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Database: UniProt
Entry: A0A1U8D813_ALLSI
LinkDB: A0A1U8D813_ALLSI
Original site: A0A1U8D813_ALLSI 
ID   A0A1U8D813_ALLSI        Unreviewed;       925 AA.
AC   A0A1U8D813;
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=Tyrosine-protein phosphatase {ECO:0000256|PIRNR:PIRNR000927};
DE            EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000927};
GN   Name=PTPN3 {ECO:0000313|RefSeq:XP_014377412.1};
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_014377412.1};
RN   [1] {ECO:0000313|RefSeq:XP_014377412.1}
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|PIRNR:PIRNR000927};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000927}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649,
CC       ECO:0000256|PIRNR:PIRNR000927}.
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DR   RefSeq; XP_014377412.1; XM_014521926.2.
DR   AlphaFoldDB; A0A1U8D813; -.
DR   GeneID; 102370971; -.
DR   CTD; 5774; -.
DR   OrthoDB; 5345383at2759; -.
DR   Proteomes; UP000189705; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13189; FERM_C_PTPN4_PTPN3_like; 1.
DR   CDD; cd17193; FERM_F1_PTPN3; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd14600; PTPc-N3; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR041783; PTPN3/4_FERM_C.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR012151; Tyr_Pase_non-rcpt_typ-3/4.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR45706; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR45706:SF5; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 3; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000927; Tyr-Ptase_nr3; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50106; PDZ; 1.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000927};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|PIRNR:PIRNR000927}; Hydrolase {ECO:0000256|PIRNR:PIRNR000927};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR000927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705}.
FT   DOMAIN          29..312
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          521..593
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          658..913
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          831..904
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          360..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        854
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000927-1"
FT   BINDING         823
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
FT   BINDING         854..860
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
FT   BINDING         898
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
SQ   SEQUENCE   925 AA;  105846 MW;  8E529B21024BAC1B CRC64;
     MNSRLRALGG RINNIRSSEL PKEKTRSEII CNVHFLDGSI QSFKVNKQDT GQILLDMAYN
     HLGVTEKEYF GLQQNEEAVD SPRWLETSKP IKKQLKGGFP CTLHFRVRFF IPDPNTLQEE
     QTRHLFFLQL KTAILEGRLT CPLNSAVVLA SYAVQAQLGD FNSTEHHSGY LSNFHFLPDQ
     NKDFLIKVES LHEQHSGLKQ SEAESCYINI ARTLEFYGVE LHSGRDLHNL DLMIGIASGG
     IAVYRKCICT SFYAWANILK ISFKRKKFFI QQRQKHNETR EHIVAFNMLN YRACKNLWKS
     CVEHHTFFQA KSLPHENKIF SHYWTLGSRN LTKSVNNQYC RKVIGGMVWN PSMRRSLSVE
     HLETKSLPSR SPPVTPNWRS PRLRHEIRKP RHSSVDNLTN EITYITETED VFYTYKVSPT
     SKNSDSEVSQ NRSPWRRSPE QESSKNILGN SPSESCLTHT SPNTSTQSPN GVGNTSGSYP
     LDGADQQFLE TYDNVTKGST SEDSSQYYCD RNEVIDGDLL SVHITPDEDG KFGFNLKGGV
     DQKMPLVVSR ITPGSPADIC IPKLNEGDQI VLINGRDISE HTHDQVVMFI KASRESHTRE
     LALLVKRKVL KHFVETKSED EADSQNFQES ILPTCSEYGD TLEESMEQLK KGLENGTVLT
     QFEQLYRKKP GLSVTCAKVP QNMDKNRYKD VLPYDATRII LQGDEDYINA NYVTMEIPSA
     GIVNRYIATQ GPLPHTCAHF WQVVWDHRLT LIIMLTTLTE RGRTKCHQYW PDPPEIMEYG
     NFRVKCQSED CTIAYVFREM VLTNIETEQE HIVTHLQYVA WPDHGVPDDS TDFLEFVNCM
     RPKRVKNEPV LVHCSAGIGR TGVLVTMETA LCLIERNQPV YPLDIVRKMR DQRAMMVQTS
     SQYKFVCEAI LRVYKEGLVR PLDSS
//
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