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Database: UniProt
Entry: A0A1U7S046_ALLSI
LinkDB: A0A1U7S046_ALLSI
Original site: A0A1U7S046_ALLSI 
ID   A0A1U7S046_ALLSI        Unreviewed;      1284 AA.
AC   A0A1U7S046;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRJ {ECO:0000313|RefSeq:XP_006022078.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006022078.1};
RN   [1] {ECO:0000313|RefSeq:XP_006022078.1}
RP   IDENTIFICATION.
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: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 3 subfamily. {ECO:0000256|ARBA:ARBA00025789}.
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DR   RefSeq; XP_006022078.1; XM_006022016.3.
DR   GeneID; 102384685; -.
DR   CTD; 5795; -.
DR   OrthoDB; 5399547at2759; -.
DR   Proteomes; UP000189705; 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; 6.
DR   CDD; cd14615; R-PTPc-J; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR041201; PTPRJ_TM.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF5; PROTEIN TYROSINE PHOSPHATASE, RECEPTOR TYPE, H; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF18861; PTP_tm; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 8.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 4.
DR   PROSITE; PS50853; FN3; 6.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Receptor {ECO:0000313|RefSeq:XP_006022078.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705};
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|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1284
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010570244"
FT   TRANSMEM        919..943
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          131..219
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          220..308
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          309..397
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          398..488
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          489..579
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          580..672
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          988..1245
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1163..1236
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          41..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1284 AA;  142646 MW;  1CA247DBAFF41925 CRC64;
     MEQPFFPSLL LLLLLSLSKI KSSNGCGPNC SSIITTTTRK LSSKELTEGS VTHGDGMSFS
     SLSTSEPTSV SSTHFASIAD FLESNSGTDS MKQNVSLSGK HNSTDNETST ASPDSTLLNN
     GTGSSDPKPS PVFDIQAIAI STDKVNLTWK NNDTSADNYT YVILKAGTEF PNITVLQKMQ
     AVIMGLEPGT LYNFTIYPVA PGSTTEGDRN STTVYTKPSP VFDIQAIDIS TDYVNLTWKN
     NDLAADNYSY MILGDSASFP NITIFEKRQA VITGLKPGTL YNITIYPLAP DNATKGDGNS
     TTVYTKPSPV FDIQAIDIST DYVNLTWKNN DSDADNYTYM ILGNSASFPN STIFQKRQAV
     ITGLEPGTLY NITIYPLAPD NATKGDGNST IVYTKPSPVF AVQAIHISTD QVNLTWKNND
     AAADKYTYEI KFFKDGNLTL WPEKPQITGA VITGLEPGTL YNFTIYPLAP DNTTRGDGNS
     TSVYTKPSPV FAVQAIHIST DQVNLTWKNN DAAADKYTYE IQFFKDGNLT FWPEKPQITG
     AVITGLEPGT LYNFTIYPLA PDNTTRGDGN STSVYTEPSP VFDIQAIDIS TDYVNLTWKN
     DDSAADNYIY VIEIFKHGTL FPSNKTLPKR EAVITGLEPG TSYHFKVFPL ALDNRTWGYP
     NSTSVCTNAA PPHEFKCEQV PRKPELKLNW LCPLGNNSGF RIKISNGIRT NESSVSSCKS
     GNVEKSIDNL TYYTTFYINI TTHSCGKDSL PEQRTCATSI TDPPAPSAPP AITGIDHNSF
     KVQFSPFKSE HGPLKAYAVL ITTANDNQPS KYNLNLTYHD FKTKKTHTYV TYVMNIEHTR
     ASLSTSRSQP YTVVVGNANT THAYYNGPLE PLGLYRTSVA GFTDITYANN KTGPIVEERS
     YVSFTPYSEP FRVPQDPGVI VGAVLGSILC VSAVLLVVVF VFWRRRRKDG KNNDVSFSQI
     KPKKSKPIKV ENFESYFKTQ QADSNCGFAE EYEELRPAGV HQPKFAAELA ENRGKNRYNN
     VLPYDISRVK LSAQSHPTDD YINANYMPGY NLRKEFIAAQ GPLPNTLEDF WRMIWEKNIY
     AIVMLTKCIE QGRTKCEQYW ADKQPMSYGD ITVTMTSEIV LAEWTIRDFT IEDNNETDSH
     CVRQFHFTAW PDHGVPETTE LLISFRHLVE EYARQNPPES PTLVHCSAGV GRTGTFIAID
     RLIQQIEMEN TADVYGVVYD LRMHRPLMVQ TEEQYVFLNQ CVLDIIKSQR DKKVDLIYQN
     TTAMAIYENL APAPNFGKAN GYCA
//
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