SEC63_YEAST
ID SEC63_YEAST Reviewed; 663 AA.
AC P14906; D6W2V5; Q08690;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Protein translocation protein SEC63;
DE AltName: Full=Protein NPL1;
DE AltName: Full=Sec62/63 complex 73 kDa subunit;
GN Name=SEC63; Synonyms=NPL1, PTL1; OrderedLocusNames=YOR254C;
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].
RX PubMed=2556404; DOI=10.1083/jcb.109.6.2665;
RA Sadler I., Chiang A., Kurihara T., Rothblatt J.A., Way J., Silver P.A.;
RT "A yeast gene important for protein assembly into the endoplasmic reticulum
RT and the nucleus has homology to DnaJ, an Escherichia coli heat shock
RT protein.";
RL J. Cell Biol. 109:2665-2675(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153759;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<483::aid-yea105>3.0.co;2-u;
RA Poirey R., Jauniaux J.-C.;
RT "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals
RT 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1
RT and VPH1.";
RL Yeast 13:483-487(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
RP IDENTIFICATION IN THE SEC62/63 COMPLEX.
RX PubMed=2000150; DOI=10.1038/349806a0;
RA Deshaies R.J., Sanders S.L., Feldheim D.A., Schekman R.;
RT "Assembly of yeast Sec proteins involved in translocation into the
RT endoplasmic reticulum into a membrane-bound multisubunit complex.";
RL Nature 349:806-808(1991).
RN [6]
RP IDENTIFICATION IN THE SEC62/63 COMPLEX.
RX PubMed=1620130; DOI=10.1128/mcb.12.7.3288-3296.1992;
RA Feldheim D., Rothblatt J., Schekman R.;
RT "Topology and functional domains of Sec63p, an endoplasmic reticulum
RT membrane protein required for secretory protein translocation.";
RL Mol. Cell. Biol. 12:3288-3296(1992).
RN [7]
RP MUTAGENESIS.
RX PubMed=8514125; DOI=10.1093/genetics/134.1.159;
RA Nelson M.K., Kurihara T., Silver P.A.;
RT "Extragenic suppressors of mutations in the cytoplasmic C-terminus of SEC63
RT define five genes in Saccharomyces cerevisiae.";
RL Genetics 134:159-173(1993).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH KAR2; SEC66 AND SEC72.
RX PubMed=8253836; DOI=10.1083/jcb.123.6.1355;
RA Brodsky J.L., Schekman R.;
RT "A Sec63p-BiP complex from yeast is required for protein translocation in a
RT reconstituted proteoliposome.";
RL J. Cell Biol. 123:1355-1363(1993).
RN [9]
RP ASSOCIATION OF THE SEC62/63 COMPLEX WITH THE SEC61 COMPLEX.
RX PubMed=7758110; DOI=10.1016/0092-8674(95)90077-2;
RA Panzner S., Dreier L., Hartmann E., Kostka S., Rapoport T.A.;
RT "Posttranslational protein transport in yeast reconstituted with a purified
RT complex of Sec proteins and Kar2p.";
RL Cell 81:561-570(1995).
RN [10]
RP FUNCTION.
RX PubMed=11226176; DOI=10.1093/emboj/20.1.262;
RA Young B.P., Craven R.A., Reid P.J., Willer M., Stirling C.J.;
RT "Sec63p and Kar2p are required for the translocation of SRP-dependent
RT precursors into the yeast endoplasmic reticulum in vivo.";
RL EMBO J. 20:262-271(2001).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [12]
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 [13]
RP INTERACTION WITH SEC63.
RX PubMed=12518317; DOI=10.1002/yea.954;
RA Willer M., Jermy A.J., Young B.P., Stirling C.J.;
RT "Identification of novel protein-protein interactions at the cytosolic
RT surface of the Sec63 complex in the yeast ER membrane.";
RL Yeast 20:133-148(2003).
RN [14]
RP PHOSPHORYLATION BY CASEIN KINASE II, INTERACTION WITH SEC63, AND
RP MUTAGENESIS OF THR-652 AND THR-654.
RX PubMed=15671059; DOI=10.1242/jcs.01671;
RA Wang X., Johnsson N.;
RT "Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of the
RT endoplasmic reticulum protein translocation apparatus.";
RL J. Cell Sci. 118:723-732(2005).
RN [15]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, 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).
