ID   PTPRV_MOUSE             Reviewed;        1705 AA.
AC   P70289;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase V;
DE            Short=R-PTP-V;
DE            EC=3.1.3.48 {ECO:0000269|PubMed:20655470};
DE   AltName: Full=Embryonic stem cell protein-tyrosine phosphatase;
DE            Short=ES cell phosphatase;
DE   Flags: Precursor;
GN   Name=Ptprv; Synonyms=Esp;
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   TISSUE=Embryonic stem cell;
RX   PubMed=8951793; DOI=10.1016/0925-4773(96)00586-2;
RA   Lee K., Nichols J., Smith A.;
RT   "Identification of a developmentally regulated protein tyrosine phosphatase
RT   in embryonic stem cells that is a marker of pluripotential epiblast and
RT   early mesoderm.";
RL   Mech. Dev. 59:153-164(1996).
RN   [2]
RP   ERRATUM OF PUBMED:8951793.
RA   Lee K., Nichols J., Smith A.;
RL   Mech. Dev. 61:213-215(1996).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17693256; DOI=10.1016/j.cell.2007.05.047;
RA   Lee N.K., Sowa H., Hinoi E., Ferron M., Ahn J.D., Confavreux C.,
RA   Dacquin R., Mee P.J., McKee M.D., Jung D.Y., Zhang Z., Kim J.K.,
RA   Mauvais-Jarvis F., Ducy P., Karsenty G.;
RT   "Endocrine regulation of energy metabolism by the skeleton.";
RL   Cell 130:456-469(2007).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=20655470; DOI=10.1016/j.cell.2010.06.003;
RA   Ferron M., Wei J., Yoshizawa T., Del Fattore A., DePinho R.A., Teti A.,
RA   Ducy P., Karsenty G.;
RT   "Insulin signaling in osteoblasts integrates bone remodeling and energy
RT   metabolism.";
RL   Cell 142:296-308(2010).
CC   -!- FUNCTION: Protein tyrosine phosphatase that acts as a regulator of
CC       energy metabolism by mediating dephosphorylation of insulin receptor
CC       (Insr) (PubMed:17693256, PubMed:20655470). Prevents decarboxylation of
CC       osteocalcin (Bglap and Bglap2) via an indirect mechanism:
CC       dephosphorylation of insulin receptor prevents insulin signaling-
CC       dependent decarboxylation of osteocalcin, preventing the hormone
CC       activity of osteocalcin (PubMed:17693256, PubMed:20655470). May play a
CC       role in the maintenance of pluripotency (PubMed:8951793).
CC       {ECO:0000269|PubMed:17693256, ECO:0000269|PubMed:20655470,
CC       ECO:0000269|PubMed:8951793}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044, ECO:0000269|PubMed:20655470};
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- DEVELOPMENTAL STAGE: Detectable in the epiblast of oocytes and
CC       throughout early mouse embryo development (PubMed:8951793). In adult,
CC       expression is localized in gonadal germ cells (PubMed:8951793).
CC       {ECO:0000269|PubMed:8951793}.
CC   -!- INDUCTION: Down-regulated during cell differentiation.
CC       {ECO:0000269|PubMed:8951793}.
CC   -!- DISRUPTION PHENOTYPE: Mice are hypoglycemic and are protected from
CC       obesity and glucose intolerance because of an increase in beta-cell
CC       proliferation, insulin secretion, and insulin sensitivity.
CC       {ECO:0000269|PubMed:17693256}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 3 subfamily. {ECO:0000305}.
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DR   EMBL; U36488; AAC52868.1; -; mRNA.
DR   AlphaFoldDB; P70289; -.
DR   SMR; P70289; -.
DR   GlyCosmos; P70289; 19 sites, No reported glycans.
DR   GlyGen; P70289; 19 sites.
DR   PeptideAtlas; P70289; -.
DR   AGR; MGI:108027; -.
DR   MGI; MGI:108027; Ptprv.
DR   InParanoid; P70289; -.
DR   PRO; PR:P70289; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P70289; Protein.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0044242; P:cellular lipid catabolic process; IMP:MGI.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IMP:MGI.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IGI:MGI.
DR   GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IMP:MGI.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; IMP:MGI.
DR   GO; GO:0031016; P:pancreas development; IMP:MGI.
DR   GO; GO:0044342; P:type B pancreatic cell proliferation; IMP:MGI.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd14618; R-PTPc-V; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR041201; PTPRJ_TM.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF6; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF18861; PTP_tm; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 9.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 8.
