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
//