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Database: UniProt
Entry: A0A3Q2VM16_HAPBU
LinkDB: A0A3Q2VM16_HAPBU
Original site: A0A3Q2VM16_HAPBU 
ID   A0A3Q2VM16_HAPBU        Unreviewed;      1448 AA.
AC   A0A3Q2VM16;
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:ENSHBUP00000013022.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000013022.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000013022.1}
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_005941065.1; XM_005941003.2.
DR   Ensembl; ENSHBUT00000032789.1; ENSHBUP00000013022.1; ENSHBUG00000015066.1.
DR   GeneID; 102308225; -.
DR   GeneTree; ENSGT00940000157151; -.
DR   OrthoDB; 2875525at2759; -.
DR   Proteomes; UP000264840; 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:UP000264840};
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..1448
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018543778"
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..1146
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1066..1137
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1178..1441
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1357..1432
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          838..872
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   1448 AA;  163192 MW;  1B6DD9B0DE7466DB CRC64;
     MYSAALLLML AIRIYADSME GPTAGCTFDE DSDPGLCEYR QGQEDDFDWQ LIRTYNWPHP
     TPDLLRGSFM MVNSSQHYGG QRAQLLLLPL SENDTHCIQF SYFLYSRDGH SPGDLQVYVR
     VNSGPKGSAV WNISGSQGRQ WHQVELAVST FWPSEYQVIF EATVSEERQG YIALDDIVLL
     NYPCYKVAHF SRLGDVEVNA GQNASFQCVA TGKVSEAEPF LLERRNGVLL DTSMLTRLSH
     KRLMATFQVE AQRGEQDLYR CITLSPRGAA VSNFGELIVR VPPTPIAPPQ LLRAGPTYLI
     IQLNTNSIVG DGPVIRREIQ YRASQSTWTE THGVGSLTYK VWHLEPDTEY HISVLLTRPG
     EGGTGAPGPP LISRTKCAEP MRALRGLTAT EIQPRQLTLQ WEPLGYNLTR CHTYTLSLCY
     RYSMPTGGSG GNNATVRECL SVDRNTSHFT LRDLPPFRAV HVRLALANPE GKKESREVTF
     QTEEDIPGGI APESLTFTPL DDMIFLKWEE PIEPNGLITQ YEISYQSIES SDPGINVPGP
     RRTVSKLRNE TYHMFSGLHP GTTYLVSVRA RTAKGFGQTA LTEITTNISA PVFDYEDIPS
     PLSESESTIT VLLRPALGRG APVSAYQVVV VEEDGSRHVK RRELGTVDCF PTPNSHNEAQ
     AKGAPHYYTA ELAPSSLPEA TPFTVGDNHT YNGYWNSPLD PTKNYLIYFQ ATSNFRGETR
     INCIRIARKA ACKDSKRALE VSQHAEDMGL ILGACAGGLV VLILLLGAIV IIVKKGRDFY
     SYPYYPRKKV AINKAAMSYR QEKSRKLSSL DCSMTEQSTL QQDERMAHSF MDAHGCNARN
     EQRSSVNESS SLLGGSPQRH CRRKSSPYHT GQLHPAVRVA DLLQHINQMK TAEGYGFKQE
     YESFFDGWDV TKKKDKTKGR HDSLLSHDRH RVKLHSLLAD PSSDYVNANY IDGYQRSNHF
     IATQGPKQEM IYDFWRMVWQ ENCFSIVMIT KLVEVGRMKC CKYWPDDTEL YGDIKITLLK
     TETLAEYTVR TFAMERRGYP AKHEVCQFHF TSWPEHGVPY HATGLLAFLR RVKASTPPDA
     GPVVVHCSMG AGRTGCYIVL DVMLDMAECE GVVDIYNCVK TLCSRRINMI QTEEQYVFIH
     DAILEACLCG ETAIPVTEFA LTYKEMLKVD SQSNSSQLKE EFQTLNSVTP HLDVEECSIS
     LMPRNREKNR SMDVLPPDRS LAFLVTTEGE SSNYINAALA DSFLRPAAFV VTPHPLPGTT
     TDFWRLVYDY GCTSVVMLNQ LNQSNSAWPC LQYWPEPGLQ QFGPMTVELL SRTADDDVII
     RLFRVQNITR LQEGQLVVRH FQFLRWSPYR DVPDSKKAFL SLLAQVHNWQ RECGEGRTIV
     HCLNGGGRSG TFCACTMILE MIRHHSIVDV FFAAKTLRNS KPNMVETMEQ YRFCYDLAQE
     YLDCLEVR
//
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