位置:首页 > 蛋白库 > BECN1_YEAST
BECN1_YEAST
ID   BECN1_YEAST             Reviewed;         557 AA.
AC   Q02948; D6W3P7;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 180.
DE   RecName: Full=Vacuolar protein sorting-associated protein 30;
DE   AltName: Full=Autophagy-related protein 6;
GN   Name=VPS30; Synonyms=APG6, ATG6, VPT30; OrderedLocusNames=YPL120W;
GN   ORFNames=LPH7;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH ATG14.
RX   PubMed=9712845; DOI=10.1074/jbc.273.35.22284;
RA   Kametaka S., Okano T., Ohsumi M., Ohsumi Y.;
RT   "Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in
RT   the yeast, Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 273:22284-22291(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=8224160; DOI=10.1016/0014-5793(93)80398-e;
RA   Tsukada M., Ohsumi Y.;
RT   "Isolation and characterization of autophagy-defective mutants of
RT   Saccharomyces cerevisiae.";
RL   FEBS Lett. 333:169-174(1993).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=9105038; DOI=10.1083/jcb.137.1.79;
RA   Seaman M.N.J., Marcusson E.G., Cereghino J.L., Emr S.D.;
RT   "Endosome to Golgi retrieval of the vacuolar protein sorting receptor,
RT   Vps10p, requires the function of the VPS29, VPS30, and VPS35 gene
RT   products.";
RL   J. Cell Biol. 137:79-92(1997).
RN   [6]
RP   FUNCTION.
RX   PubMed=11689437; DOI=10.1093/emboj/20.21.5971;
RA   Suzuki K., Kirisako T., Kamada Y., Mizushima N., Noda T., Ohsumi Y.;
RT   "The pre-autophagosomal structure organized by concerted functions of APG
RT   genes is essential for autophagosome formation.";
RL   EMBO J. 20:5971-5981(2001).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS15; VPS34; VPS38
RP   AND ATG14.
RX   PubMed=11157979; DOI=10.1083/jcb.152.3.519;
RA   Kihara A., Noda T., Ishihara N., Ohsumi Y.;
RT   "Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in
RT   autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae.";
RL   J. Cell Biol. 152:519-530(2001).
RN   [8]
RP   FUNCTION.
RX   PubMed=12244127; DOI=10.1242/jcs.00090;
RA   Burda P., Padilla S.M., Sarkar S., Emr S.D.;
RT   "Retromer function in endosome-to-Golgi retrograde transport is regulated
RT   by the yeast Vps34 PtdIns 3-kinase.";
RL   J. Cell Sci. 115:3889-3900(2002).
RN   [9]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [10]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [11]
RP   FUNCTION.
RX   PubMed=16267277; DOI=10.1091/mbc.e04-09-0779;
RA   Kruse K.B., Brodsky J.L., McCracken A.A.;
RT   "Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and
RT   functionally distinct protein quality control pathways: one for soluble Z
RT   variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for
RT   aggregates of A1PiZ.";
RL   Mol. Biol. Cell 17:203-212(2006).
RN   [12]
RP   FUNCTION.
RX   PubMed=17700056; DOI=10.4161/auto.4784;
RA   Ma J., Jin R., Dobry C.J., Lawson S.K., Kumar A.;
RT   "Overexpression of autophagy-related genes inhibits yeast filamentous
RT   growth.";
RL   Autophagy 3:604-609(2007).
RN   [13]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17295840; DOI=10.1111/j.1365-2443.2007.01050.x;
RA   Suzuki K., Kubota Y., Sekito T., Ohsumi Y.;
RT   "Hierarchy of Atg proteins in pre-autophagosomal structure organization.";
RL   Genes Cells 12:209-218(2007).
RN   [14]
RP   INTERACTION WITH ATG14, AND SUBCELLULAR LOCATION.
RX   PubMed=16421251; DOI=10.1091/mbc.e05-09-0841;
RA   Obara K., Sekito T., Ohsumi Y.;
RT   "Assortment of phosphatidylinositol 3-kinase complexes--Atg14p directs
RT   association of complex I to the pre-autophagosomal structure in
RT   Saccharomyces cerevisiae.";
RL   Mol. Biol. Cell 17:1527-1539(2006).
RN   [15]
RP   FUNCTION.
