ID A0A2K5HYB5_COLAP Unreviewed; 2279 AA.
AC A0A2K5HYB5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, 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};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000009365.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000009365.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSCANT00000032236.1; ENSCANP00000009365.1; ENSCANG00000027798.1.
DR Proteomes; UP000233080; Unplaced.
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:UP000233080};
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 1608..1633
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..283
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT DOMAIN 297..396
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1688..1956
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1873..1947
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1987..2246
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 2163..2237
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 445..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1514..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1404
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2279 AA; 250961 MW; C2486C853F0F6163 CRC64;
MEFLFRLMKI QQRKLVEEIG WSYTGALNQK NWGKKYPTCN SPKQSPINID EDLTQVNVNL
KKLKFQGWDK TSLENTFIHN TGKTVEINLT NDYRVSGGVS EMVFKASKIT FHWGKCNMSS
DGSEHSLEGQ KFPLEMQIYC FDADRFSSFE EAVKGKGKLR ALSILFEVGT EENLDFKAII
DGVESVSRFG KQAALDPFIL LNLLPNSTDK YYVYNGSLTS PPCTDTVDWI VFKDTVSISE
NQLAVFCEVL TMQQSGYVML MDYLQNNFRE QQYKFSRQVF SSYTGKEEIH EAVCSSEPEN
VQADPENYTS LLVTWERPRV VYDTMIEKFA VLYQQLDGVD QTKHEFLTDG YQDLGAILNN
LLPNMSYVLQ IVAICTNGLY GKYSDQLIVD MPTDNPGKYQ GKDVEEDTVV NPGRDSATNQ
IRKKEPQIST TTHYNRIRTK YNEAKTNRSP TRGSEFSGKG DVPNTSLNST SQSVTKLATE
KDISLTSQTV TELPAHTVEG TSASLNDGSK TVLRSPHMNL SGTVESLNTV SITEYEEESL
LTSFKLDTGA EDSSGSSPAT SAIPFISENI SQGYIFSSEN PETITYDVLI PESARNASED
STSSGSEESL KDPSVEGNVW FPSFTDVTAQ PDVGSGRESF LQTNYTEIRV DETEKTTKSF
SAGPVMSQGP SVTDLEMPHY STFAYFPTEV TPHAFTPSSR QQDLVSTVNV VRSQTTQPVY
NGETPLQPSY SSEVFPLVTP LLLDNQILNT TPAASSSDSA LHATPVFPSV DVSFESILSS
YDGAPLLPFS SASFSSELFR HLHTVSQILP QVTSATESDK VPLHASLPVA GGDLLLEPSL
VQYSDVLSHL TTTHAASETL EFGSESGVLY KTLMFSQVEP PSSDAMMHAR SSGPEPSYAL
SNNEGSQHIF TVSYSSAIPV HDSVGVTYQG SLFSGLSHIP IPKSSLITPT ASLLQPTHAL
SGDGEWSGDS SDSEFLLPDT DGLTALNISS PVSVAEFTHT TSVFGDDNKA LSKSEIIYGN
ETERQIPSFN EMVYPSESTV MPNMHDNVNK LNASLQETSV SISSTKGMFP GSLAHTTTKV
FDHEISQVPE NNFSVQPTHT VFQASGDTSL KPVLSANSEP ASSDPASSEM LSPSTQLLFY
ETSASFSTEV LLQPSFQASD IDTLLKTVLP AVSSDPILVE TPKVDKISST ILHLIVSNSA
SSENVLHSTS VPGFDVSPTS HMHSASLQGL TISYASEKYE PILFKSESSH QVVPSLYSND
ELFQTANLEI KQAYPPKGRH EFATPVLSID EQLNTLINKF IHSDEILTST KSSVTDKVFA
GIPTVASDMF VSTDHSVPIG NGHVAITAVS PNRDGSVTTT KLLFPSKATS ELSHSARSDA
DLVGGGEDGD TDDDDGDDDD DDRDSDGLSI HKCMSCSSYR ESQEKVMNDS DTHENSLMDQ
NNPVSHSLSE NSEEDNRVTS VSSDSQTGVD RSPGKSPSAN GLSQKHNDGK EENDIQTGSA
LLPLSPESKA WAVLTSDEES GSGQGTSDSL NENETSTDFS FPDTNEKDAD GILAAGDSEI
TPGFPQSPTP SVTSENSEVF HVSEAEASNS SHESRIGLAE GLESEKKAVI PLVIVSALTF
ICLVVLVGIL IYWRKCFQTA HFYLEDSTSP RVISTPPTPI FPISDDVGAI PIKHFPKHVA
DLHASSGFTE EFEEVQSCTV DLGITADSSN HPDNKHKNRY INIVAYDHSR VKLAQLAEKD
GKLTDYINAN YVDGYNRPKA YIAAQGPLKS TAEDFWRMIW EHNVEVIVMI TNLVEKGRRK
CDQYWPADGS EEYGHFLVTQ KSVQVLAYYT VRIFSLRNTK IKKGSQKGRP SGRVVTQYHY
TQWPDMGVPE YSLPVLTFVR KAAYAKRHAV GPVVVHCSAG VGRTGTYIVL DSMLQQIQHE
GTVNIFGFLK HIRSQRNYLV QTEEQYVFIH DTLVEAILSK ETEVLDSHIH AYVNALLIPG
PTGKTKLEKQ FQLLSQSNIQ QSDYSTALKQ CNREKNRTSS IIPVERSRVG ISSLSGEGTD
YINASYIMGY YQSNEFIITQ HPLLHTIKDF WRMIWDHNAQ LVVMIPDGQN MAEDEFVYWP
NKDEPINCES FKVTLMAEEH KCLTNEEKLI IQDFILEATQ DDYVLEVRHF QCPKWPNPDS
PISKTFELIS VIKEEAANRD GPMIVHDEHG GVTAGTFCAL TTLMHQLEKE NSMDVYQVAK
MINLMRPGVF ADIEQYQFLY KVILSLVSTR QEENPSTSLD SNGAALPDGN IAESLESLV
//
