UniProt: A0A0A0AE29

Database: UniProt
Entry: A0A0A0AE29_CHAVO

LinkDB:  A0A0A0AE29_CHAVO 
Original site:  A0A0A0AE29_CHAVO

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (23)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (5)   
   SMART (4)   
All databases (28)   

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ID   A0A0A0AE29_CHAVO        Unreviewed;      2305 AA.
AC   A0A0A0AE29;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 50.
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=N301_10451 {ECO:0000313|EMBL:KGL92177.1};
OS   Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX   NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL92177.1, ECO:0000313|Proteomes:UP000053858};
RN   [1] {ECO:0000313|EMBL:KGL92177.1, ECO:0000313|Proteomes:UP000053858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL92177.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-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 5 subfamily. {ECO:0000256|ARBA:ARBA00006246}.
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DR   EMBL; KL871448; KGL92177.1; -; Genomic_DNA.
DR   STRING; 50402.A0A0A0AE29; -.
DR   Proteomes; UP000053858; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd03122; alpha_CARP_receptor_like; 1.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd17669; R-PTP-Z-2; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR041887; Alpha_CARP_receptor-type.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
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; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF461; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE ZETA; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
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|EMBL:KGL92177.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1635..1659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..281
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
FT   DOMAIN          295..392
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1714..1982
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1899..1973
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          2013..2272
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          2189..2263
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          606..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1438..1479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1519..1585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2280..2305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1455..1478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1519..1553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1571..1585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2280..2294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL92177.1"
FT   NON_TER         2305
FT                   /evidence="ECO:0000313|EMBL:KGL92177.1"
SQ   SEQUENCE   2305 AA;  254966 MW;  09DA0B40075D69DC CRC64;
     DLAYGYYRQQ RKLIEEIDWS YTGTLNQKNW GKKYSACNGA KQSPINIDED LTQVNVNLKK
     LKFHGWEKET LEDTFIQNTG KTVEINLTND YYVSGGGLDT IFKASKITFH WGKCNVSSDG
     SEHSLEGQKF PLEMQIYCYD ADQFTNFEEA IKGNGKLRAL SVLFEIGLED NPDYNPIING
     VDSVSRFGKQ AALEPFILLN LLPNATDKYY TYNGSLSTPP CSETVEWIVF KDTISISENQ
     LAVFCEVLTM QQSGYVMLMD YLQNNFREQQ YKFFGQVFSS YTGQEEIHEA VCSSEPENVQ
     SDPKNYTSLL VTWERPRVVY DTTIERFAVF YQQLDGEDQT KHEFLTDGYQ DLGAILNNLL
     PNTSYVLQIV AVCSNGLYGK YSDQVIVDMP LEDAEADLIP ELNETEEYED EVDEKETEVD
     EETAVIPSTD STINQIRRKD YQVTTSSYSQ EKMGAKPNEA KTNRYLTREE LHGKDDVFKA
     VYYPTSPPVS EISEEEEEPF LESRTITGIP PQLIDSTKGV EEEYIYLSSG TEPTKITTTG
     HSDEDFLLSP FKPHQESDDF WNSVLTTSSA QLVTEEASQE DTLPSGSPDI STHYVLSQGS
     VKYVSEGVAP SSSDEPPKHT SSTDGNVWFR KAADLTTQSV DTSDSRQLSQ TSYTDAYVEG
     LKPATVPYSS SPVVSRDTSD ADLELPHYST FAFSSAELSP HSISSSSGEY GSASAASEVL
     SQTTQPVYNG EIPLQPSYSS EVFPLVTPLL FDSQMLDTTP ATSDSDVTLH ATPVFPSVDV
     SFEPTLSSYD DVPLLTFSSA SSSSKMFHRL YTVSQMFPQS ATPAVASDKV SLHAPLTLAE
     GDTLIQPSLA QYADVVSHQT THAASETLIF GHNRTHIFSQ VEPSSSDVNM HVLSTMSELP
     YALSSNVGSL QSFTVSYDSA EFVHDSVDVF RQDPLFSSYN NVLVHKPSSI LSQADTLLQP
     TRSLSSDMDW SEAYSGSESL LPDTDTLTVL NVSSSDSLDE ITYESSGFSD VNKVLQKGGV
     IYGDERELQI SSSLSEMAAN AESKVVPELS TSVSNDDVIK QNTSLQESPL PVSSTKGILP
     VSLAFPTTKI FDHDISKLTE RHLSVQPLHV TPPAFDDTLL KPVLSASSDQ ALSAPAYSKM
     LSSTQPYFYE TSATLNNEAL LQSSFQSSGD GTLLNTAVVP SDPILAESSR VHKDSSTFDQ
     ILHQMAPGSA TTETMLHSAS SPSVPDMLSN TFSKPTASLQ GLSVSYASEE YVSSSLFNRE
     DVMPSLYSSD VPLQLTSLEN TNAFPPQAAN AVTTAFLTGD TLPHVSTPAD SRISSSIFER
     REAASVSSSS ALGFDPVPMP AVVSDSDVSI HHTLPLPNVH ISVTAVPPKS EIPVTLSRLL
     VPSRESSGLS PSIVSSTDLW PSVVEDDYDE YDDGFPVSNC ISCTSHREAQ DMVVEEQDTK
     VNNDKDQSNL IISSHSEKPE EEKKISTAAS DSKINHATDR HNYTSVSTLT ASVVPKKHDD
     LTVLENHIQT ASVPLQNTSE SKSWAVFTSD EESGSGQGTS DSLNDNETST DFSFPDLNER
     DAEGAVEAGN SELSPGSSQS SASSVTSDHS SVFNISEAEF KHGLFQFSLT AEASNSSHES
     RIGLAESLES EKKTVIPLVV VSALTFICLV ILVGILIYWR KCFQTAHFYL EDNTSPRVIS
     APPAPIFPVS DDVGAIPIKH FPKHVADLHA SNGFSEEFEE IQSCTVDLGI TSDSSNHPDN
     KNKNRYINIV AYDHTRVKLA QLAEKDGKLT DYINANYVDG YNKPKAYIAA QGPLKSTAED
     FWRMIWEHNV EVIVMITNLV EKGRRKCDQY WPAEGSEEYG NFLVTQKSVH VLAYYTVRNF
     TLRNTKIKKG SQKGRSSGRI VTQYHYTQWP DMGVPEYTLP VLTFVRKASH AKRHAVGPVV
     VHCSAGVGRT GTYIVLDSML QQIQHEGTVN VFGFLKHIRT QRNYLVQTEE QYIFIHDALV
     EAILSKETEV LETHIHAYVN ALLIPGPTGK TRLEKQFKLL SQSNTQQCDY STALKQCNRE
     KNRTSSIIPV ERSRVGISSL SGEGTDYINA SYIMGYYQSN EFIITQHPLL HTIKDFWRMI
     WDHNAQLIVM LPDSQNMAED EFVYWPNKDE PINCESFKVT MIAEEHKCLS NEEKLIIQDF
     ILEATQDDYV LEVRHFQCPK WPNPDSPISK TFELISIIKE ETSNRDGPMI VHDEHGGVTA
     GTFCALTTLM HQLENENSVD VYHVAKMINL MRPGVFTDIE QYQFLYKAIL SLVSTRQEEN
     PSASMDSNGS ALPDGNAAES LESLV
//

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