PCM1_CHICK
ID PCM1_CHICK Reviewed; 1904 AA.
AC Q8AV28;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Pericentriolar material 1 protein;
DE Short=PCM-1;
GN Name=PCM1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Required for centrosome assembly and function
CC (PubMed:12403812). Essential for the correct localization of several
CC centrosomal proteins including CETN3 and PCNT (By similarity). Required
CC to anchor microtubules to the centrosome (PubMed:12403812). Probably
CC involved in the biogenesis of cilia (By similarity).
CC {ECO:0000250|UniProtKB:Q15154, ECO:0000250|UniProtKB:Q9R0L6,
CC ECO:0000269|PubMed:12403812}.
CC -!- SUBUNIT: Self-associates. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12403812}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:12403812}.
CC Cytoplasmic granule {ECO:0000269|PubMed:12403812}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriolar
CC satellite {ECO:0000269|PubMed:12403812}. Cytoplasm, cytoskeleton,
CC cilium basal body {ECO:0000250|UniProtKB:Q15154}. Note=The majority of
CC the protein dissociates from the centrosome during metaphase and
CC subsequently localizes to the cleavage site in telophase.
CC -!- SIMILARITY: Belongs to the PCM1 family. {ECO:0000305}.
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DR EMBL; AJ508717; CAD48486.1; -; mRNA.
DR RefSeq; NP_989862.1; NM_204531.1.
DR AlphaFoldDB; Q8AV28; -.
DR SMR; Q8AV28; -.
DR STRING; 9031.ENSGALP00000031473; -.
DR Ensembl; ENSGALT00000022129; ENSGALP00000022090; ENSGALG00000013602.
DR GeneID; 395204; -.
DR KEGG; gga:395204; -.
DR CTD; 5108; -.
DR VEuPathDB; HostDB:geneid_395204; -.
DR eggNOG; ENOG502QRMF; Eukaryota.
DR GeneTree; ENSGT00390000006641; -.
DR InParanoid; Q8AV28; -.
DR OrthoDB; 500021at2759; -.
DR PhylomeDB; Q8AV28; -.
DR Reactome; R-GGA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-GGA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-GGA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-GGA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-GGA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-GGA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-GGA-8854518; AURKA Activation by TPX2.
DR PRO; PR:Q8AV28; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000013602; Expressed in spermatid and 12 other tissues.
DR ExpressionAtlas; Q8AV28; baseline and differential.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IBA:GO_Central.
DR InterPro; IPR031446; PCM1_C.
DR InterPro; IPR024138; Pericentriolar_Pcm1.
DR PANTHER; PTHR14164; PTHR14164; 2.
DR Pfam; PF15717; PCM1_C; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Reference proteome.
FT CHAIN 1..1904
FT /note="Pericentriolar material 1 protein"
FT /id="PRO_0000274039"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1616..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1774..1838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1865..1904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 171..212
