ID A0A1S3LU47_SALSA Unreviewed; 2528 AA.
AC A0A1S3LU47;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Tyrosine-protein phosphatase non-receptor type 13 isoform X1 {ECO:0000313|RefSeq:XP_013994391.1, ECO:0000313|RefSeq:XP_013994392.1};
GN Name=ptpn13 {ECO:0000313|RefSeq:XP_013994391.1,
GN ECO:0000313|RefSeq:XP_013994392.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013994391.1};
RN [1] {ECO:0000313|RefSeq:XP_013994391.1, ECO:0000313|RefSeq:XP_013994392.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013994391.1,
RC ECO:0000313|RefSeq:XP_013994392.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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DR RefSeq; XP_013994391.1; XM_014138916.1.
DR RefSeq; XP_013994392.1; XM_014138917.1.
DR GeneID; 106568503; -.
DR KEGG; sasa:106568503; -.
DR CTD; 5783; -.
DR OrthoDB; 2910505at2759; -.
DR Proteomes; UP000087266; Chromosome ssa13.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13187; FERM_C_PTPH13; 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; 5.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 3..186
FT /note="KIND"
FT /evidence="ECO:0000259|PROSITE:PS51377"
FT DOMAIN 580..879
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 1077..1131
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1345..1430
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1476..1566
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1772..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 2001..2081
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 2262..2516
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 2438..2507
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 184..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1580..1659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1708..1742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2102..2192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2131..2179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2457
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-50"
FT BINDING 2427
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-51"
FT BINDING 2457..2463
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-51"
FT BINDING 2501
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000933-51"
SQ SEQUENCE 2528 AA; 279428 MW; 8486D4DBEA7A0EC8 CRC64;
MHVSLAEALE VRGGPLQEEE VWAVLSQSAE SLQELFRRDP SALGFIISPW SLLLMPSGSI
SFTDENVTQQ DLRAFTAPEV LEGVTLSSLS DIEKMHMYSL GMTLFWGADY EVPQSQPMKL
GEHLNSILLN MCDDTTLSRM SVLTVMDACS THIRNSSCEP SFTHIRKLVR LVLGSLSQLD