RX   PubMed=17404498; DOI=10.4161/auto.4127;
RA   Zhang Y., Qi H., Taylor R., Xu W., Liu L.F., Jin S.;
RT   "The role of autophagy in mitochondria maintenance: characterization of
RT   mitochondrial functions in autophagy-deficient S. cerevisiae strains.";
RL   Autophagy 3:337-346(2007).
RN   [16]
RP   FUNCTION OF THE VPS34 PI3-KINASE COMPLEX II.
RX   PubMed=18182384; DOI=10.1093/jb/mvm249;
RA   Hirayama H., Fujita M., Yoko-o T., Jigami Y.;
RT   "O-mannosylation is required for degradation of the endoplasmic reticulum-
RT   associated degradation substrate Gas1*p via the ubiquitin/proteasome
RT   pathway in Saccharomyces cerevisiae.";
RL   J. Biochem. 143:555-567(2008).
RN   [17]
RP   FUNCTION.
RX   PubMed=18701704; DOI=10.1091/mbc.e08-04-0363;
RA   Krick R., Muehe Y., Prick T., Bremer S., Schlotterhose P., Eskelinen E.L.,
RA   Millen J., Goldfarb D.S., Thumm M.;
RT   "Piecemeal microautophagy of the nucleus requires the core macroautophagy
RT   genes.";
RL   Mol. Biol. Cell 19:4492-4505(2008).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-142, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [19]
RP   FUNCTION.
RX   PubMed=19131141; DOI=10.1016/j.ejcb.2008.11.003;
RA   Fu L., Sztul E.;
RT   "ER-associated complexes (ERACs) containing aggregated cystic fibrosis
RT   transmembrane conductance regulator (CFTR) are degraded by autophagy.";
RL   Eur. J. Cell Biol. 88:215-226(2009).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=19001347; DOI=10.1074/mcp.m800372-mcp200;
RA   Wiederhold E., Gandhi T., Permentier H.P., Breitling R., Poolman B.,
RA   Slotboom D.J.;
RT   "The yeast vacuolar membrane proteome.";
RL   Mol. Cell. Proteomics 8:380-392(2009).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-142, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP   AUTOPHAGY-SPECIFIC VPS34 PI3-KINASE COMPLEX I.
RX   PubMed=24165940; DOI=10.1083/jcb.201304123;
RA   Araki Y., Ku W.C., Akioka M., May A.I., Hayashi Y., Arisaka F.,
RA   Ishihama Y., Ohsumi Y.;
RT   "Atg38 is required for autophagy-specific phosphatidylinositol 3-kinase
RT   complex integrity.";
RL   J. Cell Biol. 203:299-313(2013).
RN   [23]
RP   SUBCELLULAR LOCATION.
RX   PubMed=23549786; DOI=10.1242/jcs.122960;
RA   Suzuki K., Akioka M., Kondo-Kakuta C., Yamamoto H., Ohsumi Y.;
RT   "Fine mapping of autophagy-related proteins during autophagosome formation
RT   in Saccharomyces cerevisiae.";
RL   J. Cell Sci. 126:2534-2544(2013).
RN   [24]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MEMBRANE-SPANNING REGION.
RX   PubMed=23878393; DOI=10.1128/mcb.00079-13;
RA   Fogel A.I., Dlouhy B.J., Wang C., Ryu S.W., Neutzner A., Hasson S.A.,
RA   Sideris D.P., Abeliovich H., Youle R.J.;
RT   "Role of membrane association and Atg14-dependent phosphorylation in
RT   beclin-1-mediated autophagy.";
RL   Mol. Cell. Biol. 33:3675-3688(2013).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 320-539, DOMAIN, AND FUNCTION.
RX   PubMed=22437838; DOI=10.1074/jbc.m112.348250;
RA   Noda N.N., Kobayashi T., Adachi W., Fujioka Y., Ohsumi Y., Inagaki F.;
RT   "Structure of the novel C-terminal domain of vacuolar protein sorting
RT   30/autophagy-related protein 6 and its specific role in autophagy.";
RL   J. Biol. Chem. 287:16256-16266(2012).
