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Database: UniProt
Entry: H2ZXN2_LATCH
LinkDB: H2ZXN2_LATCH
Original site: H2ZXN2_LATCH 
ID   H2ZXN2_LATCH            Unreviewed;      2273 AA.
AC   H2ZXN2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRZ1 {ECO:0000313|Ensembl:ENSLACP00000002153.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000002153.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000002153.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   EMBL; AFYH01231332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01231333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01231334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01231335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01231336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01231337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01231338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01231339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01231340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01231341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7897.ENSLACP00000002153; -.
DR   Ensembl; ENSLACT00000002170.1; ENSLACP00000002153.1; ENSLACG00000001923.1.
DR   eggNOG; KOG0789; Eukaryota.
DR   GeneTree; ENSGT00940000155529; -.
DR   HOGENOM; CLU_001120_1_0_1; -.
DR   InParanoid; H2ZXN2; -.
DR   OMA; DPINCES; -.
DR   TreeFam; TF351978; -.
DR   Proteomes; UP000008672; 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   Reference proteome {ECO:0000313|Proteomes:UP000008672};
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        1595..1619
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..276
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
FT   DOMAIN          290..387
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1675..1950
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1867..1941
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1981..2240
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          2157..2231
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          592..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          648..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1498..1542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1498..1522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1523..1542
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2273 AA;  251864 MW;  591E32976DE11564 CRC64;
     FHRQHSKNKE QKFWISTGPL DQKNWGRKYP TCNGAKQSPI NIDDDLTQVN VNFRKLKFEG
     WEEESSENTF IHNNGKTVEI NLTNEYYVSG GGLISRFKAS RITFHWGKCN ASSDGSEHSL
     DGRKFPLEMQ IYCYDVDHVN TFDEAMKGHG KIKALSILFE IGVNDNSDYD AIISGVNSVS
     RFGKRAQLEP FVLFSLLPNS TEKYYTYNGS FTTPPCTEMV EWIVFKDTVT LSKSQLEVFC
     EILTMQKSGY VMVMDYVQNN FREQQYQFVG QVLSSYTGSE EIHEPVCSSE PENVQADPKN
     YTDMIVIWER PRVVYDAVIE NYAVFYQQLV GEDQSKHEIL TDGDQDTGAI LNNLLPNTSY
     VIQVVAVCAN GLYGRRSDQL IVDMPLDDPA EIDPFSDLNE TEDISNEMQV MFKKEEETAL
     DPEISASSET GLTEKLNVEV TKNISSASKD MKEKMGRKTG YEEDYNGQED SKNKLNFVLH
     SSTLPRTEPS SVKPLVVLYP KTKTVTTPNP VESISVSFKN KHFDTSMEHQ QINASVISKS
     IIETAVTSYE NVSSPTLPSE HAYVGSSGAN TTAFTNLTTE RSPLLEKTYS ENGTQQDLHM
     PVSSSSNDPT DTGISYNNVS ASFDIEISNK TISSAFDAQL VLHNHTSSSD AKKSLESNHT
     RTSSKISVPS TSSYSNGEMV PEGASSVDRE ILHNFTSGLS HEGALTHSAT SSSLQPFQHD
     SASADRSTVL SQTTQPVFNG EISPQSSYNS DTLLLVTPLL SDNQMLLKAT PIASDVELVL
     HATSVFPTVD VLPQPTPSSS SDAYLLKSSS ASFNSEVSLH IYTTFESQAL LKATPAVTSG
     KVSLHAALVL SDGDALVQPT LTLSPDVASH QTTSPASETF MFGHRLDIFE ESETLPQVSP
     FSNDFRVHAT QELPKGDTFI KPSLTLSSEV IFLQSFPASS DSASFVSDSG GIFLQVTPFV
     SHTDLLMNEA SALSKASAVL QRTTSLPSDK FFGDIPISCG SELLFSRPGS FKEGQLVPMV
     TSSISLDKLT CISSELVDVD MLNQPTCTLC GDNSLLQVSS VSASEMVSYD TIAPNKSRVM
     PEHIFSVQHK YTAFESYNDL LIQTTLDVLL KTIFATSELH LSATQELAQG ISATLTDDVF
     LAPTLQSSDE DTLFKPNLTF TVSTKTASVV KDSKLFLDSA NEYEKSLFED KTILHAASVL
     PTIDCIASLQ DLTASLHIET PFPTIFSSSA NLLKATVDDY NNVLHQTTPF ESMMQPHSTS
     VFSYPILQKY ATPAFTNDET LMSTAASIDN IVYNDIVPPS TSSNSLSNGI LFYVPSDFSQ
     KALSVNPTLP LLNSNMYISV TAVPPISESP VTIALSPAPL EHSSVTSSNS SHDGLWPSVL
     EGSLLIKNDT ASVLHAETML LEDSSAKTYN ITKNLTSHYL SVKSRPSGAF EEERFTTNAS
     FYHRNTDMDK TNDPVSTSVS VIMSSQNTNM TVLEKQNQTV INPVKFTKDP TSWAFVASDE
     ESGSGQSTSD NLNDNETSTD FSLPDYSERE SHGTGTAEDL HITKFKPRSA TPIKSHTVGH
     KNVSSSIISV TEASNSSHES RIGAAEGLET ERKTLIPLVI VSALTFICLV VLIAILIYWR
     KCFQTAHFYL EDNTSPRVIS TLAAPIISVS GVDVESISLK LFPKHVTNLH TKKGFTEEFE
     TLKEFYEEIQ SCTVDLGITS DNSNHPDNKN KNRYINIVAY DHSRVKLAHL TEKDGKRTDY
     INANYVDGYN KQRSYIAAQG PLKSTAEDFW RMVWEHNVEI IVMITNLVEK GRRKCDQYWP
     SENSEEYGSF LVTLKTAKVL AYYTVRHFTV RNTKLKKGSQ KGRRNERIVT QYHYTQWPDM
     GVPEYVLPLL TFVRKSSAAR SSEMNPVIVH CSAGVGRTGT YIVVDSMLKQ IRLEGTVNVL
     GFLKHIRTQR NYLVQTEEQY VFIHDALVEA ILSKETEVLA SHIHAYVNAL LTPGPSGKTS
     LEKQFKLLSQ SNVKQCDYSA ALKQCNREKN RSSSVIPVER SRVRLSSVAG EGVDYINASY
     IKGYHHSSEF IITQHPLLHT TKDFWRMIWD HNAQVIVMLS DNQNLAENEC VYWPSKEEPM
     NCEGFTVSMI SEDCMCLSNE ENLIIQDFIL EAMQDDYVLE VKHYQCPKWP NPDSPISKTF
     ELINIIKEEA TTKDGPVIVH DEHGGVTAGT FCALTTLVHQ LESENSIDVY QTTKMINLMR
     PGVFTDIEQY QFLYKAILSL VGTREEENPA TTVDSSAVLV DGNNAAESLE SLV
//
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