ID W5KY58_ASTMX Unreviewed; 1461 AA.
AC W5KY58;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=PTPRM {ECO:0000313|Ensembl:ENSAMXP00000012520.2};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000012520.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000012520.2}
RP IDENTIFICATION.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2B subfamily. {ECO:0000256|ARBA:ARBA00006396}.
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DR Ensembl; ENSAMXT00000012520.2; ENSAMXP00000012520.2; ENSAMXG00000012131.2.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000155020; -.
DR HOGENOM; CLU_001645_0_2_1; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000012131; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd00063; FN3; 3.
DR CDD; cd06263; MAM; 1.
DR CDD; cd14633; R-PTPc-M-1; 1.
DR CDD; cd14635; R-PTPc-M-2; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR003599; Ig_sub.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR045911; R-PTP-mu_cat_rpt1.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR24051:SF12; PROTEIN TYROSINE PHOSPHATASE, RECEPTOR TYPE, M; 1.
DR PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00020; MAMDOMAIN.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 1.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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 Reference proteome {ECO:0000313|Proteomes:UP000018467};
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|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1461
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017337108"
FT TRANSMEM 743..764
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..182
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 184..275
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 282..375
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 380..478
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 479..585
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 909..1163
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1083..1154
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1195..1457
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1371..1448
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 837..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1461 AA; 164262 MW; 87CA8BCBDDBBC249 CRC64;
LCLITHCPSL YCTLLLTAAP PCDCSFEKPF TACGYSQGRD DDLDWEQANT KEKPSANQWM
PPGSTFMMVN TSGRFAGQKA LLLSPQLKEN DTHCVIFQYL VSGREGGSPG HLNIYIKENN
SPMGLPVWNT SGPVSRSWNQ VELAISTYWP NFYQIVFEVV TSGQRGLLAI KDVAVQGHQC
MTTPHFLHIK GVEVNAGQTA TFHCTVNGEW RDNFNLWLQG IGGREAPMKA TKPWNNQRFI
GMFDVVNTTK QDSGRYRCIV HSNKGVGVSN YGELTIKQPP VPIAPPQLTA VGATYLWIQL
NANSINGDGP IINREVEYRT VSGTMYDLQP VDKTSHKIGH LDPDTEYEIS VLLTRPLDGG
TGAPGPPLRA RTKCAEPMHG PRQLKVVDIK ARQVTIRWEP FGYNVTRCHN YSLTVQYRAR
AGGKEDSREE VYYDSKSSAP QHTIHNLTPF TNLSVKLVLR NREGVKESDE IHLQTEEDVP
GAVPLDSIQA SVYEEKIILK WREPAHTYGV ITQYEISYKA VSSFDPVLDL SNQSGKVIKL
GNETSHVFLG LYPGSTYSFS LRASTAKGYG SPAITQATTK ISAPSMPAYD QETSLNQTDS
TVTVLLKPAQ SRGAPVSVYQ VVVEEERPRR ARGGEAEILR CYPIPVHYQN ATSLNSKYYF
TAEFPSGGIP SPQPFTVGDN KTYSGFWNAP LLPHKSYSIY YQAVSTANGE TKIDCVRVAT
KGAATHKPNA VEPEKQTDHT VKIAGVIAGI LLFVIIFLGV VLLMKKRKLA KKRKETLSST
RQEMTVMVNS MDKSYTEQGT NCDEALSFMD THNLNSRSGS SPCSLTVKTN TLSTTLPNSY
YPDETQTMTS ETSSLAPSHT HTHSSHTHSL RKRDGVDVPY QTGQLHPAIR VADLLEHVTQ
MKCAEGYGFK EEYESFFEGQ SAPWDSAKKD ENRMKNRYGN IIAYDHSRVR LQSLEGEQSS
DYINANYVDG YHRPNHYIAT QGPMQETVID FWRMVWQENT ATIVMVTNLV EVGRVKCCKY
WPDDTEIYRD MKVTLIETQL LSEYVIRTFA VEKRGAHEIR EIQQFHFTGW PDHGVPYHAT
GLLGFIRRVK AKSPANAGPI VVHCSAGAGR TGCFIVIDIM LDMAEREGVV DIYNCVRELR
SRRVNMVQTE EQYVFIHDAI LEACLCGDTT IPANQLRSVY YDMNRLDPQT NSSPIKEEFR
TLNMVTPTLR VEDCSIALLP RNHEKNRCMD VLPPDRCLPF LITIDGESSN YINAALMDSY
KQPSAFIVTQ HPLPNTVKDF WRLVLDYHCT SIVMLNDVDP AQLCPQYWPE NGVHRHGPLQ
VEFVSADLEE DIISRIFRIY NAARPQDGYR MVQQFQFLGW PMYRDTPVSK RSFLKLIHQV
DKWQEEYDGG EGRTVVHCLN GGGRSGTFCA ISIVSEMLRH QRSVDVFHAV KTLRNNKPNM
VDLLDQYKFC YEVALEYLNS G
//
