ID A0A3Q0SYM7_AMPCI Unreviewed; 2478 AA.
AC A0A3Q0SYM7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000026788.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000026788.1}
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 STRING; 61819.ENSACIP00000026788; -.
DR Ensembl; ENSACIT00000027487.1; ENSACIP00000026788.1; ENSACIG00000020479.1.
DR GeneTree; ENSGT00940000155133; -.
DR OMA; ESPPHTI; -.
DR Proteomes; UP000261340; 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; cd13187; FERM_C_PTPH13; 1.
DR CDD; cd17195; FERM_F1_PTPN13; 1.
DR CDD; cd00992; PDZ_signaling; 6.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.42.10; -; 6.
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; 6.
DR Pfam; PF16599; PTN13_u3; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000933; Tyr-Ptase_nr13; 4.
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; 6.
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; 6.
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; 6.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 3..182
FT /note="KIND"
FT /evidence="ECO:0000259|PROSITE:PS51377"
FT DOMAIN 579..878
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 1072..1158
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1343..1433
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1460..1548
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1730..1810
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1824..1907
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1959..2039
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 2211..2465
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 2387..2456
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 189..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1642..1662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2084..2125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 489..516
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 253..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2084..2102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2406
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-50"
FT BINDING 2376
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-51"
FT BINDING 2406..2412
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-51"
FT BINDING 2450
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-51"
SQ SEQUENCE 2478 AA; 274237 MW; 7687F5311911835B CRC64;
MHVSLAEALE VRGGPLQEEE VWAVLSQSAE SLQELFHKGR NPSAMGFIIS PWSLLLMPSG
NISFADEYVT QQDLRAFTAP EVLEGNSLAS VSDIEKTYHL YWQADLPYMH SPPMELGEHL
NSLLLNMCDD VTLSRMSLRT VLDISSKHIR NSSCDPPFSY IRKLVRTVLG SLSQLDGLLT
DRESLPERSK EIRERLRGKG LPSGRSAAPR VLERYRAKTQ EQISLNRGLS RSMGSLPIQD
LLKGDEGAAL QYSLSDYHTN SDSPTELYPK PPSLHSQRSY PYLHPFHPQQ KGRPVELDRR
SLPFYSGELG PSQPRKTWAS SVDLACIDPE ALRFGALEDA RRGSSALSTH SSGRRKSPLQ
VSRERDSRYL EFGGLKSRKP HHHSALSVGS GITGAYDKIK EKQRKLQALR QAVDDPVHTH
HRYHSDYSSS SESPSLASSD PDYRQAQNPT PTDNGFLSAF RQYQTLLTPI LILLSFPCRQ
NEGGADEALV GAELLLQRQE EEVQRLQAHM ARRLSRANLY PTDDPLAPSH PSMLELQDPL
YTSSNFHGPE FVKMASEPCT SLSVPSSIMK RGKVEEVQRK VGVVLLNGQK LELSCDIKAV
CKDVLDMVVA HIGLVEHHLF GLAYLKDNEF FFVDLDAKLS KVAPEGWKEE PKKRRSDVLF
NLFFRIKFFL DDINLIQHAM TKHQYYLQLR KDILEERMRC GTEDAMLLAS LALQAEFGDY
QPELHGKTYF RMEHYLPVSV LDKVDQTTIR ENLPKLHTNY YGATESEAEF EFLKVSQRLI
EYGVHFHRVL PEKRSQTGIM LGVFSKGVLI FEVLNGNRTP VLRFPWRETR KISFAKKKIC
LQNTSDGIKH LFQTDSNKTC QYLLQLCSDQ HKFHLQMKAR QNNQELQDLE NSLQYSLDSR
SSLGPSLSTR SNPDQLKRIS YSEAALNKAL SGSVLVQDEL HFPGFNPAAS TVLSNPRAMS
RSHHNLGQMP ESPEHRMAES YRGQSHSRLS QPQPNQLASH FQQHQRASSD TDSILHQQDN
KSKKESDSSS IEDTGQAYVL GKNAGLCSVV HSINSLKKKV NALPSPEREI TSVNLKKDVK
YGLGFQVVGG ENSGRADLGT IISSITPGGP ADVNGCLKPG DRLISVNEKN LEGLSHTVVV
DILQNAPDDV TLVVSQPKER LYKESAAGYA PYQPKSSFNS TQTRELDVDT SSEEHTGTRS
PSPPHLSAGI LSSISSPAQQ HTTLSSQDSR TSVVAKNNQA PASGVQQCLE RATAAVKTAP
TAQRQRPDTN VGPDPTPPAL PPKTRKSKVL EAPKVSEHSD RGDSDMDEET SSSQEKQKVK
KVWSLLFASV CWVNSLHPGE LYDIELSKKD SSLGLSVTVL FGKGGAGTTV RHGGIYVKGL
IPKGAAELDG RIQKGDRVLA VDGKSLEGAT HEQAVEALRD TGQTVHLLLE RGHLPANSIH
APLTPQSTPP SAGKVNNVFE VPLLKNTSGL GFSFSREENI PNEPPGSSMV RVKKLFPGQP
AAESGRIKVG DVIMRVNQTP LKGLSQHEVI SALRGTGQEV ILLLCRPEHG ILPEMDTAAL
TPKPSPRKEP VGLAEPSLNL GRLNSPPGSK KQGPVEEALE RLLHRTPGRR NSYSDSTDGD
EEVEEAFSAG TLENIRQNWE RGVYQNSSTN PGLRRYDSSG PLDDNIHSAF YSPXLSMTRS
DLSNRGLSSP MADDLESGTL LKVSSLSAPS PDPLPPPLPL PLNLTEVELQ VSLVKSEKGS
LGFTLTEGND HGCYIHDIIQ DPAKEDGRLR PGDRMIMVNN TNVSNMGHTE VVSLVRAAPR
VVDLVVGRVL ELPKPPIEAH LLPDICFKRN QEPLGLVLDG GGDSLYGILF VKDILLGSLA
FKEGSLRPLD LIHYINGAPT QDLTLSESTR LLEHSPSELT LKATRDGKPV SPMQKSLSFL
NNNVGAKHSS SMNGFLKGEE LRDTEGLAAL CPLEEELIKV DLEKPLTGGL GFSVIGGERG
IFVKSITPGG VAESSGNLQV GDRLLKVNEE LMTGVSHTKA VTTIRKTKGL VHLIVSRPPD
QNPNTYLASL PINSDKCNGN TGLSGDSGVK ATLCPVIPPI DYDGALEEKR ETERRAELSE
DTDCDGSSLP EDSPKNSRKV RWTEETVDDP RNENYLQMSA GQPDEDEITW GSDELPIEDM
NSESRDDGPI ITEDELTSLP LVRVVPDGQY TGQKLNSVVR MMRGLLEQKV PLQEFENLQN
LQPLDDCLIG QTKENKKKNR YKNIVPFDTT RVVLGKDGGY INANFINMSV KDENFMYIAC
QGPLPTTLGD FWQMVWEQKS NVIAMMTQEV EGGKVKCQRY WPDTPRTAEM VDDRLQITLI
RDQHLDNFVI RLIEVKDVQT NEAQVVTHLN YTGWPDHGTP SQPEQLLTFI SYMRHVHRSG
PIITHCSAGI GRSGTLICID VVLGLISKDA DFDISDVVRN MRLQRQGMVQ TEDQYIFCYQ
VILYVLRCLQ AEENISGQ
//