PTN13_MOUSE
ID PTN13_MOUSE Reviewed; 2453 AA.
AC Q64512; Q61494; Q62135; Q64499;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 13;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q12923};
DE AltName: Full=PTP36;
DE AltName: Full=Protein tyrosine phosphatase DPZPTP;
DE AltName: Full=Protein tyrosine phosphatase PTP-BL;
DE AltName: Full=Protein-tyrosine phosphatase RIP;
GN Name=Ptpn13; Synonyms=Ptp14;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=8749712; DOI=10.1002/jcb.240590403;
RA Hendriks W., Schepens J., Baechner D., Rijss J., Zeeuwen P., Zechner U.,
RA Hameister H., Wieringa B.;
RT "Molecular cloning of a mouse epithelial protein-tyrosine phosphatase with
RT similarities to submembranous proteins.";
RL J. Cell. Biochem. 59:418-430(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DBA/2J;
RX PubMed=7843407; DOI=10.1016/0014-5793(94)01432-z;
RA Chida D., Kume T., Mukouyama Y., Tabata S., Nomura N., Thomas M.,
RA Watanabe T., Oishi M.;
RT "Characterization of a protein tyrosine phosphatase (RIP) expressed at a
RT very early stage of differentiation in both mouse erythroleukemia and
RT embryonal carcinoma cells.";
RL FEBS Lett. 358:233-239(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1105-2452.
RC STRAIN=CB.17 SCID; TISSUE=Thymus;
RX PubMed=8074693; DOI=10.1006/bbrc.1994.2207;
RA Sawada M., Ogata M., Fujino Y., Hamaoka T.;
RT "cDNA cloning of a novel protein tyrosine phosphatase with homology to
RT cytoskeletal protein 4.1 and its expression in T-lineage cells.";
RL Biochem. Biophys. Res. Commun. 203:479-484(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2267-2373.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=7832766; DOI=10.1042/bj3050499;
RA Hendriks W., Schepens J., Brugman C., Zeeuwen P., Wieringa B.;
RT "A novel receptor-type protein tyrosine phosphatase with a single catalytic
RT domain is specifically expressed in mouse brain.";
RL Biochem. J. 305:499-504(1995).
RN [5]
RP INTERACTION WITH PDLIM4.
RX PubMed=9487134; DOI=10.1091/mbc.9.3.671;
RA Cuppen E., Gerrits H., Pepers B., Wieringa B., Hendriks W.;
RT "PDZ motifs in PTP-BL and RIL bind to internal protein segments in the LIM
RT domain protein RIL.";
RL Mol. Biol. Cell 9:671-683(1998).
RN [6]
RP INTERACTION WITH BRD7.
RX PubMed=10526152; DOI=10.1016/s0014-5793(99)01191-6;
RA Cuppen E., van Ham M., Pepers B., Wieringa B., Hendriks W.;
RT "Identification and molecular characterization of BP75, a novel
RT bromodomain-containing protein.";
RL FEBS Lett. 459:291-298(1999).
RN [7]
RP INTERACTION WITH PDLIM4 AND TRIP6.
RX PubMed=10826496; DOI=10.1078/s0171-9335(04)70031-x;
RA Cuppen E., van Ham M., Wansink D.G., de Leeuw A., Wieringa B., Hendriks W.;
RT "The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor
RT protein RIL and the protein tyrosine phosphatase PTP-BL.";
RL Eur. J. Cell Biol. 79:283-293(2000).
RN [8]
RP INTERACTION WITH PDLIM4.
RX PubMed=15663004; DOI=10.1007/s11033-005-1407-8;
RA van den Berk L.C., van Ham M.A., te Lindert M.M., Walma T., Aelen J.,
RA Vuister G.W., Hendriks W.J.;
RT "The interaction of PTP-BL PDZ domains with RIL: an enigmatic role for the
RT RIL LIM domain.";
RL Mol. Biol. Rep. 31:203-215(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-297; SER-298;
RP SER-883; SER-890; SER-901; SER-904; SER-907; SER-1221 AND SER-1270, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH ENTR1 AND GIT1, AND INTERACTION WITH
RP ENTR1.
