PTPRV_RAT
ID PTPRV_RAT Reviewed; 1711 AA.
AC Q64612;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
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 AltName: Full=Osteotesticular protein-tyrosine phosphatase;
DE Short=OST-PTP;
DE Flags: Precursor;
GN Name=Ptprv; Synonyms=Esp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Osteosarcoma;
RX PubMed=7527035; DOI=10.1016/s0021-9258(18)43864-1;
RA Mauro L.J., Olmsted E.A., Skrobacz B.M., Mourey R.J., Davis A.R.,
RA Dixon J.E.;
RT "Identification of a hormonally regulated protein tyrosine phosphatase
RT associated with bone and testicular differentiation.";
RL J. Biol. Chem. 269:30659-30667(1994).
CC -!- FUNCTION: May function in signaling pathways during bone remodeling, as
CC well as serve a broader role in cell interactions associated with
CC differentiation in bone and testis. Associated with differentiation in
CC bone and testis.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.6.;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A presumed alternate transcript of 4.8-5.0 kilobases, which
CC may lack PTP domains, is present in proliferating osteoblasts, but
CC not detectable at other stages.;
CC Name=1;
CC IsoId=Q64612-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q64612-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Bone and testis. In the latter, restricted to the
CC basal portion of the seminiferous tubule.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in differentiating cultures of
CC primary osteoblasts and down-regulated in late stage mineralizing
CC cultures. In testis, expression is highest between stages I and VII
CC when maturing spermatids remain buried within the Sertoli epithelium.
CC -!- INDUCTION: By parathyroid hormone and cAMP analogs.
CC -!- PTM: The cytoplasmic domain contains potential phosphorylation sites.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 3 subfamily. {ECO:0000305}.
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DR EMBL; L36884; AAA63911.1; -; mRNA.
DR PIR; A55148; A55148.
DR RefSeq; NP_149090.1; NM_033099.1. [Q64612-1]
DR AlphaFoldDB; Q64612; -.
DR SMR; Q64612; -.
DR STRING; 10116.ENSRNOP00000007597; -.
DR GlyGen; Q64612; 17 sites.
DR PaxDb; Q64612; -.
DR PRIDE; Q64612; -.
DR GeneID; 64576; -.
DR KEGG; rno:64576; -.
DR UCSC; RGD:621123; rat. [Q64612-1]
DR CTD; 13924; -.
DR RGD; 621123; Ptprv.
DR eggNOG; KOG0791; Eukaryota.
DR InParanoid; Q64612; -.
DR PhylomeDB; Q64612; -.
DR PRO; PR:Q64612; -.
DR Proteomes; UP000002494; Unplaced.
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:0046849; P:bone remodeling; IEP:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 3.
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; 8.
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 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Hydrolase; Membrane;
KW Protein phosphatase; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1711
FT /note="Receptor-type tyrosine-protein phosphatase V"
FT /id="PRO_0000025467"
FT TOPO_DOM 18..1074
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1075..1095
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1096..1711
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..391
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 393..470
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..1696
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
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 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 431
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 1711 AA; 187293 MW; 0F04D2D1A47A18A0 CRC64;
MRPLILLAAL LWLQGFLAED DACSSLEGSP DRQGGGPLLS VNVSSHGKST SLFLSWVAAE
LGGFDYALSL RSVNSSGSPE GQQLQAHTNE SGFEFHGLVP GSRYQLKLTV LRPCWQNVTI
TLTARTAPTV VRGLQLHSAG SPARLEASWS DAPGDQDSYQ LLLYHLESQT LACNVSVSPD
TLSYSFGDLL PGTQYVLEVI TWAGSLHAKT SILQWTEPVP PDHLALRALG TSSLQAFWNS
SEGATSFHLM LTDLLGGTNT TAVIRQGVST HTFLHLSPGT PHELKICASA GPHQIWGPSA
TEWTYPSYPS DLVLTPLRNE LWASWKAGLG ARDGYVLKLS GPMESTSTLG PEECNAVFPG
PLPPGHYTLQ LKVLAGPYDA WVEGSTWLAE SAALPREVPG ARLWLDGLEA SKQPGRRALL
YSDDAPGSLG NISVPSGATH VIFCGLVPGA HYRVDIASST GDISQSISGY TSPLPPQSLE
VISRSSPSDL TIAWGPAPGQ LEGYKVTWHQ DGSQRSPGDL VDLGPDTLSL TLKSLVPGSC
YTVSAWAWAG NLDSDSQKIH SCTRPAPPTN LSLGFAHQPA ALKASWYHPP GGRDAFHLRL
YRLRPLTLES EKVLPREAQN FSWAQLTAGC EFQVQLSTLW GSERSSSANA TGWTPPSAPT
LVNVTSDAPT QLQVSWAHVP GGRSRYQVTL YQESTRTATS IMGPKEDGTS FLGLTPGTKY
KVEVISWAGP LYTAAANVSA WTYPLIPNEL LVSMQAGSAV VNLAWPSGPL GQGACHAQLS
DAGHLSWEQP LKLGQELFML RDLTPGHTIS MSVRCRAGPL QASTHLVVLS VEPGPVEDVL
CHPEATYLAL NWTMPAGDVD VCLVVVERLV PGGGTHFVFQ VNTSGDALLL PNLMPTTSYR
LSLTVLGRNS RWSRAVSLVC STSAEAWHPP ELAEPPQVEL GTGMGVTVMR GMFGKDDGQI
QWYGIIATIN MTLAQPSREA INYTWYDHYY RGCESFLALL FPNPFYPEPW AGPRSWTVPV
GTEDCDNTQE ICNGRLKSGF QYRFSVVAFS RLNTPETILA FSAFSEPRAS ISLAIIPLTV
MLGAVVGSIV IVCAVLCLLR WRCLKGPRSE KDGFSKELMP YNLWRTHRPI PIHSFRQSYE
AKSAHAHQTF FQEFEELKEV GKDQPRLEAE HPDNIIKNRY PHVLPYDHSR VRLTQLPGEP
HSDYINANFI PGYSHTQEII ATQGPLKKTL EDFWRLVWEQ QVHVIIMLTV GMENGRVLCE
HYWPANSTPV THGHITIHLL AEEPEDEWTR REFQLQHGTE QKQRRVKQLQ FTTWPDHSVP
EAPSSLLAFV ELVQEQVQAT QGKGPILVHC SAGVGRTGTF VALLRLLRQL EEEKVADVFN
TVYILRLHRP LMIQTLSQYI FLHSCLLNKI LEGPPDSSDS GPISVMDFAQ ACAKRAANAN
AGFLKEYKLL KQAIKDGTGS LLPPPDYNQN SIVSRRHSQE QFALVEECPE DSMLEASLFP
GGPSGCDHVV LTGSAGPKEL WEMVWEHDAH VLVSLGLPDT KEKPPDIWPV EMQPIVTDMV
TVHRVSESNT TTGWPSTLFR VIHGESGKER QVQCLQFPCS ESGCELPANT LLTFLDAVGQ
CCFRGKSKKP GTLLSHSSKN TNQLGTFLAM EQLLQQAGTE RTVDVFNVAL KQSQACGLMT
PTLEQYIYLY NCLNSALLNG LPRAGKWPAP C
