PCM1_XENLA
ID PCM1_XENLA Reviewed; 2031 AA.
AC Q9PVV4; Q66J12;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Pericentriolar material 1 protein;
DE Short=PCM-1;
DE Short=xPCM-1;
GN Name=pcm1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=10579718; DOI=10.1083/jcb.147.5.969;
RA Kubo A., Sasaki H., Yuba-Kubo A., Tsukita S., Shiina N.;
RT "Centriolar satellites: molecular characterization, ATP-dependent movement
RT toward centrioles and possible involvement in ciliogenesis.";
RL J. Cell Biol. 147:969-980(1999).
RN [2]
RP ERRATUM OF PUBMED:10579718.
RA Kubo A., Sasaki H., Yuba-Kubo A., Tsukita S., Shiina N.;
RL J. Cell Biol. 147:1585-1585(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1336.
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND INTERACTION WITH CETN3.
RX PubMed=12403812; DOI=10.1083/jcb.200204023;
RA Dammermann A., Merdes A.;
RT "Assembly of centrosomal proteins and microtubule organization depends on
RT PCM-1.";
RL J. Cell Biol. 159:255-266(2002).
RN [5]
RP SELF-ASSOCIATION, AND SUBCELLULAR LOCATION.
RX PubMed=12571289; DOI=10.1242/jcs.00282;
RA Kubo A., Tsukita S.;
RT "Non-membranous granular organelle consisting of PCM-1: subcellular
RT distribution and cell-cycle-dependent assembly/disassembly.";
RL J. Cell Sci. 116:919-928(2003).
CC -!- FUNCTION: Required to anchor microtubules to the centrosome (By
CC similarity). Required for centrosome assembly and function. Essential
CC for the correct localization of several centrosomal proteins including
CC cetn3 and pcnt (PubMed:12403812). Probably involved in the biogenesis
CC of cilia (By similarity). {ECO:0000250|UniProtKB:Q15154,
CC ECO:0000250|UniProtKB:Q9R0L6, ECO:0000269|PubMed:12403812}.
CC -!- SUBUNIT: Self-associates. Interacts with cetn3.
CC {ECO:0000269|PubMed:12403812}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8AV28}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q15154}.
CC Cytoplasmic granule {ECO:0000250|UniProtKB:Q15154}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriolar
CC satellite {ECO:0000250|UniProtKB:Q15154}. Cytoplasm, cytoskeleton,
CC cilium basal body {ECO:0000250|UniProtKB:Q15154}. Note=Recruitment to
CC the centrosome may require cytoplasmic dynein. The majority of the
CC protein dissociates from the centrosome during metaphase. Also
CC associates with microtubules.
CC -!- SIMILARITY: Belongs to the PCM1 family. {ECO:0000305}.
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DR EMBL; AB025414; BAA87862.1; -; mRNA.
DR EMBL; BC081112; AAH81112.1; -; mRNA.
DR RefSeq; NP_001081369.1; NM_001087900.2.
DR AlphaFoldDB; Q9PVV4; -.
DR SMR; Q9PVV4; -.
DR BioGRID; 99137; 1.
DR IntAct; Q9PVV4; 1.
DR PRIDE; Q9PVV4; -.
DR GeneID; 397798; -.
DR KEGG; xla:397798; -.
DR CTD; 397798; -.
DR Xenbase; XB-GENE-958594; pcm1.L.
DR OrthoDB; 500021at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 397798; Expressed in egg cell and 19 other tissues.
DR GO; GO:0034451; C:centriolar satellite; IDA:BHF-UCL.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; ISS:UniProtKB.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IEA:InterPro.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IEA:InterPro.
DR InterPro; IPR031446; PCM1_C.
DR InterPro; IPR024138; Pericentriolar_Pcm1.
DR PANTHER; PTHR14164; PTHR14164; 1.
DR Pfam; PF15717; PCM1_C; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Reference proteome.
