PTPRF_DANRE
ID PTPRF_DANRE Reviewed; 1909 AA.
AC A4IFW2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase F;
DE EC=3.1.3.48;
DE Flags: Precursor;
GN Name=ptprf; ORFNames=si:dkey-21k10.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possible cell adhesion receptor. It possesses an intrinsic
CC protein tyrosine phosphatase activity (PTPase) (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: The first PTPase domain has enzymatic activity, while the
CC second one seems to affect the substrate specificity of the first one.
CC {ECO:0000250}.
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 {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
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DR EMBL; BX663493; CAN88403.1; -; Genomic_DNA.
DR EMBL; BX248089; CAN88403.1; JOINED; Genomic_DNA.
DR EMBL; BX248089; CAQ13596.1; -; Genomic_DNA.
DR EMBL; BX663493; CAQ13596.1; JOINED; Genomic_DNA.
DR EMBL; BC134804; AAI34805.1; -; mRNA.
DR RefSeq; NP_001077045.1; NM_001083576.1.
DR AlphaFoldDB; A4IFW2; -.
DR SMR; A4IFW2; -.
DR STRING; 7955.ENSDARP00000077749; -.
DR PaxDb; A4IFW2; -.
DR PeptideAtlas; A4IFW2; -.
DR PRIDE; A4IFW2; -.
DR Ensembl; ENSDART00000083314; ENSDARP00000077749; ENSDARG00000005754.
DR GeneID; 799867; -.
DR KEGG; dre:799867; -.
DR CTD; 799867; -.
DR ZFIN; ZDB-GENE-060503-530; ptprfb.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000155060; -.
DR HOGENOM; CLU_001645_4_0_1; -.
DR InParanoid; A4IFW2; -.
DR OrthoDB; 220353at2759; -.
DR PhylomeDB; A4IFW2; -.
DR TreeFam; TF312900; -.
DR PRO; PR:A4IFW2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000005754; Expressed in pharyngeal gill and 31 other tissues.
DR ExpressionAtlas; A4IFW2; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0097374; P:sensory neuron axon guidance; IMP:ZFIN.
DR GO; GO:0099560; P:synaptic membrane adhesion; IBA:GO_Central.
DR CDD; cd00063; FN3; 8.
DR Gene3D; 2.60.40.10; -; 11.
DR Gene3D; 3.90.190.10; -; 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 Pfam; PF00041; fn3; 7.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00102; Y_phosphatase; 2.
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; SSF48726; SSF48726; 3.
DR SUPFAM; SSF49265; SSF49265; 5.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 8.
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 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Heparin-binding; Hydrolase;
KW Immunoglobulin domain; Membrane; Protein phosphatase; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1909
FT /note="Receptor-type tyrosine-protein phosphatase F"
FT /id="PRO_0000370194"
FT TOPO_DOM 32..1266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1267..1287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1288..1909
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..125
FT /note="Ig-like C2-type 1"
FT DOMAIN 137..225
FT /note="Ig-like C2-type 2"
FT DOMAIN 233..315
FT /note="Ig-like C2-type 3"
FT DOMAIN 322..412
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 417..511
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 515..604
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 609..706
