PTPRV_MOUSE
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 03-AUG-2022, entry version 137.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase V;
DE Short=R-PTP-V;
DE EC=3.1.3.48;
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).
CC -!- FUNCTION: May play a role in the maintenance of pluripotency. Down-
CC regulated during differentiation.
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};
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. In adult, expression is
CC localized in gonadal germ cells.
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 GlyGen; P70289; 19 sites.
DR PeptideAtlas; P70289; -.
DR PRIDE; P70289; -.
DR MGI; MGI:108027; Ptprv.
DR InParanoid; P70289; -.
DR PRO; PR:P70289; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P70289; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
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: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:0018214; P:protein carboxylation; IMP:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; IMP:MGI.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 5.
DR Gene3D; 3.90.190.10; -; 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 Pfam; PF00041; fn3; 2.
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; SSF49265; SSF49265; 8.
DR SUPFAM; SSF52799; SSF52799; 2.
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 2: Evidence at transcript 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