DR   PROSITE; PS50853; FN3; 5.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Membrane; Protein phosphatase; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..1705
FT                   /note="Receptor-type tyrosine-protein phosphatase V"
FT                   /id="PRO_0000025466"
FT   TOPO_DOM        19..1077
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1078..1100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1101..1705
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          37..129
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          130..222
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          218..305
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          306..388
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          393..454
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          475..569
FT                   /note="Fibronectin type-III 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          565..654
FT                   /note="Fibronectin type-III 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          655..749
FT                   /note="Fibronectin type-III 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          744..831
FT                   /note="Fibronectin type-III 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          832..926
FT                   /note="Fibronectin type-III 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1150..1409
FT                   /note="Tyrosine-protein phosphatase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   DOMAIN          1427..1695
FT                   /note="Tyrosine-protein phosphatase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          24..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1350
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   BINDING         1316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1350..1356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1394
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        431
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        551
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        570
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        620
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        649
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        663
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        737
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        851
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        882
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        970
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        982
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1705 AA;  186796 MW;  2783755F15387D5B CRC64;
     MRPLILLAAL LWLQDSLAQE DVCSSLDGSP DRQGGGPPLS VSVTSRGRPT SLFLSWVAAE
     PGGFDYALCL RAMNLSGFPE GQQLQAHTNE SSFEFHGLVP GSRYQLELTV LRPCWQNVTI
     TLTARTAPTV VRGLQLHSTG SPASLEASWS DASGDQDSYQ LLLYHPESHT LACNVSVSPD
     TLSYNFGDLL PGSQYVLEVI TWAGSLHAKT SILQWTEPVP PDHLRVRALG TSSLQAFWNS
     SEGATWFHLI LTDLLEGTNL TKVVRQGIST HTFLRLSPGT PYQLKICAAA GPHQIWGPNA
     TEWTYPSYPS DLVLTPLWNE LWASWKAGQG ARDGYVLKLS GPVENTTTLG PEECNAVFPG
     PLPPGHYTLG LRVLAGPYDA WVEGSIWLAE SAARPMEVPG ARLWLEGLEA TKQPGRRALL
     YSVDAPGLLG NISVSSGATH VTFCGLVPGA HYRVDIASSM GDITQSLTGY TSPLPPQSLE
     IISRNSPSDL TIGWAPAPGQ MEGYKVTWHQ DGSQRSPGDL VDLGPDISSL TLKSLVPGSC
     YTVSAWAWSG NLSSDSQKIH SCTRPAPPTN LSLGFAHQPA TLRASWCHPP GGRDAFQLRL
     YRLRPLTLES EKILSQEAQN FSWAQLPAGY EFQVQLSTLW GSEESGSANT TGWTPPSAPT
     LVNVTSEAPT QLHVSWVHAA GDRSSYQVTL YQESTRTATS IVGPKADSTS FWGLTPGTKY
     KVEAISWAGP LYTAAANVSA WTYPLTPNEL LASMQAGSAV VNLAWPSGPL GRGTCHAQLS
     DAGHLSWEQP LSLGQDLLML RNLIPGHTVS LSVKCRAGPL QASTHPLVLS VEPGPVEDVF
     CQPEATYLSL NWTMPTGDVA VCLVEVEQLV PGGSAHFVFQ VNTSEDALLL PNLTPTTSYR
     LSLTVLGGNR QWSRAVTLVC TTSAEVWHPP ELAEAPQVEL GTGMGVTVTR GMFGKDDGQI
     QWYGIIATIN MTLAQPSQEA INHTWYDHYY RGHDSYLALL FPNPFYPEPW AVPRSWTVPV
     GTEDCDNTQE ICNGHLKPGF QYRFSIAAFS RLSSPETILA FSAFSEPQAS ISLVAMPLTV
     MMGTVVGCII IVCAVLCLLC RRGLKGPRSE KNGFSQELMP YNLWRTHRPI PSHSFRQSYE
     AKSARAHQAF FQEFEELKEV GKDQPRLEAE HPANITKNRY PHVLPYDHSR VRLTQLSGEP
     HSDYINANFI PGYSHPQEII ATQGPLKKTV EDFWRLVWEQ QVHVIIMLTV GMENGRVLCE
     HYWPVNSTPV THGHITTHLL AEESEDEWTR REFQLQHGAE QKQRRVKQLQ FTTWPDHSVP
     EAPSSLLAFV ELVQEEVKAT QGKGPILVHC SAGVGRTGTF VALLPAVRQL EEEQVVDVFN
     TVYILRLHRP LMIQTLSQYI FLHSCLLNKI LEGPSDASDS GPIPVMNFAQ ACAKRAANAN
     AGFLKEYRLL KQAIKDETGS LLPSPDYNQN SIASCHHSQE QLALVEESPA DNMLAASLFP
     GGPSGRDHVV LTGSAGPKEL WEMVWEHGAY VLVSLGLPDT KEKPQDIWPM EMQPIVTDMV
     TVHRVAESNT AGWPSTLIRV IHGDSGTERQ VQCLQFPHCE TGSELPANTL LTFLDAVGQC
     CSRGNSKKPG TLLSHSSKVT NQLSTFLAME QLLQQAGTER TVDVFSVALK QTQACAVKTP
     TLEQYIYLYN CLNSALRNRL PRARK
//