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Database: UniProt
Entry: A0A3Q3A0N7_KRYMA
LinkDB: A0A3Q3A0N7_KRYMA
Original site: A0A3Q3A0N7_KRYMA 
ID   A0A3Q3A0N7_KRYMA        Unreviewed;      1454 AA.
AC   A0A3Q3A0N7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRU {ECO:0000313|Ensembl:ENSKMAP00000009315.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000009315.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000009315.1}
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   RefSeq; XP_017287368.1; XM_017431879.1.
DR   STRING; 37003.ENSKMAP00000009315; -.
DR   Ensembl; ENSKMAT00000009453.1; ENSKMAP00000009315.1; ENSKMAG00000006903.1.
DR   GeneID; 108245184; -.
DR   KEGG; kmr:108245184; -.
DR   CTD; 563584; -.
DR   GeneTree; ENSGT00940000157151; -.
DR   OrthoDB; 2875525at2759; -.
DR   Proteomes; UP000264800; Unplaced.
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   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; IPR013783; Ig-like_fold.
DR   InterPro; IPR000998; MAM_dom.
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; PTHR24051:SF10; PROTEIN-TYROSINE-PHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00041; fn3; 2.
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; 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   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS00740; MAM_1; 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   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1454
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018642063"
FT   DOMAIN          24..186
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          285..380
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          383..485
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          491..591
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          915..1152
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1072..1143
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1184..1447
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1363..1438
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          838..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..856
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1454 AA;  163806 MW;  C97172C995A43A9B CRC64;
     MHSAALLLML AARICADSTE RPTAGCTFDE DSDSGLCEYK QGQEDDFDWQ LIRTYSWLHP
     TTDLLPGSFM MVNSSQHMGA QRAQLHLLPL SENDTHCIQF SYFLYSRDGH SPGALQVYIR
     VNGGPKGSAV WNISGSQGHQ WHQVELAVST FWPSEYQVIF EATISDDRQG YIALDDTVLL
     NYPCYKVAHF SRLGDVEVNA GQNASFQCVA TGKVSETEPF LLERRNGVVL NTSLLSRLSH
     KRLMATFQVE AQRGEQDLYR CITLSPRGAA VSNFGELIVR VPPTPIAPPQ LLRAGPTYLI
     IQLNTNSIVG DGPVIRREIQ YRASQSTWTE THVVGSLTYK VWHLEPDTEY QISVLLTRPG
     EGGTGAPGPP LVSRTKCAEP MRALRGLTAT EIQPRQLALQ WEPLGYNLTR CHTYSLSLCY
     RYSMPTGSSG GNNATVRECL SVDRNTSHFT LRDLPPFRTV HVRLALSNPE GKKESREVTF
     QTEEDIPGGI APESLTFTPL DDMIFLKWEE PVEPNGLITQ YEISYQSIES SDPGINVPGP
     RRTVSKLRNE TYHMFSGLHP GTTYLVSVRA RTAKGFGQTA LTEITTNISA PVFDYEDIPS
     PLSESESTIT VLLRPALGRG APVSAYQVVV VEEDGSRQVR RRELGTVDCF PSPNSHNEAQ
     AKGSPHYYTA ELAPSSLPEA TPFTVGDNHT YNGYWNSPLD PTKNYLIYFQ ATSNFRGETR
     INCIRIARKA ACKDSKTALE VSQHAEDMGL ILGACAGGLV VLILLLGAII IIVKKGRDFY
     SYPYYPRKKV AINKAAMSYR QEKSRKLSSL DCSMTEQSTL QQDEKMVHSF MDTHGCNARN
     EQRSSVNESS SLLGGSPQRH CRRKSSPYHT GQLHPAVRVA DLLQHINQMK TSEGYGFKQE
     YESFFNGWDV TKKKDKTKGR HDSLLSHDRH RVKLQSLLAD PSSEYVNANY IDIRINREGY
     QRSNHFIATQ GPNQEMIYDF WRMVWQENCF SIVMLTKLVE IGRIKCCKYW PDDTELYGDI
     KITLLKTETL AEYTVRTFAM ERRGYPAKHE VCQFHFTSWP EHGVPYHSTG LLAFLRRVKA
     STPPDAGPVV VHCSMGAGRT GCYIVLDVML DMAECEGVVD IYNCVKTLCS RRINMIQTEE
     QYVFIHDAIL EACLCGETAI PVSEFALTYK EMLKVDSQSN TSQLREEFQT LNSVTPHLDV
     EECSISLMPR NREKNRSMDV LPPDRSLAFL ITTEGESSNY VNAALADSFL RPAAFVVTPH
     PLPGTTTDFW RLVYDYGCTS VVMLNQLNQS NSAWPCLQYW PEPGLQQFGP MTVELLSRTA
     DDDIIIRLFR IQNITRLQEG QLVVRHFQFL RWSPYRDVPD SKKAFLSLLA QVHNWQRECG
     EGRTAVHCLN GGGRSGTFCA CTMILEMIRH HSMVDVFFAA KTLRNSKPNM VETMEQYRFC
     YELAQEYLDC LEVR
//
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