ID A0A0G2JT62_RAT Unreviewed; 1907 AA.
AC A0A0G2JT62;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase F {ECO:0000256|ARBA:ARBA00044158};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=Ptprf {ECO:0000313|Ensembl:ENSRNOP00000068583.2,
GN ECO:0000313|RGD:3453};
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 {ECO:0000313|Ensembl:ENSRNOP00000068583.2, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000068583.2, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068583.2,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000068583.2}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068583.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001490};
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000256|ARBA:ARBA00010504}.
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DR RefSeq; XP_017448943.1; XM_017593454.1.
DR jPOST; A0A0G2JT62; -.
DR Ensembl; ENSRNOT00000078302.2; ENSRNOP00000068583.2; ENSRNOG00000019977.8.
DR RGD; 3453; Ptprf.
DR GeneTree; ENSGT00940000155060; -.
DR OMA; YWAAENE; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000019977; Expressed in jejunum and 19 other cell types or tissues.
DR ExpressionAtlas; A0A0G2JT62; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
DR GO; GO:0035373; F:chondroitin sulfate proteoglycan binding; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0031102; P:neuron projection regeneration; IEA:Ensembl.
DR GO; GO:0048679; P:regulation of axon regeneration; IEA:Ensembl.
DR GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
DR CDD; cd00063; FN3; 8.
DR CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR CDD; cd14629; R-PTP-F-2; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 11.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
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:SF7; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR Pfam; PF00041; fn3; 7.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00014; FNTYPEIII.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 8.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 5.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR PROSITE; PS50853; FN3; 7.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2JT62};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1907
FT /note="Receptor-type tyrosine-protein phosphatase F"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035167335"
FT TRANSMEM 1261..1284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..123
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 135..224
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 232..314
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 321..411
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 416..510
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 514..604
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 609..706
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 711..819
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 820..914
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 918..1010
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1352..1607
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1527..1598
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1639..1898
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1816..1889
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 693..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1907 AA; 212753 MW; E1F3CB347BBF9BE8 CRC64;
MAPEPAPGRR MVPLVPALVM LGLMAGAHGD SKPVFVKVPE DQIGLSGGVA SFVCQATGEP
KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA
KLSVLEEDQL PSGFPTIDMG PQLKVVEKAR TATMLCAAGG NPDPEISWFK DFLPVDPASS
NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS
QEVMPGGNVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV MRSANYTCVA
ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNTEPVSFY GIQYRAAGTD
GPFQEVDGVA STRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV
QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPLS AWHKHNTDAG LLTTVGSLLP
GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA KAESDTRIQL SWLLPPQERI
IKYELVYWAA EDEGQQHKVT FDPTSSYTLE DLKPDTLYHF QLAARSDLGV GVFTPTVEAR
TAQSTPSAPP QKVTCVSTGS TTVRVSWVPP PADSRNGIIT QYSVAYEAVD GEDRKRHVVD
GISREHSSWD LLGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL
NSTAVHVSWK LPVPNKQHGQ IRGYQVTYVR LENGEPRGQP IIQDVMLAEA QWRPEESEDY
ETTISGLTPE TTYSITVAAY TTKGDGARSK PKVVTTTGAV PGRPTMMVST TAMHTALLQW
HPPKELPGEL LGYRLQYRRA DEARPNTIDF GKDDQHFTVT GLHKGATYIF RLAAKNRAGP
GEEFEKEITT PEDAPSGFPQ NLRVTGLTTS TTELAWDPPV LAERNGRITN YTVVYRDINS
QHELQNVTGD VHLTLLGLKP DTTYDIKVRA HTSKGAGPLS PSIQSQTMPM EQVFAKNFRV
AAAMKTSVLL SWEVPDSYKS AVPFKILYNG QSVEVDGHSM RKLIADLQPN TEYSFVLMNR
GSSAGGLQHL VSIRTAPDLL PQKPLPASAF IEDGRFSLSM PQVQDPSLVR WFYIVVVPID
RVGGNLLAPR WSTPEELELD ELLEAIEQGE EKQRRRRRQA ERLKPYVAAQ VDELPETFTL
GDKKNYRGFY NRPLSPDLSY QCFVLASLKE PMDQKRYASS PYSDEIVVQV TPAQQQEEPE
MLWVTGPVLA VILIILIVIA ILLFKRKRTH SPSSKDEQSI GLKDSLLAHS SDPVEMRRLN
YQTPGMRDHP PIPITDLADN IERLKANDGL KFSQEYESID PGQQFTWENS NSEVNKPKNR
YANVIAYDHS RVLLTSIDGV PGSDYINANY IDGYRKQNAY IATQGPLPET MGDFWRMVWE
QRTATVVMMT RLEEKSRVKC DQYWPARGTE TYGLIQVTLV DTVELATYTM RTFALHKSGS
SEKRELRQFQ FMAWPDHGVP EYPTPILAFL RRVKACNPLD AGPMVVHCSA GVGRTGCFIV
IDAMLERMKH EKTVDIYGHV TCMRSQRNYM VQTEDQYVFI HEALLEAAMC GHTEVLARNL
YAHIQKLGQV PPGESVTAME LEFKLLANSK AHTSRFISAN LPCNKFKNRL VNIMPYELTR
VCLQPIRGVE GSDYINASFL DGYRQQKAYI ATQGPLAEST EDFWRMLWEH NSTIIVMLTK
LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTIRQFQF
TDWPEQGVPK TGEGFIDFIG QVHKTKEQFG QDGPITVHCS AGVGRTGVFI TLSIVLERMR
YEGVVDMFQT VKTLRTQRPA MVQTEDQYQL CYRAALEYLG SFDHYAT
//