CC -!- FUNCTION: Acts as component of the Sec62/63 complex which is involved
CC in SRP-independent post-translational translocation across the
CC endoplasmic reticulum (ER) and functions together with the Sec61
CC complex and KAR2 in a channel-forming translocon complex. A cycle of
CC assembly and disassembly of Sec62/63 complex from SEC61 may govern the
CC activity of the translocon. SEC63 may affect SEC1-polypeptide
CC interactions by increasing the affinity of targeting pathways for SEC61
CC and/or by modifying SEC61 to allow more efficient polypeptide
CC interaction. May also be involved in SRP-dependent cotranslational
CC translocation. Is essential for cell growth and for germination.
CC {ECO:0000269|PubMed:11226176}.
CC -!- SUBUNIT: Component of the heterotetrameric Sec62/63complex composed of
CC SEC62, SEC63, SEC66 and SEC72. The Sec62/63 complex associates with the
CC Sec61 complex to form the Sec complex. SEC63 interacts in its
CC phosphorylated form with SEC62. May physically associate with KAR2 in
CC the endoplasmic reticulum and this interaction may be regulated by ATP
CC hydrolysis. Part of a complex consisting of KAR2, SEC63, SEC66 and
CC SEC72. {ECO:0000269|PubMed:12518317, ECO:0000269|PubMed:15671059,
CC ECO:0000269|PubMed:1620130, ECO:0000269|PubMed:2000150,
CC ECO:0000269|PubMed:8253836}.
CC -!- INTERACTION:
CC P14906; P21825: SEC62; NbExp=7; IntAct=EBI-16636, EBI-16632;
CC P14906; P33754: SEC66; NbExp=4; IntAct=EBI-16636, EBI-16647;
CC P14906; P39742: SEC72; NbExp=4; IntAct=EBI-16636, EBI-16651;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Nucleus membrane; Multi-pass membrane protein.
CC Nucleus inner membrane; Multi-pass membrane protein.
CC -!- PTM: Phosphotylated by casein kinase II.
CC -!- MISCELLANEOUS: Present with 17700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; X16388; CAA34424.1; -; Genomic_DNA.
DR EMBL; Z75162; CAA99476.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11021.1; -; Genomic_DNA.
DR PIR; A33618; A33618.
DR RefSeq; NP_014897.1; NM_001183673.1.
DR PDB; 6N3Q; EM; 3.68 A; D=1-663.
DR PDB; 6ND1; EM; 4.10 A; A=1-663.
DR PDB; 7AFT; EM; 4.40 A; D=1-663.
DR PDB; 7KAH; EM; 3.10 A; D=2-663.
DR PDB; 7KAI; EM; 3.20 A; D=2-663.
DR PDB; 7KAJ; EM; 3.10 A; D=2-663.
DR PDB; 7KAO; EM; 4.00 A; D=2-663.
DR PDB; 7KAP; EM; 4.10 A; D=2-663.
DR PDB; 7KAQ; EM; 4.00 A; D=2-663.
DR PDB; 7KAR; EM; 4.00 A; D=2-663.
DR PDB; 7KAS; EM; 3.90 A; D=2-663.
DR PDB; 7KAT; EM; 4.40 A; D=2-663.
DR PDB; 7KAU; EM; 4.00 A; D=2-663.
DR PDB; 7KB5; EM; 3.80 A; D=2-663.
DR PDBsum; 6N3Q; -.
DR PDBsum; 6ND1; -.
DR PDBsum; 7AFT; -.
DR PDBsum; 7KAH; -.
DR PDBsum; 7KAI; -.
DR PDBsum; 7KAJ; -.
DR PDBsum; 7KAO; -.
DR PDBsum; 7KAP; -.
DR PDBsum; 7KAQ; -.
DR PDBsum; 7KAR; -.
DR PDBsum; 7KAS; -.
DR PDBsum; 7KAT; -.
DR PDBsum; 7KAU; -.
DR PDBsum; 7KB5; -.
DR AlphaFoldDB; P14906; -.
DR SMR; P14906; -.
DR BioGRID; 34644; 652.
DR ComplexPortal; CPX-3055; Translocon complex.
DR ComplexPortal; CPX-3056; SEC62-SEC63 complex.
DR DIP; DIP-2396N; -.
DR IntAct; P14906; 18.
DR MINT; P14906; -.
DR STRING; 4932.YOR254C; -.
DR TCDB; 3.A.5.8.1; the general secretory pathway (sec) family.
DR iPTMnet; P14906; -.
DR MaxQB; P14906; -.
DR PaxDb; P14906; -.
DR PRIDE; P14906; -.
DR EnsemblFungi; YOR254C_mRNA; YOR254C; YOR254C.
DR GeneID; 854428; -.
DR KEGG; sce:YOR254C; -.
DR SGD; S000005780; SEC63.
