GenomeNet

Database: UniProt
Entry: A0A1S3JYW1_LINUN
LinkDB: A0A1S3JYW1_LINUN
Original site: A0A1S3JYW1_LINUN 
ID   A0A1S3JYW1_LINUN        Unreviewed;      1638 AA.
AC   A0A1S3JYW1;
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=LOC106177090 {ECO:0000313|RefSeq:XP_013415221.1};
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_013415221.1};
RN   [1] {ECO:0000313|RefSeq:XP_013415221.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013415221.1};
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_013415221.1; XM_013559767.1.
DR   EnsemblMetazoa; XM_013559767.1; XP_013415221.1; LOC106177090.
DR   GeneID; 106177090; -.
DR   KEGG; lak:106177090; -.
DR   OrthoDB; 2915192at2759; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042806; F:fucose binding; IEA:UniProt.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0010185; P:regulation of cellular defense response; IEA:UniProt.
DR   GO; GO:0001868; P:regulation of complement activation, lectin pathway; IEA:UniProt.
DR   CDD; cd00063; FN3; 4.
DR   CDD; cd00047; PTPc; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR006585; FTP1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
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; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00607; FTP; 2.
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; 3.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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_013415221.1};
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..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1638
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010339050"
FT   TRANSMEM        962..986
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          421..519
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          626..718
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          722..817
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1074..1331
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1249..1322
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1363..1626
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1542..1617
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          622..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          996..1034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..644
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1017..1034
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1638 AA;  182348 MW;  B364BD6522E85A7F CRC64;
     MNGGLRHRPG SSEVLLILFI VIQVQTSLSC VEGEGYFGWL CDTQSNCFCK QAQICQKTLG
     TCPPNCVDNP WGIGCSDDDV NLAQGKQASQ SSTNSNFLAS LAVDGNNSTQ GSDCALTNLQ
     NDPSWLVDLG GLHVVRKIAV QKPTSGVCPF NLVFACIGNS TVTSNCRDIS RADACATAYL
     EFPIDPPILG RYVRIKKVGG QILSLCEVIV KGYEYPYNLA YGKLTQQSTG ESASRAVDGN
     LDTYFYHASC THTANEANPW WRTDLGAQYA VYSVTLVNRG DCCGSRLNYF DIKLRNNTIS
     GSYDVCISRN TQIPEGQAVE LPCVQQFVGH VLIIQLRATN VLTLCEVLVK GYKYQACADG
     AFGPQCQYLC QCQLPNEVCH TVTGQCSSGC GAGWKGHGCQ VPTACLPHWK GNGCFQEVPR
     LVGPPRKVSR TGDTVTISWD AWSAATGAGT GSATRYIVEY QADGSSGSVW QRKDAGNQFS
     TTVSNLNQYT DYRFRVIVVD EEGREGKSSA SATFKTCGAP LMPPQPIAIS ALLYGDRSVA
     VIHYTVQGID SGITRCESLQ KIRVRYQRQG DSSTVGPNDT ANPTYSIYNL IPYSNYTLIL
     SIFNNAGLEG PSRAVYATTP EGVPPKMSPP TITSQQSDSV ELSWSEPNPP GGRITRYDVR
     YSTATGGQLT VVDFNETTFR GTIGNLQTNV TYAIQIRAAT NQGPGQYSDL VQAVTVEGSP
     GEPNNLENSS RTDSSLTLRW NEPIKKNGRI MGYKIICSVY NSPSDTNKTY ISNSPELRQQ
     VVENLRPSTR YVCGVAARTS VGYGTYTTRV LWTAPSPPVI DDESLRNSRT PRKRTRSTVT
     VLLPIVSVGD KYRIVVELMS RRRKRDVNSD TRNLTSYREA MDLNLNYYIT AEVDSTRLGA
     EFTVGDNQTY GGYQNTPLVE GQTYDIYFGV LSSIDGVTAQ TYSRLLSGFV PRNDDTAPSS
     DAGVIGGVIA AVVLVAVIVI VVAVILMKRR RRQMSKPSSR EEIPFKNAAF KDDNLNGSTE
     HITDPESPKK KHEPVTNEVL YTDAEPLYGN VEQGTDIPVA QIMHIMLWKT RELMKEEYEK
     LSKDLQAACT AGRKPENNIK NRFKNILPYD HSRIVLDKLP DDPQSDYINA NYIDGYKRSN
     AFIAAQGPKP NTVNDFWRMV WQVDSPLIVM VTRIVENAKA KSAEYWPNKG SVQHGEITII
     SMHVEEHEDF SIRTFQITKT GESSEKSLKQ FHFTGWPDHG VPVDPTSLIT FRKKIKEYET
     TVQRRGPVVV HCSAGVGRTG TFIALDYLMD QAQAEGKINI FQLVQLMRGA RPKMIQTVEQ
     YYFLHYTMLE ELLCGETTIP VQEFAERYAE LKKKGSSESS TKLEEQFEVL QIMTPEIDQE
     ETKTALNEEN LSKNRVRNIV PANHCRPYLE INSTQTSDYI NAVFVDGHRR FDAYIVTQMP
     LPSTVVDFWR MIHDQRSATI VMLNEIIQDD EQTVAVYWPE TGTATYGHFT VEFVKSRAPS
     EHLSVREYKL NNSERPKDAP QRICQFQYHG WKTSDAVPQS KSAFLGLIDE IEHWQQQSGN
     TRITVHCMNG AHQSGLFCAV SRIVEKTKVE QEVDVFHTIK ATRINRPQFV DSLDQCKFCY
     ECVDDYIHMF DTYANFQA
//
DBGET integrated database retrieval system