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Database: UniProt
Entry: A0A1S3H5S6_LINUN
LinkDB: A0A1S3H5S6_LINUN
Original site: A0A1S3H5S6_LINUN 
ID   A0A1S3H5S6_LINUN        Unreviewed;      1252 AA.
AC   A0A1S3H5S6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=LOC106151935 {ECO:0000313|RefSeq:XP_013380826.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013380826.1};
RN   [1] {ECO:0000313|RefSeq:XP_013380826.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26383154;
RA   Luo Y.J., Takeuchi T., Koyanagi R., Yamada L., Kanda M., Khalturina M.,
RA   Fujie M., Yamasaki S.I., Endo K., Satoh N.;
RT   "The Lingula genome provides insights into brachiopod evolution and the
RT   origin of phosphate biomineralization.";
RL   Nat. Commun. 6:8301-8301(2015).
RN   [2] {ECO:0000313|RefSeq:XP_013380826.1}
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};
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DR   RefSeq; XP_013380826.1; XM_013525372.1.
DR   AlphaFoldDB; A0A1S3H5S6; -.
DR   STRING; 7574.A0A1S3H5S6; -.
DR   EnsemblMetazoa; XM_013525372.1; XP_013380826.1; LOC106151935.
DR   GeneID; 106151935; -.
DR   KEGG; lak:106151935; -.
DR   InParanoid; A0A1S3H5S6; -.
DR   OrthoDB; 2903434at2759; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd00063; FN3; 4.
DR   CDD; cd14550; R5-PTP-2; 1.
DR   CDD; cd14549; R5-PTPc-1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
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; IPR013106; Ig_V-set.
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; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF7; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF07686; V-set; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   4: Predicted;
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_013380826.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678};
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1252
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010324409"
FT   TRANSMEM        559..588
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..121
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          132..232
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          237..331
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          332..435
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          439..548
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          644..911
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          828..902
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          944..1202
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1121..1193
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
SQ   SEQUENCE   1252 AA;  142143 MW;  B71906E69C0D2614 CRC64;
     MESAIYLPLL LCFFVFLCKA ENKVIKSRRG SVVTLPCDHG GINRANIDQV LWFKGTQSLL
     SWSNIGVTST AGTDPKAQER ITIIEADFSL RLNSVVMEDS GQYKCYVEYT SGNDTLMANS
     TLLLTIQDVP SPPGKPIISN IQSRSFHVTF TASALSNNSP IKYYNVHVIQ RGGNWENAIS
     FQVHATSNLS NILISSAGII RPYRNYVVRV SAINEIGNSS ASEETEVQTA EDEPLAKPTI
     LEIRNLTNSS VQLHWQDPSP DTLNGELLGY KIVYKRHPEG NLHPITVPNP DEKFCNITHL
     KPHTRYLVAL QLYNKAGESP KAEEIFLTDE GVPNRPRITD ISNQTSTSFV VAWVIPTEPN
     GIITSYKVRW NETDSSGNRI GQTKAETIRV EEGFKPTMKI RWLKPYTDYT VRVVAHTSKG
     EGEESVQQSV ITDVSNPGRP QRVLVKQNET GSVLLTWHSP ISFTRHIDRY LIKYYKEEDG
     ALGAVEKTLD VNPERREDAR NEPEEFALHG LEEGVVYKFS VAAATKSLFS SEYKIGQYTV
     PVTLTLEGKR ITTDAPEPAM GLAAILGVIA AVAVILIVPI VLAIVFLLRR KKNYQETATK
     GSDDNISQPL LLMELYGRSN YESVSIENWA DHVRKMHADG DLRFSEEYDD INNSVNKNIT
     QDAAYMDENK PKNRYVNILP FDHTRVVLKP MSKHNDYINA NFVDGYHKAK AYIATQGPLP
     NTFEDFWRMV WDQNSVIVVM ITNLEEKGRR KCDKYWPNEV GHTETYGNMQ VEYLDEDERA
     CYTIRKFCLR NQKAKRVSTR VKHSAFERII YQYHYTDWPD HGVPDYTLPV LTLVQKSSRH
     NPEGAGPIIV HCSAGVGRTG TYIVLDSMIR QILDKRTVNV CGFLTHIRHQ RSFLVQTEDQ
     YIFIHDALLE YIQKDGDTEV LNCKLKEFVE ENLTFCNAEG ECLLDRQYQL VTEYKPKDHE
     FSPAHMIYNK NKNRSERLLP VDKSRVHLPK QPGIDGSDYI NATFLQGYFK INEFVITQHP
     LGTTQEDFWR MVWDQNSATI VMLSEVTKDG EFPEFWQGKD ETQEIDSGNF KVTQTGEDFS
     QIHNITRDFL IESKQDDYEL TSRIISTTAW PESCTPLHTV LEFIDTVDSW HKEHQNGPII
     VIDKEGGSVA GTFCALYSLN NQRKHEDGVD VYSLAKTYHL MRPGIFSSKD DYHFLYKVMG
     SIVESQPDIL MDIKGRIGSS ESLNHGNNGQ PLSTWAHGLS LKRNEEQTTT TV
//
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