ID A0A2I2Z636_GORGO Unreviewed; 2294 AA.
AC A0A2I2Z636;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 13 {ECO:0000256|PIRNR:PIRNR000933};
DE EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000933};
GN Name=PTPN13 {ECO:0000313|Ensembl:ENSGGOP00000042460.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000042460.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000042460.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000042460.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000042460.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; CABD030031842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030031843; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030031844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030031845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030031846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030031847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030031848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030031849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030031850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030031851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_018881246.1; XM_019025701.1.
DR Ensembl; ENSGGOT00000043687.1; ENSGGOP00000042460.1; ENSGGOG00000025765.2.
DR GeneTree; ENSGT00940000155133; -.
DR OrthoDB; 2910505at2759; -.
DR Proteomes; UP000001519; Chromosome 4.
DR Bgee; ENSGGOG00000025765; Expressed in testis and 6 other cell types or tissues.
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; 2.
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:UP000001519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 3..190
FT /note="KIND"
FT /evidence="ECO:0000259|PROSITE:PS51377"
FT DOMAIN 572..872
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 902..988
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1177..1262
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1310..1398
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1597..1678
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1692..1775
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 2022..2276
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 2198..2267
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 186..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1780..1805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1885..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 473..500
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 447..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2217
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-50"
FT BINDING 2187
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-51"
FT BINDING 2217..2223
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-51"
FT BINDING 2261
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-51"
SQ SEQUENCE 2294 AA; 255801 MW; FABD30CDDA0E5681 CRC64;
MHVSLAEALE VRGGPLQEEE IWAVLNQSAE SLQELFRKVS LTDPAALGFI ISPWSLLLLP
SGSVSFTDEN ISNQDLRAFT APEVLQNQSL TSLSDVEKIH IYSLGMTLYW GADYEVPQSQ
PIKLGDHLNS ILLGMCEDVI YARVSVRTVL DACSAHIRNS NCAPSFSYVK HLVKLVLGNL
SGTDQLSCNS EQKPDRSQAI RDRLRGKGLP TGRSSTSDVL DIQKPPLSHQ TFLNKGLSKS
MGFLSIKDTQ DEDYFKDILS DNSGHEDSEN TCSPYQFKTS GPEKKPIPGI DVLSKKKIWA
SSMDLLCTAD RDFSSGETAT YRRCHPEAVT VRTSTTPRKK EARYSDGSIA LDIFGPQKMD
PIYHTRELPT SSAISSALDR IRERQKKLQV LREAMNVEEP VRRYKTYHGD AFSTSSESPS
IISSESDFRQ VRRSEASKRF ESSSGLPGVD ETLSQGQSQR PSRQYETPFE GNLINQEIML
KRQEEELMQL QAKMALRQSR LSLYPGDTIK ASMLDITRDP LREIALETAM TQRKLRNFFG
PEFVKMTIEP FISLDLPRSI LTKKGKNEDN RRKVNIMLLN GQRLELTCDT KTICKDVFDM
VVAHIGLVEH HLFALATLKD NEYFFVDPDL KLTKVAPEGW KEEPKKKTKA TVNFTLFFRI
KFFMDDVSLI QHTLTCHQYY LQLRKDILEE RMHCDDETSL LLASLALQAE YGDYQPEVHG
VSYFRMEHYL PARVMEKLDL SYIKEELPKL HNTYVGASEK ETELEFLKVC QRLTEYGVHF
HRVHPEKKSQ TGILLGVCSK GVLVFEVHNG VRTLVLRFPW RETKKISFSK KKITLQNTSD
GIKHAFQTDN SKICQYLLHL CSYQHKFQLQ MRARQSNQDA QDIDVLHKRW SIVSSPEREI
TLVNLKKDAK YGLGFQIIGG EKMGRLDLGI FISSVAPGGP ADLDGCLKPG DRLISVNSVS
LEGVSHHAAI EILQNAPEDV TLVISQPKEK ISKVPSTPVH LTNEMKNYMK KSSYVQDSAI
DSSSKDHHWS RGTLRHISEN SFGLSGGLRE GSLSSQDSRT ESASLSQSQV NGFFASHLGD
QTWQESQHGS PSPSVISKAT EKETFTDSNQ SKTKKPGISD ATDYSDRGDS DMDEATYSSS
QDHQTPKQES SSSVNTSNKM NFKTFSSSPP KPGDIFEVEL AKNDNSLGIS VTGGVNTSVR
HGGIYVKAVI PQGAAESDGR IHKGDRVLAV NGVSLEGATH KQAVETLRNT GQVVHLLLEK
GQSPTSKEHV LVTPQCTLSD QNAQGQGPEK VKKTTQVKDY SFVTEENTFE VKLFKNSSGL
GFSFSREDNL IPEQINASIV RVKKLFPGQP AAESGKIDVG DVILKVNGAS LKGLSQQEVI
SALRGTAPEV FLLLCRPPPG VLPEIDTALL TPLQSPAQVL PNSSKDSSQP SCVEQSTSSD
ENEMSDKSKK QCKSPSRRDS YSDSSGSGED DLVTAPANIS NSTWSSALHQ TLSNMVSQAQ
SHREAPKSQE DTICTMFYYP QKIPNKPEFE DSNPSPLPPD MAPGQSYQPQ SESASSSSMD
KYHIHHISEP TRQENWTPLK NDLENHLKDF ELEVELLITL IKSEKGSLGF TVTKGNQRIG
CYVHDVIQDP AKSDGRLKPG DRLIKVNDTD VTNMTHTDAV NLLRAASKTV RLVIGRVLEL
PRIPMLPHLL PDITLTCNKE ELGFSLCGGH DSLYQVVYIS DINPRSVAAI EGNLQLLDVI
HYVNGVSTQG MTLEEVNRAL DMSLPSLVLK ATRNDLPVVP SSKRSAVSAP KSTKGNGSYS
VGSCSQPALT PNDSFSTVAG EEINEISYPK GKCSTYQIKG SPNLTLSKES YIQEDDIYDD
SQEAEVIQSL LDVVDEEAQN LLNENNAAGN SCGPGTLKMN GKLSEERTED TDCDGSPLPE
YFTEATKMNG CEEYCEEKVK SESLIQKSQE KKTDDDEITW GNDELPIERT NHEDSDKDHS
FLTNDELAVL PVVKVLPSGK YTGANLKSVI RVLRGLLDQG IPSKELENLQ ELKPLDQCLI
GQTKENRRKN RYKNILPYDA TRVPLGDEGG YINASFIKIP VGKEEFVYIA CQGPLPTTVG
DFWQMIWEQK STVIAMMTQE VEGEKIKCQR YWPNILGKTT MVSNRLRLAL VRMQQLKGFV
VRAMTLEDIQ TREVRHISHL NFTAWPDHDT PSQPDDLLTF ISYMRHIHRS GPIITHCSAG
IGRSGTLICI DVVLGLISQD LDFDISDLVR CMRLQRHGMV QTEDQYIFCY QVILYVLTRL
QAEEEQKQQP QLLK
//