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 711..819
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 820..914
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 918..1013
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1014..1098
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1354..1609
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1641..1900
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 399..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1550
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1841
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 68..77
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 1518
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1550..1556
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1594
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 963
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 158..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 254..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1909 AA; 213454 MW; 2568D6434864E596 CRC64;
MVPNTCTSVP LLPVGLPLLL LLSCIQFSSQ ADSLPNFVRS PEDQTGISGG VASFVCQAAG
EPKPRITWMK KGKKVSSQRF EVIEFDDGSG SVLRIQPLRT HRDEAIYECT ATNSLGEINT
SAKLTVLEEN QIPHGFPTID MGPQLKVVER TRTTTMLCAA SGNPDPEITW FKDFLPVDIN
GNGRIKQLRS GALQIENSEE SDQGKYECVA TNSAGTRYSA PANLYVRVRR VPPRFSIPPT
NHEVMPGGSV NLTCVAVGAP MPYVKWMTGE VELTKDEEMP VGRNVLELTN IRQSTNYTCV
AISSLGMIEA TAQVSVKALP KPPTSLTVTE TTATSVTLTW DSGNPEPVSY YIIQYRAKTS
DTNFQEVDGV ATTRYSIGGL SPYSEYEFRV MAVNNIGRGP PSEPVETRTG EQAPSSPPLH
VQARMLSAST MLVQWEPPEE PNGQIRGYRI YYTSDLDAPL SAWQKHNTDD SRLTTISSLT
TGITYSLRVL GFTSVGDGPP SDVLQVKTQQ GVPAQPSSFE AEAELDTRIL LTWLWPVQDP
IIKYELQYWE ADSDNKIHVT FDPAGSYAVE GLKPDTLYKF SLAARSEMGQ GVFTHPIEAR
TAQSAPSAPP QDVHLLSLSS TSIKVSWVAP PAASRHGAIV RYTVSYQAVN GEDTERHEVP
DIGADASSCV LEGLEKWTEY QVWVRAHTDV GPGPESTAVR IRTNEDVPGA PPRKLEVEAL
NSTAIRVTWK PPLSGKQHGQ IRGYQVIYSR LENGEPRGHP NIMDVALPEA QWKIEESTEY
EAVIAGLASE TSYSVTVAAY TTKGDGARSK AKVVTTTGAV PGKPTMIIST TVGNTALIQW
QPPKDMVGEL MGYRLRYKRL EEENYEIREF SRTDDHHTVT DLHKGATYSF HLSARNRAGL
GEEYVKDIGT PEDVPSGFPL NLQVVGLTTS TTRLTWEPPA LSERNGRIIH YIVVYRDINS
KQNSTNRTSD TQMTIQGLRP DTTYDIRVQA FTSKGGGPIS PSIQSRTMST SPAFATSFGV
KAVMKTSVLL TWEVPENYKS QVPFKILYNQ QSVEVQGNLK RKLITRLQPD TDYSFVLMSR
GNSAGGLQQQ VSIRTAPDLF KTKPVLYTAD QTNNGKLTIN LPKVPTSAPV RCYYIVVVPV
SQTSSRQWIN PDEMELDELL ESSEGAHLRR RRRHTDTVRP YIAAKLSTLP ETFTLGDELD
YSGFINRPLP NNQHFQCFVM AELKDQYPVT ANEKQRTFSA SPYSDPIIVQ GENQMQRSVD
QPEMLWVMGP VLAVVLIIII VIAILLFKRK RASPLPKDDH SGGVKDCLLA SSSDPVEMRR
LNYQTPGMRE HPPISVSELA DHIERLKAND ALRFSQEYES IDPGQQFTWE NSNLEVNKPK
NRYANVIAYD HSRVVLTPVD GVPGSDYINS NYIDGYRKQN AYIATQGPLP ETLSDFWRMI
WEQRASTIVM MTRLEEKSRV KCDQYWPIRG TETYGMIQVT MLDAVELATY SVRTFALYKN
GSSEKREVRQ FQFMAWPDHG VPEYPTPILA FLRRVKACNP PDAGPMVVHC SAGVGRTGCF
IVIDAMLERM KHEKTVDIYG HVTCMRSQRN YMVQTEDQYI FIHEALLEAA TCGNTEVPAR
NLYAHIQKLT QPSAGETVTA MELEFKRLAN SKAHTSRFIS ANLPCNKFKN RLVNIMPFES
TRVCLQPIRG VEGSDYINAS CIDGYRQQKA YIATQGPLAE TTEDFWRMLW EHNSTIVVML
TKLREMGREK CHQYWPAERS ARYQYFVVDP MAEYNMPQYI LREFKVTDAR DGQSRTIRQF
QFTDWPEQGV PKTGEGFIDF IGQVHKTKEQ FGQDGPITVH CSAGVGRTGV FITLSIVLER
MRYEGVVDLF QTVKTLRTQR PAMVQTEDQY QLCYRAALEY LGSFDHYAT