CC   -!- FUNCTION: Required for cytoplasm to vacuole transport (Cvt), autophagy,
CC       nucleophagy, and mitophagy, as a part of the autophagy-specific VPS34
CC       PI3-kinase complex I. This complex is essential to recruit the ATG8-
CC       phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-
CC       autophagosomal structure. Also involved in endosome-to-Golgi retrograde
CC       transport as part of the VPS34 PI3-kinase complex II. This second
CC       complex is required for the endosome-to-Golgi retrieval of PEP1 and
CC       KEX2, and the recruitment of VPS5 and VPS7, two components of the
CC       retromer complex, to endosomal membranes (probably through the
CC       synthesis of a specific pool of phosphatidylinositol 3-phosphate
CC       recruiting the retromer to the endosomes). Also plays a role in
CC       regulation of filamentous growth. {ECO:0000269|PubMed:11157979,
CC       ECO:0000269|PubMed:11689437, ECO:0000269|PubMed:12244127,
CC       ECO:0000269|PubMed:16267277, ECO:0000269|PubMed:17404498,
CC       ECO:0000269|PubMed:17700056, ECO:0000269|PubMed:18182384,
CC       ECO:0000269|PubMed:18701704, ECO:0000269|PubMed:19131141,
CC       ECO:0000269|PubMed:22437838, ECO:0000269|PubMed:23878393,
CC       ECO:0000269|PubMed:8224160, ECO:0000269|PubMed:9105038,
CC       ECO:0000269|PubMed:9712845}.
CC   -!- SUBUNIT: Component of the autophagy-specific VPS34 PI3-kinase complex I
CC       composed of VPS15, VPS30, VPS34, ATG14 and ATG38; and of the VPS34 PI3-
CC       kinase complex II composed of VPS15, VPS30, VPS34 and VPS38.
CC       {ECO:0000269|PubMed:24165940}.
CC   -!- INTERACTION:
CC       Q02948; P38270: ATG14; NbExp=12; IntAct=EBI-2670, EBI-2699;
CC       Q02948; Q05919: VPS38; NbExp=15; IntAct=EBI-2670, EBI-29972;
CC   -!- SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein.
CC       Vacuole membrane; Peripheral membrane protein. Preautophagosomal
CC       structure membrane {ECO:0000269|PubMed:23878393}; Peripheral membrane
CC       protein. Note=With the VPS34 PI3-kinase complex I, localizes to the
CC       vacuole-isolation membrane contact site (VICS) during isolation
CC       membrane (IM) expansion. The IM is a membrane sac generated from the
CC       pre-autophagosomal structure that ultimately expands to become a mature
CC       autophagosome.
CC   -!- DOMAIN: The C-terminal domain called the BARA domain is dispensable for
CC       the construction of both VPS34 PI3-kinase complexes, but is
CC       specifically required for autophagy through the targeting of complex I
CC       to the pre-autophagosomal structure. {ECO:0000269|PubMed:22437838}.
CC   -!- MISCELLANEOUS: Present with 2490 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the beclin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB011072; BAA32104.1; -; Genomic_DNA.
DR   EMBL; U43503; AAB68242.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11313.1; -; Genomic_DNA.
DR   PIR; S62002; S62002.
DR   RefSeq; NP_015205.1; NM_001183934.1.
DR   PDB; 3VP7; X-ray; 2.30 A; A=320-539.
DR   PDB; 5DFZ; X-ray; 4.40 A; D=1-557.
DR   PDBsum; 3VP7; -.
DR   PDBsum; 5DFZ; -.
DR   AlphaFoldDB; Q02948; -.
DR   SMR; Q02948; -.
DR   BioGRID; 36061; 491.
DR   ComplexPortal; CPX-1677; Phosphatidylinositol 3-kinase complex II.
DR   ComplexPortal; CPX-1881; Phosphatidylinositol 3-kinase complex, class III, type I.
DR   DIP; DIP-2961N; -.
DR   IntAct; Q02948; 11.
DR   MINT; Q02948; -.
DR   STRING; 4932.YPL120W; -.
DR   iPTMnet; Q02948; -.
DR   MaxQB; Q02948; -.
DR   PaxDb; Q02948; -.
DR   PRIDE; Q02948; -.
DR   EnsemblFungi; YPL120W_mRNA; YPL120W; YPL120W.
DR   GeneID; 855983; -.
DR   KEGG; sce:YPL120W; -.
DR   SGD; S000006041; VPS30.
DR   VEuPathDB; FungiDB:YPL120W; -.
DR   eggNOG; KOG2751; Eukaryota.
DR   GeneTree; ENSGT00390000008164; -.
DR   HOGENOM; CLU_024219_3_2_1; -.
DR   InParanoid; Q02948; -.
DR   OMA; DTFCIGH; -.