RX PubMed=23108400; DOI=10.1038/onc.2012.485;
RA Hagemann N., Ackermann N., Christmann J., Brier S., Yu F., Erdmann K.S.;
RT "The serologically defined colon cancer antigen-3 interacts with the
RT protein tyrosine phosphatase PTPN13 and is involved in the regulation of
RT cytokinesis.";
RL Oncogene 32:4602-4613(2013).
CC -!- FUNCTION: Tyrosine phosphatase which regulates negatively FAS-induced
CC apoptosis and NGFR-mediated pro-apoptotic signaling. May regulate
CC phosphoinositide 3-kinase (PI3K) signaling through dephosphorylation of
CC PIK3R2. {ECO:0000250|UniProtKB:Q12923}.
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:0000250|UniProtKB:Q12923};
CC -!- SUBUNIT: Interacts (via the first PDZ domain) with PLEKHA1 and PLEKHA2.
CC Interacts (via the second PDZ domain) with TNFRSF6 (Fas receptor) (via
CC C-terminus) (By similarity). Interacts (via the second PDZ domain) with
CC TRIP6 (via the third LIM domain and C-terminus) (PubMed:10826496).
CC Interacts (via the third PDZ domain) with NGFR (via C-terminal SVP
CC motif) and PKN2 (via C-terminus) (By similarity). Interacts (via the
CC second or fourth PDZ domains) with PDLIM4 (via C-terminus only or via
CC combined C-terminus and LIM domain, but not LIM domain only)
CC (PubMed:9487134, PubMed:15663004). Found in a complex with PDLIM4 and
CC TRIP6 (PubMed:10826496). Interacts with PDLIM4; this interaction
CC results in dephosphorylation of SRC 'Tyr-419' by this protein leading
CC to its inactivation (By similarity). Interacts with BRD7
CC (PubMed:10526152). Interacts with RAPGEF6. Interacts with ARHGAP29.
CC Interacts with PIK3R2; dephosphorylates PIK3R2. Interacts with FBXL2
CC (By similarity). Interacts (via the FERM domain) with ENTR1
CC (PubMed:23108400). Found in a complex with ENTR1, PTPN13 and GIT1
CC (PubMed:23108400). {ECO:0000250|UniProtKB:Q12923,
CC ECO:0000269|PubMed:10526152, ECO:0000269|PubMed:10826496,
CC ECO:0000269|PubMed:15663004, ECO:0000269|PubMed:23108400,
CC ECO:0000269|PubMed:9487134}.
CC -!- INTERACTION:
CC Q64512; O88665: Brd7; NbExp=3; IntAct=EBI-4284057, EBI-643930;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q12923}. Nucleus {ECO:0000250|UniProtKB:Q12923}.
CC Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q12923}.
CC Note=Colocalizes with PKN2 in lamellipodia-like structure, regions of
CC large actin turnover. {ECO:0000250|UniProtKB:Q12923}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in kidney and, to a lesser
CC extent, in lung, heart, brain and testis.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
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DR EMBL; Z32740; CAA83650.1; -; mRNA.
DR EMBL; D83966; BAA12158.1; -; mRNA.
DR EMBL; D28529; BAA05885.1; -; mRNA.
DR EMBL; Z23059; CAA80594.1; -; mRNA.
DR PIR; S40290; S40290.
DR PIR; S71625; S71625.
DR RefSeq; NP_035334.2; NM_011204.2.
DR PDB; 1GM1; NMR; -; A=1351-1444.
DR PDB; 1OZI; NMR; -; A=1351-1444.
DR PDB; 1VJ6; NMR; -; A=1351-1444.
DR PDB; 6GBD; NMR; -; A=1475-1588.
DR PDB; 6GBE; NMR; -; A=1475-1588.
DR PDBsum; 1GM1; -.
DR PDBsum; 1OZI; -.