DR VEuPathDB; FungiDB:YOR254C; -.
DR eggNOG; KOG0721; Eukaryota.
DR GeneTree; ENSGT00390000001965; -.
DR HOGENOM; CLU_014210_0_0_1; -.
DR InParanoid; P14906; -.
DR OMA; ETWPFFL; -.
DR BioCyc; YEAST:G3O-33745-MON; -.
DR PRO; PR:P14906; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P14906; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0031207; C:Sec62/Sec63 complex; IPI:SGD.
DR GO; GO:0071256; C:translocon complex; IPI:ComplexPortal.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IDA:SGD.
DR GO; GO:0046967; P:cytosol to endoplasmic reticulum transport; IMP:SGD.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IMP:SGD.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IDA:SGD.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IMP:SGD.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR027137; Sec63.
DR InterPro; IPR004179; Sec63-dom.
DR PANTHER; PTHR24075:SF0; PTHR24075:SF0; 1.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Endoplasmic reticulum; Membrane; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..663
FT /note="Protein translocation protein SEC63"
FT /id="PRO_0000071095"
FT TOPO_DOM 1..13
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..220
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 123..198
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 228..532
FT /note="SEC63"
FT REPEAT 461..471
FT /note="1"
FT REPEAT 493..503
FT /note="2"
FT REGION 461..503
FT /note="2 X 11 AA repeats"
FT REGION 615..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..663
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 179
FT /note="A->T: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:8514125"
FT MUTAGEN 426
FT /note="P->L: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:8514125"
FT MUTAGEN 431
FT /note="I->N: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:8514125"
FT MUTAGEN 503
FT /note="P->A: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:8514125"
FT MUTAGEN 511
FT /note="G->R: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:8514125"
FT MUTAGEN 652
FT /note="T->A: Abolishes interaction with SEC62; defect in
FT protein translocation."
FT /evidence="ECO:0000269|PubMed:15671059"
FT MUTAGEN 654
FT /note="T->A: Abolishes interaction with SEC62; defect in
FT protein translocation."
FT /evidence="ECO:0000269|PubMed:15671059"
FT CONFLICT 263
FT /note="V -> I (in Ref. 1; CAA34424)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="F -> L (in Ref. 1; CAA34424)"
FT /evidence="ECO:0000305"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 14..35
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 94..112
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:7KAJ"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:7KAH"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 256..267
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 277..284
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 319..342
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 346..361
FT /evidence="ECO:0007829|PDB:7KAH"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 379..385
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 392..396
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 400..407
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 412..422
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 430..436
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 450..455
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:7KAI"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:7KAH"
FT TURN 487..490
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 503..507
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 513..522
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:7KAJ"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:7KAJ"
FT STRAND 569..574
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 584..597
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 602..610
FT /evidence="ECO:0007829|PDB:7KAH"
SQ SEQUENCE 663 AA; 75345 MW; 7D6757144C8A301F CRC64;
MPTNYEYDEA SETWPSFILT GLLMVVGPMT LLQIYQIFFG ANAEDGNSGK SKEFNEEVFK
NLNEEYTSDE IKQFRRKFDK NSNKKSKIWS RRNIIIIVGW ILVAILLQRI NSNDAIKDAA
TKLFDPYEIL GISTSASDRD IKSAYRKLSV KFHPDKLAKG LTPDEKSVME ETYVQITKAY
ESLTDELVRQ NYLKYGHPDG PQSTSHGIAL PRFLVDGSAS PLLVVCYVAL LGLILPYFVS
RWWARTQSYT KKGIHNVTAS NFVSNLVNYK PSEIVTTDLI LHWLSFAHEF KQFFPDLQPT
DFEKLLQDHI NRRDSGKLNN AKFRIVAKCH SLLHGLLDIA CGFRNLDIAL GAINTFKCIV
QAVPLTPNCQ ILQLPNVDKE HFITKTGDIH TLGKLFTLED AKIGEVLGIK DQAKLNETLR
VASHIPNLKI IKADFLVPGE NQVTPSSTPY ISLKVLVRSA KQPLIPTSLI PEENLTEPQD
FESQRDPFAM MSKQPLVPYS FAPFFPTKRR GSWCCLVSSQ KDGKILQTPI IIEKLSYKNL
NDDKDFFDKR IKMDLTKHEK FDINDWEIGT IKIPLGQPAP ETVGDFFFRV IVKSTDYFTT
DLDITMNMKV RDSPAVEQVE VYSEEDDEYS TDDDETESDD ESDASDYTDI DTDTEAEDDE
SPE
