PR2C2_MOUSE
ID PR2C2_MOUSE Reviewed; 224 AA.
AC P04095; B7ZNU8; Q498A4; Q61899;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Prolactin-2C2;
DE AltName: Full=Mitogen-regulated protein 1;
DE AltName: Full=Proliferin-1;
DE Flags: Precursor;
GN Name=Prl2c2; Synonyms=Mrp1, Plf, Plf1;
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).
RC STRAIN=BALB/cJ;
RX PubMed=6087314; DOI=10.1073/pnas.81.14.4255;
RA Linzer D.I.H., Nathans D.;
RT "Nucleotide sequence of a growth-related mRNA encoding a member of the
RT prolactin-growth hormone family.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4255-4259(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Ehrlich ascites tumor cell;
RX PubMed=8050594; DOI=10.1016/0014-5793(94)00698-9;
RA Gil-Torregrosa B., Urdiales J.L., Lozano J., Mates J.M.,
RA Sanchez-Jimenez F.;
RT "Expression of different mitogen-regulated protein/proliferin mRNAs in
RT Ehrlich carcinoma cells.";
RL FEBS Lett. 349:343-348(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RC STRAIN=BALB/cJ;
RX PubMed=3478191; DOI=10.1002/j.1460-2075.1987.tb02502.x;
RA Linzer D.I.H., Mordacq J.C.;
RT "Transcriptional regulation of proliferin gene expression in response to
RT serum in transfected mouse cells.";
RL EMBO J. 6:2281-2288(1987).
RN [7]
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 [8]
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04095-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04095-2; Sequence=VSP_043544;
CC -!- TISSUE SPECIFICITY: Expressed in brain and cerebellum
CC (PubMed:16876275). 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, PubMed:10537154). Also
CC expressed in body fluids such as plasma and amniotic fluid
CC (PubMed:10537154). Expressed in embryonic fibroblasts and at low levels
CC in keratinocytes (PubMed:11316781). Isoform 1: Expressed in brain and
CC Neuro-2a cells (PubMed:16876275). Isoform 2: Expressed in brain
CC (PubMed:16876275). {ECO:0000269|PubMed:10537154,
CC ECO:0000269|PubMed:11316781, ECO:0000269|PubMed:16876275}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels during hair follicle
CC morphogenesis, with highest expression levels detected at late anagen
CC stage of the hair follicle cycle (PubMed:11316781). Expressed in
CC developing brain from embryo to adult (PubMed:16876275). In placenta,
CC detected at 8 dpc, peaks at 10 dpc and declines thereafter
CC (PubMed:10537154). {ECO:0000269|PubMed:10537154,
CC ECO:0000269|PubMed:11316781, 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}.
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DR EMBL; K02245; AAA39946.1; -; mRNA.
DR EMBL; X75557; CAA53234.1; -; mRNA.
DR EMBL; CT033774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC080826; AAH80826.1; -; mRNA.
DR EMBL; BC100300; AAI00301.1; -; mRNA.
DR EMBL; BC145439; AAI45440.1; -; mRNA.
DR EMBL; X05786; CAA29230.1; -; Genomic_DNA.
DR EMBL; X05787; CAA29231.1; -; Genomic_DNA.
DR CCDS; CCDS36596.1; -. [P04095-1]
DR PIR; A05086; A05086.
DR RefSeq; NP_112468.1; NM_031191.1. [P04095-1]
DR AlphaFoldDB; P04095; -.
DR SMR; P04095; -.
DR BioGRID; 202244; 3.
DR STRING; 10090.ENSMUSP00000106224; -.
DR GlyGen; P04095; 4 sites.
DR MaxQB; P04095; -.
DR PaxDb; P04095; -.
DR PeptideAtlas; P04095; -.
DR PRIDE; P04095; -.
DR ProteomicsDB; 289822; -. [P04095-1]
DR DNASU; 18811; -.
DR Ensembl; ENSMUST00000110594; ENSMUSP00000106224; ENSMUSG00000079092. [P04095-1]
DR Ensembl; ENSMUST00000221612; ENSMUSP00000152538; ENSMUSG00000079092. [P04095-2]
DR GeneID; 18811; -.
DR KEGG; mmu:18811; -.
DR UCSC; uc007plx.1; mouse. [P04095-1]
DR UCSC; uc011ywi.1; mouse. [P04095-2]
DR CTD; 18811; -.
DR MGI; MGI:97618; Prl2c2.
DR VEuPathDB; HostDB:ENSMUSG00000079092; -.
DR eggNOG; ENOG502QYU3; Eukaryota.
DR GeneTree; ENSGT00950000182818; -.
DR HOGENOM; CLU_088274_0_0_1; -.
DR InParanoid; P04095; -.
DR OMA; CEDETGS; -.
DR PhylomeDB; P04095; -.
DR TreeFam; TF332592; -.
DR BRENDA; 7.6.2.3; 3474.
DR BioGRID-ORCS; 18811; 5 hits in 37 CRISPR screens.
DR ChiTaRS; Prl2c2; mouse.
DR PRO; PR:P04095; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P04095; protein.
DR Bgee; ENSMUSG00000079092; Expressed in placenta and 23 other tissues.
DR ExpressionAtlas; P04095; baseline and differential.
DR Genevisible; P04095; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
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:0043534; P:blood vessel endothelial cell migration; IDA:MGI.
DR GO; GO:0030030; P:cell projection organization; IDA:MGI.
DR GO; GO:0007565; P:female pregnancy; IBA:GO_Central.
DR GO; GO:0030879; P:mammary gland development; IBA:GO_Central.
DR GO; GO:0045445; P:myoblast differentiation; IDA:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IDA:MGI.
DR GO; GO:0007405; P:neuroblast proliferation; IDA:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0031346; P:positive regulation of cell projection organization; IDA:MGI.
DR GO; GO:1903489; P:positive regulation of lactation; IBA:GO_Central.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IDA:MGI.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0032534; P:regulation of microvillus assembly; IDA:MGI.
DR GO; GO:0031667; P:response to nutrient levels; IBA:GO_Central.
DR GO; GO:0002040; P:sprouting angiogenesis; IDA:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
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 Alternative splicing; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..224
FT /note="Prolactin-2C2"
FT /id="PRO_0000032967"
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 VAR_SEQ 70..105
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16876275"
FT /id="VSP_043544"
SQ SEQUENCE 224 AA; 25367 MW; 3786F100C338374B CRC64;
MLPSLIQPCS WILLLLLVNS SLLWKNVASF PMCAMRNGRC FMSFEDTFEL AGSLSHNISI
EVSELFTEFE KHYSNVSGLR DKSPMRCNTS FLPTPENKEQ ARLTHYSALL KSGAMILDAW
ESPLDDLVSE LSTIKNVPDI IISKATDIKK KINAVRNGVN ALMSTMLQNG DEEKKNPAWF
LQSDNEDARI HSLYGMISCL DNDFKKVDIY LNVLKCYMLK IDNC
