ID A0A2K5K8L3_COLAP Unreviewed; 2468 AA.
AC A0A2K5K8L3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 13 {ECO:0000256|PIRNR:PIRNR000933};
DE EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000933};
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:ENSCANP00000037427.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000037427.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Regulates negatively FAS-induced apoptosis and NGFR-mediated
CC pro-apoptotic signaling. {ECO:0000256|PIRNR:PIRNR000933}.
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|PIRNR:PIRNR000933};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000933}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649,
CC ECO:0000256|PIRNR:PIRNR000933}.
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DR RefSeq; XP_011807182.1; XM_011951792.1.
DR Ensembl; ENSCANT00000060678.1; ENSCANP00000037427.1; ENSCANG00000042235.1.
DR GeneID; 105518703; -.
DR CTD; 5783; -.
DR OrthoDB; 2910505at2759; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd17195; FERM_F1_PTPN13; 1.
DR CDD; cd00992; PDZ_signaling; 5.
DR CDD; cd14597; PTPc-N13; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.42.10; -; 5.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011019; KIND_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR012153; PTPN13.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46900; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 13; 1.
DR PANTHER; PTHR46900:SF1; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 13; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00595; PDZ; 5.
DR Pfam; PF16599; PTN13_u3; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000933; Tyr-Ptase_nr13; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00750; KIND; 1.
DR SMART; SM00228; PDZ; 5.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 5.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS51377; KIND; 1.
DR PROSITE; PS50106; PDZ; 5.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000933};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR000933}; Hydrolase {ECO:0000256|PIRNR:PIRNR000933};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR000933};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 3..190
FT /note="KIND"
FT /evidence="ECO:0000259|PROSITE:PS51377"
FT DOMAIN 573..873
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 1075..1161
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1350..1435
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1483..1571
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1771..1852
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1866..1949
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 2196..2450
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 2372..2441
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 187..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1255..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1590..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1698..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1956..1975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2116..2152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 474..501