DR PDBsum; 1VJ6; -.
DR PDBsum; 6GBD; -.
DR PDBsum; 6GBE; -.
DR AlphaFoldDB; Q64512; -.
DR SMR; Q64512; -.
DR BioGRID; 202479; 32.
DR ELM; Q64512; -.
DR IntAct; Q64512; 9.
DR MINT; Q64512; -.
DR STRING; 10090.ENSMUSP00000048119; -.
DR iPTMnet; Q64512; -.
DR PhosphoSitePlus; Q64512; -.
DR jPOST; Q64512; -.
DR MaxQB; Q64512; -.
DR PaxDb; Q64512; -.
DR PRIDE; Q64512; -.
DR ProteomicsDB; 301873; -.
DR DNASU; 19249; -.
DR GeneID; 19249; -.
DR KEGG; mmu:19249; -.
DR CTD; 5783; -.
DR MGI; MGI:103293; Ptpn13.
DR eggNOG; KOG0792; Eukaryota.
DR InParanoid; Q64512; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q64512; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 19249; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Ptpn13; mouse.
DR EvolutionaryTrace; Q64512; -.
DR PRO; PR:Q64512; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q64512; protein.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 5.
DR Gene3D; 3.90.190.10; -; 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 Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00595; PDZ; 5.
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; SSF47031; SSF47031; 1.
DR SUPFAM; SSF50156; SSF50156; 5.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF54236; SSF54236; 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 1: Evidence at protein level;
KW 3D-structure; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Repeat.
FT CHAIN 1..2453
FT /note="Tyrosine-protein phosphatase non-receptor type 13"
FT /id="PRO_0000219436"
FT DOMAIN 3..190
FT /note="KIND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00709"
FT DOMAIN 565..865
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 1084..1170
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1357..1442
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1491..1579
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1764..1845
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1857..1942
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 2180..2434
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 183..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1602..1662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1695..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1991..2024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2051..2139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 458..493
FT /evidence="ECO:0000255"
FT COMPBIAS 189..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..961
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2108..2138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2375
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 2345
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 2375..2381