FT CHAIN 1..2031
FT /note="Pericentriolar material 1 protein"
FT /id="PRO_0000274040"
FT REGION 1..484
FT /note="Self-association"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..1271
FT /note="Self-association and localization to centrosomes"
FT REGION 806..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1219..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1514..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1817..1870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1922..1965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2007..2031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 302..394
FT /evidence="ECO:0000255"
FT COILED 523..549
FT /evidence="ECO:0000255"
FT COILED 684..711
FT /evidence="ECO:0000255"
FT COILED 757..805
FT /evidence="ECO:0000255"
FT COILED 858..892
FT /evidence="ECO:0000255"
FT COILED 1025..1049
FT /evidence="ECO:0000255"
FT COILED 1550..1599
FT /evidence="ECO:0000255"
FT COMPBIAS 20..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..578
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..961
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1344
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1922..1960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 832
FT /note="V -> I (in Ref. 3; AAH81112)"
FT /evidence="ECO:0000305"
FT CONFLICT 1334
FT /note="N -> K (in Ref. 3; AAH81112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2031 AA; 227868 MW; BB4D72AB3DB194AC CRC64;
MATGGGPPDE ALSDQDLPNW SHESLDDRLN NMHWNGQKKG NRSAEKNKKK FVECDLRLTN
DISPESSPGV GRRRARTPHT FPHTRYVSQM SVPEQAELEK LKQKINFSDL DQRSIGSDSQ
GRATAANNKR QLADNRKPFN FLPSQLNTNK EKSKSPPKRE ASTRSLTKDF LASALNKDFL
SNSQAFLEEE SKREPAIDSS QVVSRLVQIR DYITKASSLR DDLVQKKDLS VNVERLSNLI
EHLKFQEKSY LKFLQKMLAS ENEEEDVRTV DSAVGSGSVV ESTLLTFDVP SEASDTTGVD
PRQEAKEELK NMKKQHALLT RMLQQQEQLR TLKGRQAALL ALQHKAEQAI AKMDESVVTE
TTGSVSGLSL TSELNEELND LIQRFHNQLH DSEDPPAPDN RRQAESLSLA REVYRSRNSS
TSDTPLEDKS PLFNNVGVLL EKKQKMDTLL GELHTLQDQQ LNNTAFVASS VSPRRSTEQR
TLGSAVSSAL TSDNRAARSP VTIGAYQTAS VNESEDEENQ NPAEKLKKLK EVRKRLNELR
ELVHYYEQTS DMMTDAMNEN TKDEDETEDS EYDSEQEDAE PTTNIRNPQY RSSWAQMNIN
SNNQSGTNNR DERQLNTECE INNRSAVNLR SFNMPSALDC LYNIEHSDKE EDGNRELDDE
DAEDQGSRAS LSSQNSVADD VQSVDFEQKF NRLVAAKQKL KQLQDLVAMY GDDSESEPVA
PERSFSGDQF PPEATTLKQQ PNNTRPNVSK AQKDIALKEQ AREKFYESKL QQQQRELSQL
QEERKKLIEI QEKIQTLRKA CPDLQLSTSS AGTNPANRQN RQMTTTTSTP DVNTNGNIVV
PAMPDPEDSS SVDNEVWSEI RKHQILREDL RQRRKQLETL MAEHQRRQGN TETTSAASIR
SDDSDTQGLQ QQTRTEKTMA TWGGSTQCAL EEEEEEEEVD DEECLSDVHQ IDIEEDEQDN
TSCENNSYPQ NSIRKTSFNG RSSKDGWKNQ CPLSVEGNHR PSPKTRQQQN VSMRRQENYR
WMSELSHVEE KEHWQEQIDQ IKKQLDYSTS ICQTLMRDQQ ALSYLLQSMI TTPYSVMPSN
VGASQVQLIM HQLNQCYTQL NWQQSNVLRL KQMLNDLLVQ QPQHLQGESH QREDRGSSAP
PLTSPNIFPN FSFLPPTMNL LNMPAFGSIP NVVPGMNFNP VFPHGFENFT QNVASHTDTP
LQPHDQNTSG KTEYMAFPKP FESHRSNSTE KERNPPKKPD ESEQGRRVWV ENHQKSDQEK
KPACFGAGLS AGGASAKLAE ESRKVKQFDE VSVESLSSMP DPVDPTTVTK MFKSRKASAQ
ASLASKDKTP KAKNKKRKVF HQKSKGIKSC GFQAASASSA SEPNQTTCKH AQTEEVVVGN
VIKTSSAQRV EKESKATEMS SEAGSDVSMF ETLRDTIYSE VATLISQNES RPHFLIELFH
ELQLLNTDYL RQKALFALQD IVTRHVSEGN AKKHETCTKA LESTGWMAST SELTPSESLV
TTDDEMYAKN SDGPVCQEGE QNDGDNISSL STSSNFEPFA TDDLGNTVIH FDQALARMRE
YERMKSETEN GLVADCCNNL NAAASSLEGT NDEARGRAQH SVDDASGIPC PYIDSKQLDR
QIKAIMKEVI PFLKEHMEEV CSPNLLTSIR RLVLTLTQQN DESKEFVKFF HKQLGSILQD
SLAKFSSKKL KDCGEDLLVE ISEVLFNELA FFRLMQDLDN NSTAVQGTVS RKPEAVVVLE
SFTKEADKEE KTCPEENFSA TRETDDEDKD KDETETAEEN RNFDAEVLSG KSDISEEDDL
DESLPVSISF TKAETQALTN YGSGEDENED EENYEFEARP VDVQTSLETS SEIADETEKE
EMEVRPEANI ENEKALSLAV NVMGELSIHE DQAKSDCDVL AHPSLLLSNE KATDFSGTAL
VNNVKSPVDS PGTSGAGSSD TESPVLVNDF ETGSGNLSQK SDEDDFVKVE DLPLKLSLPQ
EQIMKDIEEE ENKNNLCDEI LNINDEENGA DQLAGDPLAL KEPDSPAIHP A
