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Database: UniProt
Entry: G3SUI0_LOXAF
LinkDB: G3SUI0_LOXAF
Original site: G3SUI0_LOXAF 
ID   G3SUI0_LOXAF            Unreviewed;      2310 AA.
AC   G3SUI0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 82.
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:ENSLAFP00000003815.4};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000003815.4, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000003815.4, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003815.4,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000003815.4}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003815.4};
RG   Ensembl;
RL   Submitted (JUL-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   STRING; 9785.ENSLAFP00000003815; -.
DR   Ensembl; ENSLAFT00000004571.4; ENSLAFP00000003815.4; ENSLAFG00000004565.4.
DR   eggNOG; KOG0789; Eukaryota.
DR   GeneTree; ENSGT00940000155529; -.
DR   InParanoid; G3SUI0; -.
DR   OMA; DPINCES; -.
DR   TreeFam; TF351978; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0072534; C:perineuronal net; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
DR   GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; IEA:Ensembl.
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|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..2310
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003454530"
FT   TRANSMEM        1633..1657
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          36..300
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
FT   DOMAIN          314..411
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1712..1987
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1904..1978
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          2018..2277
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          2194..2268
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          472..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1403..1518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1538..1600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1435..1471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1478..1497
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1538..1564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1584..1600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2310 AA;  254048 MW;  CCFBABB59648CE21 CRC64;
     MQILKCFLAC IQLLCVCRLD WAYGYYRQQR KLVEEIGWSY TGALNQKNWG KKYPVCNSPK
     QSPINIDEDL TQVNVNLKKL KFQGWDKPSL ENTFIHNTGK TVQINLTNDY RLSGGVSEMV
     FKASKITFHW GKCNMSSDGS EHSLEGQKFP LEMQIYCFDA DRFSSLEEAV KGRGRLRALS
     ILFEVGIEEN LDYKAIIDGV ESVSRFGKQA VLDPFILLNL LPNSTDKYYT YNGSLTSPPC
     TDTVDWIVFK DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY
     TGKEEIHEAV CSSEPENVQA DPENYTSLLV TWERPRVVYD TMIEKFAVLY QQLEGDDQTK
     HEFLTDGYQD LGAILNNLLP NMSYVLQIVA VCTNGLYGKY SDQLIVDMPS NDLGKCLPGV
     PLIFFCFSKE EGEGKEIEED TIVNPGRDST TNQIRKKEPQ IPTTTNYNRV GTKYNEAETN
     RSPTRGGEYS GKGDVPNTFL NSTSQTATEL VPGKDTSSAS QTVTQQPRHT VEGTSASLND
     SSKTVVRYPQ MNLSGTVEAL NTVSITESPE VSTDISEEEN LLPGFKLDTE ADGSSGSSPT
     TSAIPFVSEN PEAITNDVLI PETMRNASED SVSSGLEESL KDPSTDGNMW FLSTTDETTE
     HDVGSGTERF RQTNYSEVHI DESEKTTESF SLGPLGSQVP SVTDTEMPHY STLAYFPTEV
     TPHAFTPSYG QHDSVPTVNM VPLQTTQPVH NGETPPQPSY SSEVFPLVTP LLLDNQILNT
     TPAASSSDSA LHATPVFPSV DVSFDSILSS YDGAPLLPFF SASFSSELSH HLYTASQILP
     QVTSALESDK VSPHASLPVA GGDLVLEPSL AQYSDVVSHQ STAHAASETL EFGSEAGVLS
     KTLMFSQVEP GSADVVMHAR SPGPELSHAL SDNKGSQYIS TVSHGSAIPV HDSVDVSHQG
     SLFSSPSHVL MPKSSLIAPT AALLQPTRAL SDDVEWSGAS SGSEFLLPDT DGLTVLNISS
     PVSVAEFTYT TSVFGDNKRL PKSDIISGNE TELPISSFSE MIYHSESTVI PDPYENVNNL
     SASLQETPTF ISSTKGVLPE SLACTITKVF DHEISQTPEN NFALQPTHAV SQTFGDTLLK
     PVLSATSEPA LSDPASSEIS PSTQLFLYEA SASFNTEALL QAPFQASDVD TLLKTALPAV
     PSDPVLAETP KVDKISSTIL HLIASDSALS KNMQHSTSVP VFDVLPTSSK QSTSLQGVTI
     SYASKKYLER VLLKSESPQQ VVPPLYSNNE LFQTANWHIS HAFPPQGRHT FATPVLSVDT
     LLTTPVNKLV YSDDVFTSTK ISITDEVFAG IPTAVSDTLV SADDSVPVGN EYVSITAISP
     TRGGSLITVK SLFPSKTTAE LTHSASSGAD LVGGGDMDDD DDDDGDRDSD GLTIHKCMSC
     SSSRQSQEKV TNDSDTQDNS LVHQDNLVSH SLSENSEEEQ KVTGVTSDSQ TGMDRSPDKT
     PRINVLPSKH NDAKEENDIQ TGSALFPFTP ESKSWAVLTS DEESGSGQST SDSLNDNETS
     TDFGFPDMTE RDADGVLEAG DSEMTAGSPQ SSAASVTSGH AEMFSVSEAE ASNSSHESRI
     GLAEGLESEK KTVIPLVIVS ALTFICLVVL VGILIYWRKC FQTAHFYLED STSPRVISTP
     PTPIFPISDD VGAIPIKQFP KHVADLHASS GFTEEFETLK EFYQEVQSCT VDLGITADSS
     NHPDNKHKNR YINIVAYDHS RVKLAQLAEK DGKLTDYINA NYVDGYNRPK AYIAAQGPLK
     STAEDFWRMI WEHNVEVIVM ITNLVEKGRR KCDQYWPVDG SEEYGNFLVT QKSVQVLAYY
     TVRNFTVRNT KIKKGSQKGR PSGRVVTQYH YTQWPDMGVP EYSLPVLTFV RKASHAKRHA
     VGPVVVHCSA GVGRTGTYIV LDSMLQQIHH EGTVNIFGFL KHIRSQRNYL VQTEEQYVFI
     HDALVEAILS KETEVPDSHI HAYVNALLIP GPTGKTKLEK QFKLLSQSNI QQSDYSTALK
     QCNREKNRTS SIIPVERSRV GISSLSGEGT DYINASYIMG YYQSNEFIIT QHPLLHTIKD
     FWRMIWDHNA QLVVMLPDGQ NMAEDEFVYW PNKDEPINCE SFKVTLMAEE HKCLSNEEKL
     IIQDFILEAT QDDYVLEVRH FQCPKWPNPD SPISKTFELI SVIKEEAANR DGPMIVHDEH
     GGVTAGTFSA LTTLMHQLEK ENSMDVYQVA KMINLMRPGV FADIEQYQFL YRAILSLVST
     RQEENPSISL DSNGTALPDG NIAESLESLV
//
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