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Database: UniProt
Entry: A0A087QQA5_APTFO
LinkDB: A0A087QQA5_APTFO
Original site: A0A087QQA5_APTFO 
ID   A0A087QQA5_APTFO        Unreviewed;      1982 AA.
AC   A0A087QQA5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, 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};
DE   Flags: Fragment;
GN   ORFNames=AS27_09674 {ECO:0000313|EMBL:KFM03409.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM03409.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM03409.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM03409.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 3 subfamily. {ECO:0000256|ARBA:ARBA00025789}.
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DR   EMBL; KL225807; KFM03409.1; -; Genomic_DNA.
DR   STRING; 9233.A0A087QQA5; -.
DR   Proteomes; UP000053286; Unassembled WGS sequence.
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; 10.
DR   CDD; cd14617; R-PTPc-B; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 15.
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:SF3; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   Pfam; PF00041; fn3; 15.
DR   Pfam; PF18861; PTP_tm; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 17.
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; 15.
DR   PROSITE; PS50853; FN3; 9.
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};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Receptor {ECO:0000313|EMBL:KFM03409.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT   DOMAIN          97..186
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          187..275
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          361..453
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          454..546
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          627..714
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          715..805
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          894..986
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1248..1341
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1342..1433
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1688..1948
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1866..1939
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFM03409.1"
FT   NON_TER         1982
FT                   /evidence="ECO:0000313|EMBL:KFM03409.1"
SQ   SEQUENCE   1982 AA;  221682 MW;  3B420B5DDB52E2B3 CRC64;
     QAAPGEAAGC SANLTERRVA GQSVRLRWGA AGRACNFSLT GRSEDGEAAG CQPAPTGNGS
     YGCILRGLEA GTWYHLRIEP LSDGEAVNIS VQTDPLPPPR FEINKEKTTL TSLQVQWDPS
     SGKVDLYNLV LFDHDNKKIQ EVSVPGRISK TENTFSSLIP GNKYNIVLSA VAGNKSTLEL
     HISGSTVPSP VKNIQVSVKT DTIHASWSPG SGHVDSYRLV LLDDHVPVHE IHQEDPLTSY
     TFSGLTAGHL YNLSVITQAA GLESSSFQTV RTAPAEVLDL TVTNDDSLDA LEVKWRRPSG
     NLDFYNITLS HLGSVKEVKT LQPLVTEIHF DKLTPGRLYQ VTARTISGEL FTDRMATGRT
     FPQKVSELKA GGGGWLRSLR VNWLPPAGDW ERYHLLLWNR SALVLNTTLE KDTTEYLIHD
     VGLIPGRQYD VEVVVESGDL QSKTSCTGRT APEPVLQLRV KHANESSLGV MWVTPVAEWD
     SYVVSLGDRD LTVIKKGLAK EAKEFTFTDL VPGRKYTATI TTISGILSNW TSVEGRTVPA
     QVTGLTVASQ GSTNSLFTNW TRALGDVDSY QVLLIHENVV IKNETVPSET NRYHFYPLKP
     GGLYSVVVTT VSGGISSRQT IAEGRTVPSS VTGVTVNNSG RSDYLSVSWL PASGDVDSYL
     VTLSHDDQIV QTLTISKSFS ECSFSSLTPG TLYNVMITTK SGKYENYSFS QERTVPSSVQ
     GLTVSNSARS DYLKVSWLHA SGYFDNYEVI IKNNNDFIQT KSVPKDENEC VFTNLVPGRQ
     YSVTVSTRSG KYETSERVYG RTMPESVKEL TLSNRSTEDL QVTWSKAEGD VDKYEIQLLF
     NDMKIFPPIF LGNTIEEYWF TALTPGRLYK ILVLTISGDA QRATFIEGLT IPSAVRNIHV
     SPNGMTNSLK VSWTPGGGDV DSYTVTIFQQ NHQLDSRSVS KHVSEHIFHK LEAGEQYRVV
     VQSNSGTLHS SLAAFGRTIP ASVQELLAHH AYSSHSLLVT WQKAPGVAER YDILLLNEQG
     ILLSNKSEPA TAKQHKFEDL LAGKKYKIQV LTVSGGLFSK RAETVGRTVP AAVTNLKVTE
     NTTDRLSFSW TTSLGELDSY DIFLYNPDKS LHDRISGEQH LQQCSFQNLR QGRMYRMVIV
     THSGDLTNES SVFGRTVPAP VVGLKASNRN MTDSLWFTWG PAAGDVDFYE LNLYNPNGTQ
     KETWHRKDLK EWHFQGLIPG RKYTLVVVTH SGDLTNTANA EGRTAPSPPN TVSFTDVANT
     SLSITWLGPP DWTDYDDFEL QWLPKDPLTV FNPYSSSKSK VRIMYGLRPG RLYEFSVRTV
     SGDSWKTYSQ SQSASVRTKP DKIQSLHCRP QTSTAIACSW TPPNSDFDGY SVECKKLDAP
     KLEFSKRIEK DKSLLNIMTL VPHKRYLVSI KVHSADMTSE VVEDSTITMI DRPPQPPPDI
     RVNKKEVLIT KSSINFTFNC SWFSDTNGAV KYFTVVVREA DGSEGPKPDE QHPLPSYLEY
     KHNDSIRIYQ TNYFASRCAE NPDSDYKSFD IKLGGEMENL GGRCDPDQQK FCDGPLKPRT
     AYRISIRAFT QLFSEDPKEL PKPLFADTFF SLPIITEAEP LFGVIEGVSA GLFLIVMLVA
     VTALFVCRQK VSNGHERPTA RLSIRRDRPL SVHLNLGQKG NRKTSSPIKV SHFEAHFTKL
     QADSNYLLSK EYEDLKDVGR NQTCDIALLP ENRGKNRYNN ILPYDTSRVK LSNVDDDPCS
     DYINASYIPG NNFRREYIAT QGPLPGTKDE FWKMAWEQNV HNIVMVTQCV EKGRVKCDHY
     WPLDQDSLYY GDLIVEMLSE SVLPEWTIRE FKICSEEQLD STRLIRHFHY TVWPDHGVPE
     TTQSLIQFVR TVRDYINRTP DTGPTIVHCS AGVGRTGTFI ALDRILQQLD SKDTVDIYAA
     VHDLRLHRVY MVQTECQYVY LHQCVRDVLR ARKLRSEQEN PLFPIYENVN PEYHRDAVYS
     RH
//
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