PCP2_MOUSE
ID PCP2_MOUSE Reviewed; 120 AA.
AC P12660; P22941; Q3TV53;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Purkinje cell protein 2;
DE AltName: Full=Protein PCD-5;
DE AltName: Full=Purkinje cell-specific protein L7;
GN Name=Pcp2; Synonyms=Pcp-2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=3199205; DOI=10.1523/jneurosci.08-12-04780.1988;
RA Nordquist D.T., Kozak C.A., Orr H.T.;
RT "cDNA cloning and characterization of three genes uniquely expressed in
RT cerebellum by Purkinje neurons.";
RL J. Neurosci. 8:4780-4789(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Purkinje cell;
RX PubMed=2483097; DOI=10.1016/0896-6273(88)90186-9;
RA Oberdick J., Levinthal F., Levinthal C.;
RT "A Purkinje cell differentiation marker shows a partial DNA sequence
RT homology to the cellular sis/PDGF2 gene.";
RL Neuron 1:367-376(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=2065970; DOI=10.1101/gad.5.7.1136;
RA Vandaele S., Nordquist D.T., Feddersen R.M., Tretjakoff I., Peterson A.C.,
RA Orr H.T.;
RT "Purkinje cell protein-2 regulatory regions and transgene expression in
RT cerebellar compartments.";
RL Genes Dev. 5:1136-1148(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May function as a cell-type specific modulator for G protein-
CC mediated cell signaling.
CC -!- TISSUE SPECIFICITY: Cerebellum (Purkinje cells) and retinal bipolar
CC neurons.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA02989.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB19316.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC25015.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE35767.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=Ref.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M21532; AAA02989.1; ALT_INIT; mRNA.
DR EMBL; S40022; AAB19316.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK003002; BAC25015.1; ALT_INIT; mRNA.
DR EMBL; AK160398; BAE35767.1; ALT_INIT; mRNA.
DR CCDS; CCDS52470.1; -.
DR PIR; A40322; B34955.
DR RefSeq; NP_001123276.1; NM_001129804.1.
DR RefSeq; NP_032816.1; NM_008790.2.
DR RefSeq; XP_006508793.2; XM_006508730.2.
DR AlphaFoldDB; P12660; -.
DR BioGRID; 202055; 11.
DR STRING; 10090.ENSMUSP00000121079; -.
DR iPTMnet; P12660; -.
DR PhosphoSitePlus; P12660; -.
DR PaxDb; P12660; -.
DR PRIDE; P12660; -.
DR ProteomicsDB; 289329; -.
DR Antibodypedia; 57393; 31 antibodies from 13 providers.
DR DNASU; 18545; -.
DR Ensembl; ENSMUST00000133459; ENSMUSP00000122902; ENSMUSG00000004630.
DR GeneID; 18545; -.
DR KEGG; mmu:18545; -.
DR UCSC; uc009ksa.2; mouse.
DR CTD; 126006; -.
DR MGI; MGI:97508; Pcp2.
DR VEuPathDB; HostDB:ENSMUSG00000004630; -.
DR eggNOG; KOG1130; Eukaryota.
DR GeneTree; ENSGT00940000162025; -.
DR HOGENOM; CLU_166511_0_0_1; -.
DR InParanoid; P12660; -.
DR OMA; GHRMDDQ; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 18545; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Pcp2; mouse.
DR PRO; PR:P12660; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P12660; protein.
DR Bgee; ENSMUSG00000004630; Expressed in retinal neural layer and 88 other tissues.
DR ExpressionAtlas; P12660; baseline and differential.
DR Genevisible; P12660; MM.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; IMP:MGI.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR042168; Pcp2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR47503; PTHR47503; 1.
DR Pfam; PF02188; GoLoco; 2.
DR SMART; SM00390; GoLoco; 2.
DR PROSITE; PS50877; GOLOCO; 2.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..120
FT /note="Purkinje cell protein 2"
FT /id="PRO_0000058261"
FT DOMAIN 7..29
FT /note="GoLoco 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT DOMAIN 47..69
FT /note="GoLoco 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT REGION 16..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 120 AA; 13054 MW; D186BF2710DCA03E CRC64;
MAGSPDQEGF FNLLTHVQGD RMEEQRCSLQ AGPGQNPESQ GGPAPEMDNL MDMLVNTQGR
RMDDQRVTVN SLPGFQPIGP KDGMQKRPGT LSPQPLLTPQ DPAALSFRRN SSPQPQTQAP
