PTPRF_BOVIN
ID PTPRF_BOVIN Reviewed; 1898 AA.
AC A7MBJ4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase F;
DE EC=3.1.3.48;
DE Flags: Precursor;
GN Name=PTPRF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possible cell adhesion receptor. It possesses an intrinsic
CC protein tyrosine phosphatase activity (PTPase) and dephosphorylates
CC EPHA2 regulating its activity (By similarity). {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 -!- SUBUNIT: Interacts with GRIP1. Interacts with PPFIA1, PPFIA2 and
CC PPFIA3. Interacts with INSR. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
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DR EMBL; BC151592; AAI51593.1; -; mRNA.
DR RefSeq; NP_001094549.1; NM_001101079.1.
DR AlphaFoldDB; A7MBJ4; -.
DR SMR; A7MBJ4; -.
DR STRING; 9913.ENSBTAP00000024046; -.
DR PaxDb; A7MBJ4; -.
DR PRIDE; A7MBJ4; -.
DR Ensembl; ENSBTAT00000087285; ENSBTAP00000059113; ENSBTAG00000000253.
DR GeneID; 512072; -.
DR KEGG; bta:512072; -.
DR CTD; 5792; -.
DR VEuPathDB; HostDB:ENSBTAG00000000253; -.
DR VGNC; VGNC:33550; PTPRF.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000155060; -.
DR HOGENOM; CLU_001645_4_0_1; -.
DR InParanoid; A7MBJ4; -.
DR OrthoDB; 220353at2759; -.
DR TreeFam; TF312900; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000000253; Expressed in saliva-secreting gland and 105 other tissues.
DR ExpressionAtlas; A7MBJ4; baseline and differential.
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; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:1900121; P:negative regulation of receptor binding; ISS:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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; Phosphoprotein; Protein phosphatase;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1898
FT /note="Receptor-type tyrosine-protein phosphatase F"
FT /id="PRO_0000370192"
FT TOPO_DOM 30..1254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1255..1275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1276..1898
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..123
FT /note="Ig-like C2-type 1"
FT DOMAIN 135..224
FT /note="Ig-like C2-type 2"
FT DOMAIN 232..314
FT /note="Ig-like C2-type 3"
FT DOMAIN 321..411
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 416..510
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 514..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..810
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 811..905
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 909..1001
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1005..1089
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1343..1598
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1630..1889
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 REGION 693..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1539
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1830
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 1507
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1539..1545
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1583
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10586"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
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 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 156..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 253..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1898 AA; 211382 MW; 863570011A8BF6F1 CRC64;
MTPEPAPGRT MVPLVPALVM LGLVAGAHGD SKPVFVKVPE DQTGLSGGVA SFVCQATGEP
KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA
KLSVLEEEQL PLGFPSIDMG PQLKVVEKAR TATMLCAAGG NPDPEISWFK DFLPVDPAAS
NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS
QEVMPGGSVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV VRSANYTCVA
ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNSEPVSYY GIQYRPAGAE
GPFQEVDGVA TTRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV
QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPLS AWHKHNTDAG LLTTVGSLLP
GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA EVDSDTRIQL SWLLPPQERI
VKYELVYWAA EDEGQQHKVT FDPTSSYTVE DLKPDTLYRF QLAARSELGV GVFTPTIEAR
TAQSTPSAPP QKVTCVSVGS TTVRVSWVPP PADSRNGVIT QYSVAYEAVD GEDRGRHVVD
GIGREHSSWD LVGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL
NSTAVRVSWK LPVPSKQHGQ IRGYQVTYVR LENGEPRGAP IIQDVMLAEA QETTISGLTP
ETTYSITVAA YTTKGDGARS KPKIVTTTGA VPGRPTMMVS TTAMNTALLQ WHPPKELPGE
LLGYRLQYRR ADEARPSTID FGKDDQHFTV TGLHKGATYI FRLTAKNRAG LGEEFEKEIT
TPEDVPSGFP QNLRVIGLTT STTELIWDPP VLAERNGRIT NYTVVYRDIN SQQELQNVTA
DTHLTLSGLK PDTTYDIKVR ARTSKGAGPL SPSIQSRTMP VEQVFAKNFR VEAAMKTSVL
LSWEVPDSYK SAVPFRILYN GQSVEVDGHS MRKLIADLQP NTEYSFVLMN RGSSAGGLQH
LVSIRTAPDL LPHKPLPASA YIEDGRFTLT MPRVQEPALV RWFYIMVVPI DRMGGSMLAP
QWSTPEELEL DELLEAIEQG GGERLRRRRQ TERLKPYVAA QVDVLPETFT LGDKKNYQGF
YNRPLSPDLS YQCFVLASLK EPVDQKRYAC SPYSDEIVVQ VTPAQQQEEP ELLWVTGPVL
AVILIVLIVI AILLFKRKRT HSPSSKDEQS IGLKDSLLAH SSDPVEMRRL NYQTPGMRDH
PPIPITDLAD NIERLKANDG LKFSQEYESI DPGQQFTWEN SNLEVNKPKN RYANVIAYDH
SRVILTSIDG VPGSDYINAN YIDGYRKQNA YIATQGPLPE TMGDFWRMVW EQRTATVVMM
TRLEEKSRVK CDQYWPARGT ETYGLIQVTL LDTVELATYT VRTFALYKSG SSEKRELRQF
QFMAWPDHGV PEYPTPILAF LRRVKACNPL DAGPMVVHCS AGVGRTGCFI VIDAMLERMK
HEKTVDIYGH VTCMRAQRNY MVQTEDQYVF IHEALLEAAM CGHTEVPARN LYAHIQKLGQ
VPPGESVTAM ELEFKLLANS KAHTSRFISA NLPCNKFKNR LVNIMPYELT RVCLQPIRGV
EGSDYINASF LDGYRQQKAY IATQGPLAES TEDFWRMLWE HNSTIIVMLT RLREMGREKC
HQYWPAERSA RYQYFVVDPM AEYNMPQYIL REFKVTDARD GQSRTIRQFQ FTDWPEQGVP
KTGEGFIDFI GQVHKTKEQF GQDGPITVHC SAGVGRTGVF ITLSIVLERM RYEGVVDMFQ
TVKTLRTQRP AMVQTEDQYQ LCYRAALEYL GSFDHYAT
