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PCBP3_MOUSE
ID   PCBP3_MOUSE             Reviewed;         371 AA.
AC   P57722; Q8BSB0; Q8C544;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Poly(rC)-binding protein 3;
DE   AltName: Full=Alpha-CP3;
GN   Name=Pcbp3;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=10936052; DOI=10.1006/geno.2000.6244;
RA   Makeyev A.V., Liebhaber S.A.;
RT   "Identification of two novel mammalian genes establishes a subfamily of KH-
RT   domain RNA-binding proteins.";
RL   Genomics 67:301-316(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Hypothalamus;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
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: Single-stranded nucleic acid binding protein that binds
CC       preferentially to oligo dC. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P57722-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P57722-2; Sequence=VSP_010015;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in testis and
CC       fat tissues and lowest in heart. {ECO:0000269|PubMed:10936052}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC       site. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG09238.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF176327; AAG09238.1; ALT_INIT; mRNA.
DR   EMBL; AK034811; BAC28838.1; -; mRNA.
DR   EMBL; AK079564; BAC37686.1; -; mRNA.
DR   CCDS; CCDS35946.2; -. [P57722-1]
DR   CCDS; CCDS83716.1; -. [P57722-2]
DR   RefSeq; NP_001334145.1; NM_001347216.1. [P57722-2]
DR   RefSeq; NP_067543.2; NM_021568.2. [P57722-1]
DR   RefSeq; XP_017169527.1; XM_017314038.1. [P57722-1]
DR   AlphaFoldDB; P57722; -.
DR   SMR; P57722; -.
DR   BioGRID; 208528; 7.
DR   IntAct; P57722; 1.
DR   STRING; 10090.ENSMUSP00000001148; -.
DR   iPTMnet; P57722; -.
DR   PhosphoSitePlus; P57722; -.
DR   EPD; P57722; -.
DR   jPOST; P57722; -.
DR   MaxQB; P57722; -.
DR   PaxDb; P57722; -.
DR   PeptideAtlas; P57722; -.
DR   PRIDE; P57722; -.
DR   ProteomicsDB; 288265; -. [P57722-1]
DR   ProteomicsDB; 288266; -. [P57722-2]
DR   Antibodypedia; 24497; 86 antibodies from 20 providers.
DR   DNASU; 59093; -.
DR   Ensembl; ENSMUST00000001148; ENSMUSP00000001148; ENSMUSG00000001120. [P57722-1]
DR   Ensembl; ENSMUST00000105411; ENSMUSP00000101051; ENSMUSG00000001120. [P57722-2]
DR   Ensembl; ENSMUST00000168465; ENSMUSP00000129465; ENSMUSG00000001120. [P57722-1]
DR   GeneID; 59093; -.
DR   KEGG; mmu:59093; -.
DR   UCSC; uc007fuz.2; mouse. [P57722-1]
DR   UCSC; uc007fva.2; mouse. [P57722-2]
DR   CTD; 54039; -.
DR   MGI; MGI:1890470; Pcbp3.
DR   VEuPathDB; HostDB:ENSMUSG00000001120; -.
DR   eggNOG; KOG2190; Eukaryota.
DR   GeneTree; ENSGT00940000162185; -.
DR   HOGENOM; CLU_022670_0_1_1; -.
DR   InParanoid; P57722; -.
DR   OMA; ANIHMRC; -.
DR   OrthoDB; 954970at2759; -.
DR   PhylomeDB; P57722; -.
DR   TreeFam; TF318292; -.
DR   BioGRID-ORCS; 59093; 1 hit in 75 CRISPR screens.
DR   ChiTaRS; Pcbp3; mouse.
DR   PRO; PR:P57722; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; P57722; protein.
DR   Bgee; ENSMUSG00000001120; Expressed in retinal neural layer and 257 other tissues.
DR   ExpressionAtlas; P57722; baseline and differential.
DR   Genevisible; P57722; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:1990829; F:C-rich single-stranded DNA binding; IDA:MGI.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:MGI.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0051252; P:regulation of RNA metabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.1370.10; -; 3.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   Pfam; PF00013; KH_1; 3.
DR   SMART; SM00322; KH; 3.
DR   SUPFAM; SSF54791; SSF54791; 3.
DR   PROSITE; PS50084; KH_TYPE_1; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; DNA-binding; Reference proteome; Repeat;
KW   Ribonucleoprotein; RNA-binding.
FT   CHAIN           1..371
FT                   /note="Poly(rC)-binding protein 3"
FT                   /id="PRO_0000050093"
FT   DOMAIN          45..95
FT                   /note="KH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          129..182
FT                   /note="KH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          293..357
FT                   /note="KH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   VAR_SEQ         240
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010015"
FT   CONFLICT        188
FT                   /note="I -> F (in Ref. 1; AAG09238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="S -> C (in Ref. 1; AAG09238)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   371 AA;  39294 MW;  BDBAFEB7EA99DDD7 CRC64;
     MGEGDAIWAP PILPHSTLGT LSHHPELHFG GKMESKVSEG GLNVTLTIRL LMHGKEVGSI
     IGKKGETVKK MREESGARIN ISEGNCPERI VTITGPTDAI FKAFAMIAYK FEEDIINSMS
     NSPATSKPPV TLRLVVPASQ CGSLIGKGGS KIKEIRESTG AQVQVAGDML PNSTERAVTI
     SGTPDAIIQC VKQICVVMLE SPPKGATIPY RPKPASTPVI FAGGQAYTIQ GQYAIPHPDQ
     LTKLHQLAMQ QTPFPPLGQT NPAFPGEKLP LHSSEEAQNL MGQSSGLDAS PPASTHELTI
     PNDLIGCIIG RQGTKINEIR QMSGAQIKIA NATEGSSERQ ITITGTPANI SLAQYLINAR
     LTSEVTGMGA L
 
 
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