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 2419
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12923"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12923"
FT MOD_RES 1076
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12923"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 79..81
FT /note="STA -> FTG (in Ref. 2; BAA12158)"
FT /evidence="ECO:0000305"
FT CONFLICT 156..168
FT /note="HIRNSNCAPSFSN -> TSGTASRAFVSY (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="V -> L (in Ref. 2; BAA12158)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="N -> I (in Ref. 2; BAA12158)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="K -> E (in Ref. 2; BAA12158)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="Q -> K (in Ref. 2; BAA12158)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="S -> L (in Ref. 2; BAA12158)"
FT /evidence="ECO:0000305"
FT CONFLICT 1233
FT /note="S -> T (in Ref. 3; BAA05885)"
FT /evidence="ECO:0000305"
FT CONFLICT 1449
FT /note="R -> Q (in Ref. 2; BAA12158)"
FT /evidence="ECO:0000305"
FT CONFLICT 1474..1489
FT /note="QTPHVKDYSFVTEDNT -> KHPMSKTTALLLKII (in Ref. 1;
FT CAA83650)"
FT /evidence="ECO:0000305"
FT CONFLICT 1622
FT /note="D -> H (in Ref. 2; BAA12158)"
FT /evidence="ECO:0000305"
FT CONFLICT 1872
FT /note="S -> P (in Ref. 1; CAA83650)"
FT /evidence="ECO:0000305"
FT CONFLICT 1979
FT /note="N -> I (in Ref. 3; BAA05885)"
FT /evidence="ECO:0000305"
FT CONFLICT 2078
FT /note="D -> N (in Ref. 2; BAA12158)"
FT /evidence="ECO:0000305"
FT CONFLICT 2233
FT /note="S -> T (in Ref. 2; BAA12158)"
FT /evidence="ECO:0000305"
FT CONFLICT 2448..2452
FT /note="PGLPQ -> GSHSDAEQPPKAPP (in Ref. 1; CAA83650)"
FT /evidence="ECO:0000305"
FT STRAND 1354..1361
FT /evidence="ECO:0007829|PDB:1GM1"
FT STRAND 1364..1366
FT /evidence="ECO:0007829|PDB:1OZI"
FT STRAND 1369..1378
FT /evidence="ECO:0007829|PDB:1GM1"
FT STRAND 1383..1389
FT /evidence="ECO:0007829|PDB:1GM1"
FT STRAND 1391..1393
FT /evidence="ECO:0007829|PDB:1OZI"
FT HELIX 1394..1398
FT /evidence="ECO:0007829|PDB:1GM1"
FT STRAND 1406..1410
FT /evidence="ECO:0007829|PDB:1GM1"
FT HELIX 1420..1428
FT /evidence="ECO:0007829|PDB:1GM1"
FT STRAND 1432..1440
FT /evidence="ECO:0007829|PDB:1GM1"
FT STRAND 1482..1485
FT /evidence="ECO:0007829|PDB:6GBD"
FT STRAND 1490..1495
FT /evidence="ECO:0007829|PDB:6GBD"
FT STRAND 1505..1507
FT /evidence="ECO:0007829|PDB:6GBD"
FT STRAND 1521..1523
FT /evidence="ECO:0007829|PDB:6GBD"
FT HELIX 1531..1534
FT /evidence="ECO:0007829|PDB:6GBD"
FT STRAND 1535..1537
FT /evidence="ECO:0007829|PDB:6GBD"
FT STRAND 1543..1549
FT /evidence="ECO:0007829|PDB:6GBD"
FT STRAND 1552..1554
FT /evidence="ECO:0007829|PDB:6GBE"
FT HELIX 1557..1563
FT /evidence="ECO:0007829|PDB:6GBD"
FT STRAND 1567..1576
FT /evidence="ECO:0007829|PDB:6GBD"
