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Database: UniProt
Entry: A0A2D0RL04_ICTPU
LinkDB: A0A2D0RL04_ICTPU
Original site: A0A2D0RL04_ICTPU 
ID   A0A2D0RL04_ICTPU        Unreviewed;      1450 AA.
AC   A0A2D0RL04;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=ptprub {ECO:0000313|RefSeq:XP_017331194.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017331194.1};
RN   [1] {ECO:0000313|RefSeq:XP_017331194.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017331194.1};
RG   RefSeq;
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_017331194.1; XM_017475705.3.
DR   GeneID; 108269706; -.
DR   CTD; 335096; -.
DR   OrthoDB; 2875525at2759; -.
DR   Proteomes; UP000221080; Chromosome 1.
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; 2.
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; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
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; 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; 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   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Receptor {ECO:0000313|RefSeq:XP_017331194.1};
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..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1450
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012180886"
FT   TRANSMEM        747..772
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..185
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          187..272
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          285..380
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          383..486
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          492..593
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          914..1148
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1068..1139
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1180..1443
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1359..1434
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          835..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        835..855
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1450 AA;  163663 MW;  4BA4580BB275F0C3 CRC64;
     MKACAIILIL VVHIHADSVE GPTAAGCTFD EDSDPSLCEF SQGEEDDFDW QLFRTHTLLH
     STPDLLHGSY MIVNSSQHAA GQRAQLLLQT LSENDTHCVQ FSYFLYSRDG HSPGALRAYV
     RVNGGPLGMA VWNISGSQGH QWYQVELAVS TFWPNEYQVL LEATVDRWGY IAVDNILLLN
     YPCYKAPHFS RLGDVEVNAG QNATFQCVAA GRASEAEKFL LEQHNGKVSS GGSVKHLGRN
     RFSVSFQLED VQRPEQDLYR CVTQSSRGSG VSNFAELIVK VPPSPIAPPQ LLRAGSTYLI
     IQLNTNSILG DGPIIRREIE YRASHAPWSE INGVNMLTYK LWHLDPDTEY HISVLLTRPG
     EGGTGPPGPP LISRTKCAEP MRALRDLRAS EIQARQLILQ WEPLAFNLTR CHTYSVSLCY
     RYAIAGGTSG AGHNTTIREC LAVERNTSRF TLRDLPPYHS IHVRLALANT EGKKEGKEVM
     FQTEEDIPGG IAPESLTFTP LDDMVFLKWE EPVEPNGIIT QYEISYQSIE SSDPGINVPG
     PRRTVSKLRN ETYHMFSNLH PGTTYLISVR ARTAKGFGQT ALTEITTNIS APTFDYGDMP
     SPLSETESTI TVLLRPAQGR GAPVSMYQVV VEEESGRKLK RELGMQECFP VPTSHGEAQA
     RGAPHYYTAE LPPSSLAEGT PFTVGDNHTY NGYWNSPLDP RKNYLIYFQA MSNFRGETRI
     NCIRIARKAA CKDLRRAMEV TQHSEEMGLI LGICAGGLVV LILLLGAIII IIKKGRDYYS
     YSYYPRKPVN MNKTPITYRQ EKSHMMGSME RSFADQSTLQ EDERMALSFM DAHTCSTRSD
     PRSSMNESSS LLGGSPRRHC GSKGSPYHTG QLHPAVRVAD LLQHINQMKT AEGYGFKQEY
     ESFFEGWDVT KKKDKTKGRH DTLMDYDRHR VKLHPLLGDP NSDYINANYI DIRINREGYH
     RSNHFIATQG PKQETVYDFW RMVWQENCFS IVMITKLVEV KCYKYWPDDT EMYGDIKISL
     LKTETLAEYA VRTFSLERRG YSAKHEVQQF HFMSWPEHGV PYHATGLLAF IRRVKASTPA
     DAGPVVVHCS MGAGRTGCYI VLDVMLDMAE CEGVVDIYNC VKTLCSRRIN MIQTEEQYIF
     IHDAILEACL CGETAIPVNE FALTYKELLR VDSQSNSSQL REEFQTLNSV TPHLDVEECS
     IALLPRNRER NRSMDVLPPD RALAFLVTTE GDSNNYINAA LTDSFHRPAA FIVTPHPLPG
     TTTDFWRLVF DYGCTSIVML NQLNQSNSAW PCVQYWPEPG LQQYGPMQVE FLSMSADEDI
     ITRLFRVTNV SRLQEGHLVV CQFQFLRWSA YRDVPDSKKA FLNLLAHVQK WQRECGDGRT
     VVHCLNGGGR SGTFCACTIL MEMIQYQSMV DVFYAAKTLR NAKPNMVESL EQYRFCYDLV
     MEYLECMDLR
//
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