PRP19_YEAST
ID PRP19_YEAST Reviewed; 503 AA.
AC P32523; D6VXW9; Q07870;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Pre-mRNA-processing factor 19 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:12627222};
DE AltName: Full=RING-type E3 ubiquitin transferase PRP19 {ECO:0000305};
GN Name=PRP19; Synonyms=PSO4; OrderedLocusNames=YLL036C;
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=8441419; DOI=10.1128/mcb.13.3.1876-1882.1993;
RA Cheng S.C., Tarn W.Y., Tsao T.Y., Abelson J.;
RT "PRP19: a novel spliceosomal component.";
RL Mol. Cell. Biol. 13:1876-1882(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8918805; DOI=10.1093/nar/24.20.4009;
RA Grey M., Duesterhoeft A., Henriques J.A.P., Brendel M.;
RT "Allelism of PSO4 and PRP19 links pre-mRNA processing with recombination
RT and error-prone DNA repair in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 24:4009-4014(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 CHARACTERIZATION.
RX PubMed=7680101; DOI=10.1128/mcb.13.3.1883-1891.1993;
RA Tarn W.Y., Lee K.R., Cheng S.C.;
RT "The yeast PRP19 protein is not tightly associated with small nuclear RNAs,
RT but appears to associate with the spliceosome after binding of U2 to the
RT pre-mRNA and prior to formation of the functional spliceosome.";
RL Mol. Cell. Biol. 13:1883-1891(1993).
RN [6]
RP SELF-ASSOCIATION, AND IDENTIFICATION IN THE PRP19-ASSOCIATED COMPLEX.
RX PubMed=8194532; DOI=10.1002/j.1460-2075.1994.tb06527.x;
RA Tarn W.Y., Hsu C.H., Huang K.T., Chen H.R., Kao H.Y., Lee K.R., Cheng S.C.;
RT "Functional association of essential splicing factor(s) with PRP19 in a
RT protein complex.";
RL EMBO J. 13:2421-2431(1994).
RN [7]
RP IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT "Proteomics analysis reveals stable multiprotein complexes in both fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CWC2.
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 [9]
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 [10]
RP TETRAMERIZATION, ELECTRON MICROSCOPY OF THE TETRAMER, AND INTERACTION WITH
RP CEF1.
RX PubMed=15601865; DOI=10.1128/mcb.25.1.451-460.2005;
RA Ohi M.D., Vander Kooi C.W., Rosenberg J.A., Ren L., Hirsch J.P.,
RA Chazin W.J., Walz T., Gould K.L.;
RT "Structural and functional analysis of essential pre-mRNA splicing factor
RT Prp19p.";
RL Mol. Cell. Biol. 25:451-460(2005).
RN [11]
RP IDENTIFICATION BY 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 [12]
RP IDENTIFICATION BY 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP STRUCTURE BY NMR OF 1-56, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=12627222; DOI=10.1038/nsb906;
RA Ohi M.D., Vander Kooi C.W., Rosenberg J.A., Chazin W.J., Gould K.L.;
RT "Structural insights into the U-box, a domain associated with multi-
RT ubiquitination.";
RL Nat. Struct. Biol. 10:250-255(2003).
CC -!- FUNCTION: Probable ubiquitin-protein ligase involved in pre-mRNA
CC splicing. Acts as a central component of the NTC complex (or PRP19-
CC associated complex) that associates to the spliceosome to mediate
CC conformational rearrangement or to stabilize the structure of the
CC spliceosome after U4 snRNA dissociation, which leads to spliceosome
CC maturation. It is also probably involved in DNA repair.
CC {ECO:0000269|PubMed:12627222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:12627222};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:12627222}.
CC -!- SUBUNIT: Homotetramer. Component of the NTC complex (or PRP19-
CC associated complex), composed of at least CEF1, CLF1, ISY1, NTC20,
CC SNT309, SYF1, SYF2, and PRP19. The NTC complex associates with the
CC spliceosome after the release of the U1 and U4 snRNAs and forms the CWC
CC spliceosome subcomplex (or CEF1-associated complex) reminiscent of a
CC late-stage spliceosome composed also of the U2, U5 and U6 snRNAs and at
CC least BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22,
CC CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9,
CC PRP11, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2,
CC SMX3, SNU114, SPP2, RSE1 and YJU2. Interacts with CLF1, ISY1, NTC20,
CC PRP19, PRP46, SYF1 and SYF2. Interacts with CWC2.
CC {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:14690591,
CC ECO:0000269|PubMed:15601865, ECO:0000269|PubMed:8194532}.
