHL ITVSGDSCVF IWHLGPEITN CMKQHLLEID QREQPQQNTK DGKWSRDPRQ
ETCTSMPSEI SLSPGEQTED ELEEECEPEE LLKTPSKESL DSDPRCLLTN GKLPLWAKRL
LGDDDVADGS AFHAKRSYQP HGRWAERADQ EPLKTILDAR DLDCYFTPMK PESLEDSILD
TVESQRLAGL LSQSESPQED GCRHPSLTPP QRESSEVSEL LCSLESEVTI TGTDSKPCAE
EGEGAPGDQQ DDFYLRVPSI TSKDLNPPED SGESEADLEC SFTAVHSPPR PDPDPPFDVA
VPPAPGCPGA TEELARPEVP GLSNGSLPQT PEQEKFLRHH FETLTDAPAE ELFHGSLRDL
KASEAKDDFF NPRLSISAQF LSRFQKPSRF THTFPTRLPR HPMQSPEVKL TDLAGSQPRA
EPLRAGTGYT SPGRTNVLSA GKAEEPLEAW SPLTSCLTGL APCVSSSSVP PTDKTPPTPT
ALPTPGLAQG VHTPATSSYV EATAGSRAKM SRSISLEDSK GPVLAELARP PCRPSSLGEL
SSLGQELRAI TTTVTPSSDS EGQEPALPSR GNHEARASLK LTLSSICDRL LLPPPQLEPS
AMCVWSQEPV AIQPNVMVTT ASFSAPSPVN VSASRLHNST FLPRFLAPEP LNTSAHPNSP
PLPEARPGVP GNITSLLESA PDALSPVHRC PGHCGQPRVP ARVPPPGPLE LSNVGSIVHR
LQTAFQEALD LYHMMVSRDE VSAEQQQAQT ELASTFLWIH SQLEANDWLV GTDGAPAQAL
PSPGPPSPPT LCPLASPDLH ALLEHYSELL VQAVRRKAQR D
//
