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PR2C3_MOUSE
ID   PR2C3_MOUSE             Reviewed;         224 AA.
AC   P04768; P18918; Q498A5; Q6PDB6;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 2.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Prolactin-2C3;
DE   AltName: Full=Mitogen-regulated protein 2;
DE   AltName: Full=Mitogen-regulated protein 3;
DE   AltName: Full=Prolactin-2C4;
DE   AltName: Full=Proliferin-2;
DE   AltName: Full=Proliferin-3;
DE   Flags: Precursor;
GN   Name=Prl2c3; Synonyms=Mrp2, Mrp3, Mrpplf3, Plf2, Plf3, Prl2c4;
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], TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC   STRAIN=BALB/cJ; TISSUE=Placenta;
RX   PubMed=3859868; DOI=10.1073/pnas.82.13.4356;
RA   Linzer D.I.H., Lee S.-J., Ogren L., Talamantes F., Nathans D.;
RT   "Identification of proliferin mRNA and protein in mouse placenta.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:4356-4359(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CD-1; TISSUE=Embryonic fibroblast;
RX   PubMed=2790033; DOI=10.1016/0167-4781(89)90081-x;
RA   Connor A.M., Waterhouse P., Khokha R., Denhardt D.T.;
RT   "Characterization of a mouse mitogen-regulated protein/proliferin gene and
RT   its promoter: a member of the growth hormone/prolactin gene superfamily.";
RL   Biochim. Biophys. Acta 1009:75-82(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Placenta;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg, and Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-224.
RC   STRAIN=C57BL/6J;
RX   PubMed=8043949; DOI=10.1007/bf00356553;
RA   Ko M.S., Wang X., Horton J.H., Hagen M.D., Takahashi N., Maezaki Y.,
RA   Nadeau J.H.;
RT   "Genetic mapping of 40 cDNA clones on the mouse genome by PCR.";
RL   Mamm. Genome 5:349-355(1994).
RN   [6]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   GLYCOSYLATION.
RX   PubMed=10537154; DOI=10.1210/endo.140.11.7142;
RA   Fang Y., Lepont P., Fassett J.T., Ford S.P., Mubaidin A., Hamilton R.T.,
RA   Nilsen-Hamilton M.;
RT   "Signaling between the placenta and the uterus involving the mitogen-
RT   regulated protein/proliferins.";
RL   Endocrinology 140:5239-5249(1999).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11316781; DOI=10.1210/endo.142.5.8132;
RA   Fassett J.T., Nilsen-Hamilton M.;
RT   "Mrp3, a mitogen-regulated protein/proliferin gene expressed in wound
RT   healing and in hair follicles.";
RL   Endocrinology 142:2129-2137(2001).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=16876275; DOI=10.1016/j.neures.2006.05.011;
RA   Wang J.W., Jiang Y.N., Huang C.Y., Huang P.Y., Huang M.C., Cheng W.T.,
RA   Shen C.K., Ju Y.T.;
RT   "Proliferin enhances microvilli formation and cell growth of neuroblastoma
RT   cells.";
RL   Neurosci. Res. 56:80-90(2006).
CC   -!- FUNCTION: May have a role in embryonic development. It is likely to
CC       provide a growth stimulus to target cells in maternal and fetal tissues
CC       during the development of the embryo at mid-gestation. May play a role
CC       during wound healing and in the hair follicle cycle as a growth factor
CC       and/or an angiogenesis factor. May play a role in microvilli formation
CC       and cell proliferation of neuroblastoma cells.
CC       {ECO:0000269|PubMed:11316781, ECO:0000269|PubMed:16876275}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10537154,
CC       ECO:0000269|PubMed:16876275}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:16876275}.
CC   -!- TISSUE SPECIFICITY: Expressed in placenta and hair follicles, with
CC       highest expression levels detected in the outer root sheath and no
CC       expression detected in bulb (PubMed:11316781). Expressed in placenta,
CC       skin wounds, keratinocytes and weakly in embryonic fibroblasts
CC       (PubMed:10537154, PubMed:11316781, PubMed:16876275). Expressed in
CC       brain, cerebellum and in Neuro-2a cell line (PubMed:16876275). Not
CC       detected in liver, kidney, ovary, pituitary gland and brain
CC       (PubMed:3859868). {ECO:0000269|PubMed:10537154,
CC       ECO:0000269|PubMed:11316781, ECO:0000269|PubMed:16876275,
CC       ECO:0000269|PubMed:3859868}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during hair follicle morphogenesis, with
CC       highest expression levels detected at late anagen stage of the hair
CC       follicle cycle (PubMed:11316781). Expressed in developing brain from
CC       embryo to adult (PubMed:16876275). In placenta, detected at 8 dpc,
CC       peaks at 10 dpc and declines thereafter (PubMed:10537154).
CC       {ECO:0000269|PubMed:10537154, ECO:0000269|PubMed:11316781,
CC       ECO:0000269|PubMed:16876275}.
CC   -!- PTM: N-glycosylated and sialylated. {ECO:0000269|PubMed:10537154}.
CC   -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Prl2c3 and Prl2c4 have previously been regarded as different
CC       proteins, but they seem to be products of the same gene. {ECO:0000305}.
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DR   EMBL; K03235; AAA39945.1; -; mRNA.
DR   EMBL; X16009; CAA34146.1; -; Genomic_DNA.