SQ SEQUENCE 2453 AA; 270334 MW; 53396F27AE2582F2 CRC64;
MHVSLAEALE VRGGPLQEEE IWAVLNQSAE SLQEVFRRVS IADPAALGFI ISPWSLLLLP
SGSVSFTDEN VSNQDLRAST APEVLQSHSL TSLADVEKIH IYSLGMTLYW GADHEVPQSQ
PIKLGDHLNS ILLGMCEDVI YARVSVRTVL DACSAHIRNS NCAPSFSNVK QLVKLVLGNI
SGTDPLSRSS EQKPDRSQAI RDRLRGKGLP TGRSSTSDAL DTHEAPLSQQ TFVNKGLSKS
MGFLSIRDTR DEEDYLKDTP SDNNSRHEDS ETFSSPYQFK TSTPQMDALS KKKTWASSMD
LLCAANRDIS GETGRYQRCD PKTVTGRTSI TPRKKEGRYS DGSIALDIFG PQKVEPVIHT
RELPTSTAVS SALDRIRERQ QKLQVLREAM NVEEPVRRYK TYHSDIFSIS SESPSVISSE
SDFRQVRKSE ASKRFESSSG LPGVDETGQT RPSRQYETSL EGNLINQDIM LRRQEEEMMQ
LQARMALRQS RLSLYPGDTV KASMLDISRD PLREMALETA MTQRKLRNFF GPEFVKMTVE
PFVSLDLPRS ILSQTKKGKS EDQRRKVNIR LLSGQRLELT CDTKTICKDV FDMVVAHIGL
VEHHLFALAT RKENEYFFVD PDLKLTKVAP EGWKEEPKRK GKAAVDFTLF FRIKFFMDDV
SLIQHDLTCH QYYLQLRKDL LDERVHCDDE AALLLASLAL QAEYGDYQPE VHGVSYFRLE
HYLPARVMEK LDVSYIKEEL PKLHNTYAGA SEKETELEFL KVCQRLTEYG VHFHRVHPEK
KSQTGILLGV CSKGVLVFEV HNGVRALVLR FPWRETKKIS FSKKKITLQN TSDGIKHAFQ
TDSSKACQYL LHLCSSQHKF QLQMRARQSN QDAQDIERAS FRSLNLQAES VRGFNMGRAI
STGSLASSTI NKLAVRPLSV QAEILKRLSS SEWSLYQPLQ NSSKEKTDKA SWEEKPRGMS
KSYHDLSQAS LCPHRKQVIN MEALPQAFAE LVGKPLYPMA RSDTESLAGL PKLDNSKSVA
SLNRSPERRN HESDSSTEDP GQAYVVGMSL PSSGKSSSQV PFKDNDTLHK RWSIVSSPER
EITLVNLKKD PKHGLGFQII GGEKMGRLDL GVFISAVTPG GPADLDGCLK PGDRLISVNS
VSLEGVSHHA AVDILQNAPE DVTLVISQPK EKPSKVPSTP VHFANGMKSY TKKPAYMQDS
AMDPSEDQPW PRGTLRHIPE SPFGLSGGLR EGSLSSQDSR TESASLSQSQ VNGFFASHLG
DRGWQEPQHS SPSPSVTTKV NEKTFSDSNR SKAKRRGISD LIEHLDCADS DKDDSTYTSS
QDHQTSKQEP SSSLSTSNKT SFPTSSASPP KPGDTFEVEL AKTDGSLGIS VTGGVNTSVR
HGGIYVKAII PKGAAESDGR IHKGDRVLAV NGVSLEGATH KQAVETLRNT GQVVHLLLEK
GQVPTSRERD PAGPQSPPPD QDAQRQAPEK VAKQTPHVKD YSFVTEDNTF EVKLFKNSSG
LGFSFSREDN LIPEQINGSI VRVKKLFPGQ PAAESGKIDV GDVILKVNGA PLKGLSQQDV
ISALRGTAPE VSLLLCRPAP GVLPEIDTTF LNPLYSPANS FLNSSKETSQ PSSSVEQGAS
SDDNGVSGKT KNHCRAPSRR ESYSDHSESG EDDSVRAPAK MPNVTRVAAF PHEAPRSQEE
SICAMFYLPR KIPGKLESES SHPPPLDVSP GQTCQPPAEC APSDATGKHF THLASQLSKE
ENITTLKNDL GNHLEDSELE VELLITLVKS EKGSLGFTVT KGSQSIGCYV HDVIQDPAKG
DGRLKAGDRL IKVNDTDVTN MTHTDAVNLL RAAPKTVRLV LGRILELPRM PVFPHLLPDI
TVTCHGEELG FSLSGGQGSP HGVVYISDIN PRSAAAVDGS LQLLDIIHYV NGVSTQGMTL
EDANRALDLS LPSVVLKVTR DGCPVVPTTR AAISAPRFTK ANGLTSMEPS GQPALMPKNS
FSKVNGEGVH EAVCPAGEGS SSQMKESAGL TETKESNSRD DDIYDDPQEA EVIQSLLDVV
DEEAQNLLNQ RHATRRACSP DPLRTNGEAP EEGDTDYDGS PLPEDVPESV SSGEGKVDLA
SLTAASQEEK PIEEDATQES RNSTTETTDG EDSSKDPPFL TNEELAALPV VRVPPSGKYT
GTQLQATIRT LQGLLDQGIP SKELENLQEL KPLDQCLIGQ TKENRRKNRY KNILPYDTTR
VPLGDEGGYI NASFIRIPVG TQEFVYIACQ GPLPTTVGDF WQMVWEQNST VIAMMTQEVE
GEKIKCQRYW PSILGTTTMA NERLRLALLR MQQLKGFIVR VMALEDIQTG EVRHISHLNF
TAWPDHDTPS QPDDLLTFIS YMRHIRRSGP VITHCSAGIG RSGTLICIDV VLGLISQDLE
FDISDLVRCM RLQRHGMVQT EGQYVFCYQV ILYVLTHLQA EEQKAQQPGL PQP