GLLSQSDRES IPERSKEIRE RLRGKGLPSG RSAAPRVLER YKARSQEQAS LNRGLSRSMG
SLPIQDLLRG EGALPGPYPP SDYHPGSESS ADLALYLEPQ QRGRPVELDR RSLPYRGDST
AQQKKNWASS VDLAHIDPDM LRFGALEDAR RGSSALSTRS GGRHKSASRV YRDRENRYSD
FGGLETPRTK AHHHSPLSSS SALTSAYDRI KEKQRKLQVL RQAMDDPLHS HRRYHSDYSS
SSESPSVASS DTDYRQVKKP EEARRYSSQL ALSDHHGMSL TSHNAHRHRR YEGAADEGLM
LQRREEEVQR LQAHLANRLS RASLYPGDDP RASLYTGDEP LARTSMLDLR DPLNATLPHH
RRPKNFFGPE FVKMTSEPCV ALTVPSSIMN KRGKLDEVQR KVGVVLLTGQ KLELSCDIKA
VCKDVLDMVV AHVGLVEHHL FGLACLTDNE FFFIDPDAKL SKVAPEGWKE EPKKKKPDIQ
FNLFLRIKFF LDDVNLIQHT MTKHQYYLQL RKDILEERVC CDMENAMLLA SLALQAEFGD
YQAELHGKTY FRMEHYMSAS VLDNIDQSSI KEELLKLHST YYGATEAETE FEFLKASQRL
TEYGVHFHRV LPEKRSQTGI MLGVFSKGVL IFEVLNGNRT PVLRFPWRET KKISFTKKKI
CLQNTSDGIK HLFQTDSNKT CQYLLCLCSA QHKFHLQTKA RQNNQELQDL ENSPLNLLQY
SLGQGGVEGM GRAVSSASLT PSSSARSAHS DSDLKRISYS EVALNKAPGG RLHAQEEVLF
PGFNSGLGPH HHHPSNARLM MSRSHHNLGQ VPESPEHRTV SFNSQSQSAV NHAQLLDSHH
RASSDTDSIS VAYQQDRRFG SSASHGSTAW SLKSFQKESD SSSSVEETGH ADVVGLLQIV
GGQNSGHVDL GTFISSITPG GPADVNGSLK PGDRLISVNE VNLEGLPHTA ATDDVTLVVS
QPRERLYEAP PSGFVYKPQA PLTVSGQRQQ DLDFESSIEE QEAGTGSPSP PLPTTTSSSS
SVSTVPRQSS LRSQDSRTES TNAPLQTPVN GTHPHRTLPT EAASVPVSIL HHQDRTNNIA
LTFDPLKASP PALPPKTRKA KIPEVPKDPD YSDRGDSEMD EETYSSSQDK PKFKKELTPL
PNGSVGGLSG NVPGVSSLSP GDLFDVELSK KDSSLGISVT GGVNTSVKHG GVYVKAIIPK
GAAELDGRIQ KGDRVVAVNG KSLEGTTHKQ AVETLRDTGK MVHLLLEKGQ LPADRIHAPL
TPQCTPPSDQ QQPAQEAAPP KAQPEYSFIT DNNVFEVPLL KNSSGLGFSF SREEILPDQT
TGNGSSMVRV KKLFPGQPAA ESGRINVGDV ILRVNQTPLK GLSQHEVISA LRGTGQEVTL
LLCRPDQGVL PEMDASALTP MASPRKEPVV QTQQPESSLA RPRTASPVGE EGKRSLGLGP
GQMEEALDRL LMKSPSRRDS YSDSTDDEEV EEAFSPSLEQ GRQAWDRGIY QTPSSNLTLG
RLHQYETPCE LDDTIRSAYY SSNLSLSNLS RRCPSSSSPR VPDLTTTPQP MVLSPEAPSP
DPLPLPRPPH FNHTLTDNRQ DLDEFVPDVE LKVSLVKSEK GSLGFTLTKG NDLGCYIHDI
IQDPAKGDGR LRPGDRMIMV NNKDVSNMGH TEVVNLVRAA PRVVDLVVGR VLEAPKPPIE
AHLLPDISFQ CPDQTLGLVL DGGSDSVYGV LFIKEVLPGS AALLEGSLRP LDLVHFINGA
PTLDLTLNES CRLLEISLRE LTIKATRDGK PVSPGQKSSS FLNNNVSPED STSLNDYVYG
ADRREAEAFT TLCPPEEEII QLDLDKPAAG GLGFSVIGGE RGIFVKSITP GGIADRTGRL
QVGDRLLKVN EELMTGVSHT KAVTTIRKVK GLVHLIMSRP PDQNPNTYLS YLPINSDKCN
GNSDDIGVKT KPCSPPDENS SPPDIPPIDY DVGSMERRTR EGEVENTELS EDTDRDGSSL
PEDSPETSRK ADWKEESVDN PLNESYLPMT SELPEEDEIT WGSDELPIEN INSKFTDDKP
IITEDELTSL PLVKVIPDGQ YTGAKLNTVV RMLRGLLEQK IPLQEFENLQ NLQPLDDCLI
GQTKENKKKN RYKNIVPFDT TRVILGKNGG YINANFINMP VKDENFMFIA CQGPLPTTLG
DFWQMIWEQK SNVIAMMTQE VEGGKVKCQR YWPDTPRTAE MVDERLQITL VKDQHLDNFV
IRLIEVKDIQ TEEIQRVTHL NYTGWPDHGT PSQPEQLLTF ISYMRHIHQS GPIITHCSAG
IGRSGTLICV DVVLGLISKD ADFDISDVVR SMRLQRQGMV QTEEQYIFCY QVILYVLRCL
QAEEKISG
//