DR   EMBL; X16010; CAA34146.1; JOINED; Genomic_DNA.
DR   EMBL; X16011; CAA34146.1; JOINED; Genomic_DNA.
DR   EMBL; X16012; CAA34146.1; JOINED; Genomic_DNA.
DR   EMBL; X16013; CAA34146.1; JOINED; Genomic_DNA.
DR   EMBL; AK145995; BAE26816.1; -; mRNA.
DR   EMBL; AK164068; BAE37612.1; -; mRNA.
DR   EMBL; BC058816; AAH58816.1; -; mRNA.
DR   EMBL; BC064772; AAH64772.1; -; mRNA.
DR   EMBL; BC100299; AAI00300.1; -; mRNA.
DR   EMBL; BC132078; AAI32079.1; -; mRNA.
DR   EMBL; BC132080; AAI32081.1; -; mRNA.
DR   EMBL; U05747; AAB60482.1; -; Genomic_DNA.
DR   CCDS; CCDS36595.1; -.
DR   PIR; A23159; A23159.
DR   PIR; S05648; S05648.
DR   RefSeq; NP_035248.2; NM_011118.2.
DR   RefSeq; NP_036084.2; NM_011954.2.
DR   AlphaFoldDB; P04768; -.
DR   SMR; P04768; -.
DR   STRING; 10090.ENSMUSP00000097393; -.
DR   GlyGen; P04768; 4 sites.
DR   PaxDb; P04768; -.
DR   PRIDE; P04768; -.
DR   ProteomicsDB; 291808; -.
DR   DNASU; 18812; -.
DR   DNASU; 26421; -.
DR   Ensembl; ENSMUST00000099805; ENSMUSP00000097393; ENSMUSG00000056457.
DR   GeneID; 18812; -.
DR   GeneID; 26421; -.
DR   KEGG; mmu:18812; -.
DR   KEGG; mmu:26421; -.
DR   UCSC; uc007plw.3; mouse.
DR   CTD; 18812; -.
DR   CTD; 26421; -.
DR   MGI; MGI:1341833; Prl2c3.
DR   VEuPathDB; HostDB:ENSMUSG00000056457; -.
DR   eggNOG; ENOG502QYU3; Eukaryota.
DR   GeneTree; ENSGT00950000182818; -.
DR   HOGENOM; CLU_088274_0_0_1; -.
DR   InParanoid; P04768; -.
DR   OMA; MISCHTS; -.
DR   OrthoDB; 1290070at2759; -.
DR   PhylomeDB; P04768; -.
DR   TreeFam; TF332592; -.
DR   BioGRID-ORCS; 18812; 9 hits in 40 CRISPR screens.
DR   BioGRID-ORCS; 26421; 5 hits in 16 CRISPR screens.
DR   ChiTaRS; Prl2c3; mouse.
DR   PRO; PR:P04768; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; P04768; protein.
DR   Bgee; ENSMUSG00000056457; Expressed in placenta and 30 other tissues.
DR   ExpressionAtlas; P04768; baseline and differential.
DR   Genevisible; P04768; MM.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0008083; F:growth factor activity; IDA:MGI.
DR   GO; GO:0005179; F:hormone activity; IDA:MGI.
DR   GO; GO:0005148; F:prolactin receptor binding; IBA:GO_Central.
DR   GO; GO:0007565; P:female pregnancy; IBA:GO_Central.
DR   GO; GO:0071425; P:hematopoietic stem cell proliferation; IDA:MGI.
DR   GO; GO:0030879; P:mammary gland development; IBA:GO_Central.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IDA:MGI.
DR   GO; GO:1903489; P:positive regulation of lactation; IBA:GO_Central.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:0031667; P:response to nutrient levels; IBA:GO_Central.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR001400; Somatotropin/Prolactin.
DR   InterPro; IPR018116; Somatotropin_CS.
DR   PANTHER; PTHR11417; PTHR11417; 1.
DR   Pfam; PF00103; Hormone_1; 1.
DR   PRINTS; PR00836; SOMATOTROPIN.
DR   SUPFAM; SSF47266; SSF47266; 1.
DR   PROSITE; PS00266; SOMATOTROPIN_1; 1.
DR   PROSITE; PS00338; SOMATOTROPIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..224
FT                   /note="Prolactin-2C3"
FT                   /id="PRO_0000032968"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..40
FT                   /evidence="ECO:0000250"
FT   DISULFID        87..199
FT                   /evidence="ECO:0000250"
FT   DISULFID        216..224
FT                   /evidence="ECO:0000250"
FT   CONFLICT        81
FT                   /note="D -> G (in Ref. 4; AAH58816)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="L -> S (in Ref. 1; AAA39945)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="D -> N (in Ref. 4; AAH58816)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   224 AA;  25338 MW;  C87F3A2310C91320 CRC64;
     MLPSSIQPCS WILLLLLVNS SLLWKNVASF PMCAMRNGRC FMSFEDTFEL AGSLSHNISI
     EVSELFNEFE KHYSNVSGLR DKSPMRCNTS FLPTPENKEQ ARLTHYAALL KSGAMILDAW
     ESPLDDLVSE LSTIKNVPDI IISKATDIKK KINAVRNGVN ALMSTMLQNG DEEKKNPAWF
     LQSDNEDARI HSLYGMISCL DNDFKKVDIY LNVLKCYMLK IDNC
 
 
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