FT /evidence="ECO:0000255"
FT COILED 301..334
FT /evidence="ECO:0000255"
FT COILED 403..429
FT /evidence="ECO:0000255"
FT COILED 562..592
FT /evidence="ECO:0000255"
FT COILED 636..686
FT /evidence="ECO:0000255"
FT COILED 731..768
FT /evidence="ECO:0000255"
FT COILED 895..927
FT /evidence="ECO:0000255"
FT COILED 970..1000
FT /evidence="ECO:0000255"
FT COILED 1421..1447
FT /evidence="ECO:0000255"
FT COMPBIAS 15..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..832
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1664..1679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1694
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1698..1741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1904 AA; 212725 MW; CA1A4C63698BBA0C CRC64;
MATGGGPFEE GMNDQDLPSW SNESLDDRLN NTDWGCQQKK ANRSSEKNKK KLGGEAETRL
TNDISPESSP GMGRRKTRTP HSFPHARYMT QMSVPEQAEL ERLKQRINFS DLDQINTNKS
KDPVSGSQKK ESGEPLQCKE LFGAALNKDF LQNGQLSIQE DGRGEPTMDS SQARDPQQEA
KEELENLKKQ HDLLKRMLQQ QEQLKALQGR QAALLALQHK AEQAVAVVDD SVVTETTGSV
SGVSLTSELN EELIDLIQRF HNQLHDSQTQ SVPDNRRQAE SLSLTREISQ SRNSSVSEHQ
SDEKAQLFNK MRMLQGKKQK MDKLLGELHT LRDQHLNNSS FFPASSSPQR SIDQRSTTSA
ASAPVGVVTV INGESNSLAS APYPPDSLAS QNESEEDDNL NPTEKLQKLN EVRKRLNELR
ELVHYYEQTS DMMTDAVNEN TKEEEETEDS GSDSEHGDPQ PVTNIRNPQG ISSWSEINSN
SNVQCGTNNR DGRHLNTDCE INNRSAANIR TLKMSSTLDC HNREDDKHAD LPHGEDDEVE
EDRASEDSMS SHRSSLGDVA GDAEFEQKIN RLMAAKQKLR QLQNLAAMVQ DDDPEPQVLT
ANASNMGDFL GEMEETKQQP NNVRVSTNKL QKDAGLNEKA REKFYEAKLQ QQQRELKQLQ
EERRKLMEIQ EKIEVLQKAC PDLQSAGLGN SPANRQTSPA TSTPAMNECN TAGKPLLEFG
ESVPVGNELW SEMRRHEILR EELRRRRKQL EALMAEHQRR RELAETISTV AASVKSEGSE
AQRTPQQSRT ENRTMATWGG STQCALDEED GDEDGYLSDG LDQAEEEEDA PSMNDSFSAY
PNNQIPESVY YLKGNKDRWK NCRPLSADGN YRPMSKTRQQ QNISMRRQEN FRWISELSYV
EEKEQWQEQI NQLKKQLEFS VSICQTLMQD QQTLSCFLQT LLAGPYNVVP NNVASSQVHL
IMHQLNQCYT QLSWQQNNVQ RLKQMLNDLM HQQEQQCQEK PSRKERGSSA PPPPSPVFCP
FSFPPQPVNL FNIPGFTNIS SFAPGINYNP VFPCGFGDFA HSGFPQSSEQ QQHPLDHNAS
GKTEYMAFPK PFESSSSTGA ENQRSHRQPE DEVEKRSTWL NDSQEVKKDD QSQQKAGFPV
SVQSIASGHK NQSDTSRRRN FDEESLESFS SMPDPVDPTT VTKTFKSRKA SAQASLASKD
KTPKSKNKRK NSSQLKGRIK NTGYDSASAS SVCEPCKSTK SKHSEEVVHA KVFSKKNREQ
LEKIIKYSRS TEMSSETGSD LSMFEALRDT IYSEVATLIS QNESRPHFLI ELFHELQLLN
TDYLRQRALY ALQDIVTRHL SENNEKGRCI KSLNTATWIA SNSELTPSES LASTDDETFD
KNFPTEACQD CEQNDADNGS TMSTSSHFEP FATDDLGNTV IHLDQALARM REYERMKIEA
ESTLDSEGCS SNLQGATAAK LEGPSTSECL SVPQSSEVSA VPCPRIDTQQ LDRQIKAIMK
EVIPFLKEHM DEVCSSQLLT SVRRMVLTLT QQNDESKEFV KFFHKQLGSI LQDSLAKFAG
RKLKDCGEDL LVEISEVLFN ELAFFKLMQD LDNNSISVKQ RCKRKIETTE EIQSYAKEDK
DETETVKPVQ GLETYDGNEV PESIKSDASD QEEDEESESG PVAISLSKAE TQALTNYGSG
EDENEDEEIE FEEGPVDVQT SLQASSETAT ENEQISSQEL SKTKGSDILS SEQQSVNVKG
EQDAATILPH YLNVVENTPP LPVNTPESFI AASMKTEESS SSLPGNETQM LDTACVVNKS
SAGSSESSMA GSPDTESPVL VNEYEAGSGN VSQKSDEDDF VKVEDLPLKL AVYSEADLLK
KIASEAQTNS LSDELLGGGG EQDRELVGDA QTLKEPETFG AQSA