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 189..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1718..1733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2391
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-50"
FT BINDING 2361
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-51"
FT BINDING 2391..2397
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-51"
FT BINDING 2435
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-51"
SQ SEQUENCE 2468 AA; 274773 MW; 952D323AE4F02EF5 CRC64;
MHVSLAEALE VRGGPLQEEE IWAVLNQSAE SLQELFRKVS LADPAALGFI ISPWSLLLLP
SGSVSFTDEN ISSQDLRAFT APEVLQNQSL SSLSDVEKIH IYSLGMTLYW GADHEVPQSQ
PIKLGDHLNS ILLGMCEDVI YARVSVRTVL DACSAHIRNS NCAPSFSYVK HLVKLVLGNL
SGTDHLSCNS EQKPDRSQAI RDRLRGKGLP TGRSSTSDVL DIQKAPLSHQ TFLNKGLSKS
MGFLSIRDTQ DEEDYFKDIL SDNSGHEDSE NTRSTYQFKT SGPEKKPIPG ADVLSKKKIW
ASSMDLLCTA DRDFSSGETA SYRRCHPEAV TVRTSTTPRK KEARYSDGSI ALDIFGPQKM
DPIYHTQELP TSSAISSALD RIRERQKKLQ VLREAMNVEE PVRRYKTYHG DVFSTSSESP
SVISSESDFR QVKRSEASKR FESSSGLPEV DETLSQSQSQ RPSRQYETPF EGNLINQEIM
LKRQEEELMQ LQAKMALRQS RLSLYPGDTI KASMLDITRD PLREIALETA MTQRKLRNFF
GPEFVKMTIE PFISLDLPRS ILTKKGKNED NRRKVNIMLL NGQRLELTCD TKTICKDVFD
MVVAHIGLVE HHLFALATLK DNEYFFVDPD LKLTKVAPEG WKEEPKKKTK ATVNFTLFFR
IKFFVDDVSL IQHTLTCHQY YLQLRKDILE ERMHCDDETS LLLASLALQA EYGDYQPEVH
GVSYFRMEHY LPARVMEKLD LSYIKEELPK LHSTYVGASE KETELEFLKV CQRLTEYGVH
LHRVHPEKKS QTGILLGVCS KGVLVFEVHN GVRTLVLRFP WRETKKISFS KKKITLQNTS
DGIKHAFQTD NGKVCQYLLH LCSSQHKFQL QMRARQSNQD AQDIERASFR SLNLQAESVR
GFNMGRAIST GSLASSTLNK LAVRPLSVQA EILKRLSCSE LSLYQPLQNS SKEKNDKASW
EEKPREMSKS YHDLSQASFY PHWKNVLVNM EPPPQTVAEL VGKPSHQMSR SDAESLAGVT
KLNNSKSVAS LNRSPERRKH ESDSSSIEDP GQAYVLDVLH KRWSIVSSPE REITLVNLKK
DAKYGLGFQI IGGEKMGRLD LGIFISSVTA GGPADLDGCL KPGDRLISVN SVSLEGVSHH
AAIEILQNAP EDVTLVISQP KEKISKVPST PVHLTNGMKN YMKKSSYMQD SATDSSSKDH
HWSRGTLRHI SENSFGLSGG LREGSLSSQD SRTESASLSQ SQVNGFFVSH LGDQTWQESQ
HGSPSPSIIS KATEKKTSTD SNQSKTKKPG ISDATDYSDR GDSDMDEATY SSSQDHQTPK
KESSSSVNTS NKMNFKTFSS SPPKPGDIFE VELAKNDNSL GISVTGGVNT SVKHGGIYVK
AVIPKGAAES DGRIHKGDRV LAVNGVSLEG ATHKQAVETL RNTGQVVHLL LEKGQSPTSK
EHIPVTPQCA LSDQNAQGQG PEKVKKTTQV KDYSFVTEEN TFEVKLFKNS SGLGFSFSRE
DNLIPEQINA SIVRVKKLFP GQPAAESGKI DVGDVILKVN GASLKGLSQQ EVISALRGTA
PEVFLLLCRP PPGVLPEIDT ALLTPLQSPA QVLPNSSKDS SQPSCVEQST SSDENEMSDK
SKKHCKSPSR RDSYSDSSGS GEDDLVTAPT NISNSTWSSA LHQTLSSMVS QAQSHHESPK
SQEDTICTMF YYPQKIPSKP EFVDSNPSSP LPPDMAPGQS YQPQSESASS NSMDKYHIHH
ISEPTRQENW TPSKNDLENH LEDFELEVEL LITLIKSEKG SLGFTVTKGN QRIGCYVHDV
IQDPAKSDGR LKPGDRLIKV NDTDVTNMTH TDAVNLLRAA SKTVRLLIGR VLELPRIPML
PHLLPDIALT CNKEELGFSL SGGHDSLYQV VYISDINPRS IAATEGNLQL LDVIHYVNGV
STQGMTLEEV NRALDMSLPS LVLKATRNDL PVVPSSKRSA VSAPKPTKGN VSYSVGSCSQ
PALTPNDSFS MVDGEEINEI SYPKGKCSTY QIKGSPNLAL SKESYIQEDD IYDDPQEAEV
IQSLLDVVDE EAQNLLNQNN AAGNSCVPGT LKMNGKLSAE RTEDTDCNGS PLPEYLTEPT
KINGCEEYCE EKVKSESLIQ KSQEKKTDDD EITWESDELP TERTNHEDSD KDHSFLTNEE
LAVLPVVKVL PSGKYTGANL KSVIRVLRGL LDQGIPSKEL ENLQELKPLD QCLIGQTKEN
RRKNRYKNIL PYDATRVPLG DEGGYINASF IKIPVGKEEF VYIACQGPLP STVGDFWQMI
WEQKSTVIAM MTQEVEGEKI KCQRYWPNIL GKTTMVSNRL RLALVRMQQL KGFVMRAMTL
EDIQTREVRH ISHLNFTAWP DHDTPSQPDD LLTFISYMRH IHRSGPIITH CSAGIGRSGT
LICIDVVLGL ISQDLDFDIS DLVRCMRLQR HGMVQTEDQY IFCYQVILYV LTRLQAEEEQ
KQQPQLLK
//
