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Database: UniProt
Entry: A0A2D0RZB2_ICTPU
LinkDB: A0A2D0RZB2_ICTPU
Original site: A0A2D0RZB2_ICTPU 
ID   A0A2D0RZB2_ICTPU        Unreviewed;      1385 AA.
AC   A0A2D0RZB2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=ca16b {ECO:0000313|RefSeq:XP_017335834.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017335834.1};
RN   [1] {ECO:0000313|RefSeq:XP_017335834.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017335834.1};
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   -!- 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   RefSeq; XP_017335834.1; XM_017480345.3.
DR   Ensembl; ENSIPUT00000036891; ENSIPUP00000035495; ENSIPUG00000023782.
DR   GeneID; 108272134; -.
DR   KEGG; ipu:108272134; -.
DR   CTD; 569183; -.
DR   OrthoDB; 2903434at2759; -.
DR   Proteomes; UP000221080; Chromosome 11.
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   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:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA; 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|RefSeq:XP_017335834.1};
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..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1385
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013243213"
FT   TRANSMEM        712..737
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          52..315
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
FT   DOMAIN          344..443
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          794..1061
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          981..1052
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1092..1350
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1267..1341
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          525..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..558
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..602
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1385 AA;  156594 MW;  72613E2FD65F3C7D CRC64;
     MSVRNPHRSG LLCWGLSVLL IQSISSHPAA APPRMKHGKM SNQREKRAAG EPYWAYSGMH
     GPWRWASMYP ECGEKNQSPV NIPDEHAWVS QECQELTLEG FEVKSSNKTS MKNTGKTVAI
     LLKNDYFVRG AGLPGRFKAE KVEFHWGLSN GSAGSEHSIN GKRFPVEMQI FFYNSDDFDS
     LNTAIKERRI IAAMAVFFQV GKKNNVAAEP IIAGLKRVVH HEKETNLAPF VLRDLLPSSL
     GSYYRYAGSL TTPPCSKVVE WIILSRPVYL SYHQLEAFYS IFTTEQQDHV KSVEYLRNNF
     RPTQDLHNRR VVKSAVKDAW FPDPMTDGHT SSTDTEPSRV CSSIPDNMKV RPLNRTAMVL
     TWDRPSTIYH PPLVGFLVTY SWVKDDVTIE KMFTQSSEHH TRAVITHMSP DALYLFRVQA
     LCQRDQRSDF SQTLLFKANT TRIFEGTRII KTGMPTVSSS SDMAPISSGS STWSSSGLPF
     SFVSIATGMG PPSSGGQTTM ASLVTSTLLA GLGFSGGVIS SLPGSLWPTH SPSSGPAPTR
     QPASPTSETT QNGNRPLPSE EGELTEELNK EEHKQEEDEE DDNEGERVEE KKKKEKNVTV
     NEKKQEQTTL QEPADSVSPS GARGREGGLV NTEISTVSPI APEEKIYTVT LRPSRGDLSQ
     TTWLQENYTT DMQLASSPTQ AIKLTNKEIH TERNSKLLVS REPASSVNRM EWIIPLMVVS
     ALTLLCLIML LAVLVYWRKF FQTTHMYIED RNSPQVIHNE SLTGFLIADD LEALSVRQFI
     KHVMELYSNN QQGFSQEFND IQHSVGDIEI TAEHSNHPDN KHKNRYINIV AYDHSRVKLQ
     PLAGKDSKHT DYINANYVDG YNRPRAYIAA QGPLKSTFED FWRMIWEQSI SVIVMITNLV
     EQGRRKCDQY WPSENTEEYG SIVVTLKSTK MLAWYTLRHF LIRNTRVTKS QKGRQNERLV
     IQYHYTQWPD MGVPEYTLPV LTFISRSSAA RAPKSGPVLV HCSAGVGRTG TYIVIDSMLQ
     QIKDKGMVNV LGFLKHIRTQ RNYLVQTEEQ YVFIHDALME AMLGKNTEVP ACKLHSYVNN
     ILTLSPSGTT HIEKQFKLVM QCNIQKCFSA QKDCNKVKNR NSSVVPSEQA RVLLSPLRGM
     KGTDYINASY ITGYYRSNEF IITQHPLPHT TMDFWRMIWD HNVQVIIMLP DNLSLTEDEF
     VYWPSREQPM NCAAFTVTLI NTDTLCLCDE QQIIIHDFIL EATQDDYVLE VRHFQCPNWP
     ELTGPVSNTF ELINIIKEEA MTRDGPTIVH DEFGGVSAGM LCALTTLYQQ LEIESAVDVY
     QVAKMINLMR PGVFTDIEHY QYLYKAMLSL VGSTDSEIFC SYMGRHGRIL KTDKANPSES
     MESLV
//
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