DR   BioCyc; YEAST:G3O-34019-MON; -.
DR   Reactome; R-SCE-1632852; Macroautophagy.
DR   Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR   PRO; PR:Q02948; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q02948; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR   GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IC:ComplexPortal.
DR   GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IDA:SGD.
DR   GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IDA:SGD.
DR   GO; GO:0120095; C:vacuole-isolation membrane contact site; IDA:SGD.
DR   GO; GO:0000045; P:autophagosome assembly; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0006914; P:autophagy; IDA:ComplexPortal.
DR   GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD.
DR   GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IMP:SGD.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:ComplexPortal.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR   GO; GO:0006623; P:protein targeting to vacuole; IDA:UniProtKB.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:SGD.
DR   Gene3D; 1.10.418.40; -; 1.
DR   InterPro; IPR007243; Atg6/Beclin.
DR   InterPro; IPR038274; Atg6/Beclin_C_sf.
DR   InterPro; IPR041691; Atg6/beclin_CC.
DR   InterPro; IPR040455; Atg6_BARA.
DR   PANTHER; PTHR12768; PTHR12768; 1.
DR   Pfam; PF04111; APG6; 1.
DR   Pfam; PF17675; APG6_N; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Autophagy; Coiled coil; Endosome; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport; Vacuole.
FT   CHAIN           1..557
FT                   /note="Vacuolar protein sorting-associated protein 30"
FT                   /id="PRO_0000218559"
FT   REGION          93..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..539
FT                   /note="BARA"
FT   REGION          515..540
FT                   /note="Required for membrane-association, autophagic
FT                   function during starvation and normal autophagosome
FT                   morphology"
FT                   /evidence="ECO:0000269|PubMed:23878393"
FT   COILED          189..322
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        102..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         142
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   TURN            322..326
FT                   /evidence="ECO:0007829|PDB:3VP7"
FT   STRAND          329..332
FT                   /evidence="ECO:0007829|PDB:3VP7"
FT   STRAND          335..338
FT                   /evidence="ECO:0007829|PDB:3VP7"
FT   STRAND          341..343
FT                   /evidence="ECO:0007829|PDB:3VP7"
FT   HELIX           353..373
FT                   /evidence="ECO:0007829|PDB:3VP7"
FT   STRAND          379..384
FT                   /evidence="ECO:0007829|PDB:3VP7"
FT   HELIX           387..389
FT                   /evidence="ECO:0007829|PDB:3VP7"
FT   STRAND          391..395
FT                   /evidence="ECO:0007829|PDB:3VP7"
FT   STRAND          413..419
FT                   /evidence="ECO:0007829|PDB:3VP7"
FT   HELIX           435..459
FT                   /evidence="ECO:0007829|PDB:3VP7"
FT   STRAND          502..504
FT                   /evidence="ECO:0007829|PDB:3VP7"
FT   HELIX           513..537
FT                   /evidence="ECO:0007829|PDB:3VP7"
SQ   SEQUENCE   557 AA;  63261 MW;  4BA74B614CABE1C0 CRC64;
     MKCQTCHLPL QLDPSLEGLS LTQRNLLLSN NSIITATNEN VISNKGIEAA DNCGPQIPKE
     RLRRLGEIQN IKDLNLKDDK LITDSFVFLN HDDDDNANIT SNSREDQRYG NANGNDNKKA
     NSDTSDGTST FRDHDEEEQE ATDEDENQQI QLNSKTLSTQ VNAMTNVFNI LSSQTNIDFP
     ICQDCCNILI NRLKSEYDDA IKERDTYAQF LSKLESQNKE ISESNKEKQY SHNLSEKENL
     KKEEERLLDQ LLRLEMTDDD LDGELVRLQE KKVQLENEKL QKLSDQNLMD LNNIQFNKNL
     QSLKLQYELS LNQLDKLRKI NIFNATFKIS HSGPFATING LRLGSIPESV VPWKEINAAL
     GQLILLLATI NKNLKINLVD YELQPMGSFS KIKKRMVNSV EYNNSTTNAP GDWLILPVYY
     DENFNLGRIF RKETKFDKSL ETTLEIISEI TRQLSTIASS YSSQTLTTSQ DESSMNNAND
     VENSTSILEL PYIMNKDKIN GLSVKLHGSS PNLEWTTAMK FLLTNVKWLL AFSSNLLSKS
     ITLSPTVNYN DKTISGN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024