CC -!- INTERACTION:
CC P32523; P40968: CDC40; NbExp=7; IntAct=EBI-493, EBI-13834;
CC P32523; Q03654: CEF1; NbExp=9; IntAct=EBI-493, EBI-476;
CC P32523; Q12309: CLF1; NbExp=9; IntAct=EBI-493, EBI-484;
CC P32523; Q12046: CWC2; NbExp=13; IntAct=EBI-493, EBI-553;
CC P32523; P21374: ISY1; NbExp=6; IntAct=EBI-493, EBI-9382;
CC P32523; P38302: NTC20; NbExp=5; IntAct=EBI-493, EBI-20921;
CC P32523; P32523: PRP19; NbExp=2; IntAct=EBI-493, EBI-493;
CC P32523; Q06091: SNT309; NbExp=8; IntAct=EBI-493, EBI-818;
CC P32523; Q04048: SYF1; NbExp=6; IntAct=EBI-493, EBI-540;
CC P32523; P53277: SYF2; NbExp=4; IntAct=EBI-493, EBI-23308;
CC P32523; Q06525: URN1; NbExp=7; IntAct=EBI-493, EBI-35138;
CC P32523; Q12208: USB1; NbExp=3; IntAct=EBI-493, EBI-31589;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 11700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: The tetramer is an elongated particle consisting of four
CC globular WD40 domains held together by a central stalk.
CC -!- SIMILARITY: Belongs to the WD repeat PRP19 family. {ECO:0000305}.
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DR EMBL; L09721; AAA34912.1; -; Genomic_DNA.
DR EMBL; X99770; CAA68103.1; -; Genomic_DNA.
DR EMBL; Z73142; CAA97487.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09285.1; -; Genomic_DNA.
DR PIR; S64787; S64787.
DR RefSeq; NP_013064.1; NM_001181856.1.
DR PDB; 1N87; NMR; -; A=1-56.
DR PDB; 2BAY; X-ray; 1.50 A; A/B/C/D/E/F=1-58.
DR PDB; 3LRV; X-ray; 2.60 A; A=165-503.
DR PDB; 4ZB4; X-ray; 2.30 A; A/B=144-503.
DR PDB; 5GM6; EM; 3.50 A; o/p/q/r=1-503.
DR PDB; 5GMK; EM; 3.40 A; o/p/q/r=1-503.
DR PDB; 5LJ5; EM; 3.80 A; t/u/v/w=1-503.
DR PDB; 5M8C; X-ray; 2.30 A; A/B=144-503.
DR PDB; 5MQ0; EM; 4.17 A; t/u/v/w=1-503.
DR PDB; 5WSG; EM; 4.00 A; o/p/q/r=1-503.
DR PDB; 5Y88; EM; 3.70 A; q/r/s/t=1-503.
DR PDB; 5YLZ; EM; 3.60 A; q/r/s/t=1-503.
DR PDB; 6BK8; EM; 3.30 A; u/v/w/x=1-503.
DR PDB; 6EXN; EM; 3.70 A; t/u/v/w=1-503.
DR PDB; 6J6G; EM; 3.20 A; o/p/q/r=1-503.
DR PDB; 6J6H; EM; 3.60 A; o/p/q/r=1-503.
DR PDB; 6J6N; EM; 3.86 A; o/p/q/r=1-503.
DR PDB; 6J6Q; EM; 3.70 A; o/p/q/r=1-503.
DR PDBsum; 1N87; -.
DR PDBsum; 2BAY; -.
DR PDBsum; 3LRV; -.
DR PDBsum; 4ZB4; -.
DR PDBsum; 5GM6; -.
DR PDBsum; 5GMK; -.
DR PDBsum; 5LJ5; -.
DR PDBsum; 5M8C; -.
DR PDBsum; 5MQ0; -.
DR PDBsum; 5WSG; -.
DR PDBsum; 5Y88; -.
DR PDBsum; 5YLZ; -.
DR PDBsum; 6BK8; -.
DR PDBsum; 6EXN; -.
DR PDBsum; 6J6G; -.
DR PDBsum; 6J6H; -.
DR PDBsum; 6J6N; -.
DR PDBsum; 6J6Q; -.
DR AlphaFoldDB; P32523; -.
DR BMRB; P32523; -.
DR SMR; P32523; -.
DR BioGRID; 31217; 523.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR ComplexPortal; CPX-1885; NineTeen complex.
DR DIP; DIP-1112N; -.
DR IntAct; P32523; 58.
DR MINT; P32523; -.
DR STRING; 4932.YLL036C; -.
DR BindingDB; P32523; -.
DR ChEMBL; CHEMBL5058; -.
DR iPTMnet; P32523; -.
DR MaxQB; P32523; -.
DR PaxDb; P32523; -.
DR PRIDE; P32523; -.
DR EnsemblFungi; YLL036C_mRNA; YLL036C; YLL036C.
DR GeneID; 850623; -.
DR KEGG; sce:YLL036C; -.
DR SGD; S000003959; PRP19.
DR VEuPathDB; FungiDB:YLL036C; -.
DR eggNOG; KOG0289; Eukaryota.
DR GeneTree; ENSGT00940000153662; -.
DR HOGENOM; CLU_023894_0_0_1; -.
DR InParanoid; P32523; -.
DR OMA; TSLQNEW; -.
DR BioCyc; YEAST:G3O-32139-MON; -.
DR BRENDA; 2.3.2.27; 984.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P32523; -.
DR PRO; PR:P32523; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32523; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000974; C:Prp19 complex; IDA:SGD.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IMP:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013915; Pre-mRNA_splic_Prp19.
DR InterPro; IPR038959; Prp19.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR43995; PTHR43995; 2.
DR Pfam; PF08606; Prp19; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Repeat; Spliceosome; Transferase;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..503
FT /note="Pre-mRNA-processing factor 19"
FT /id="PRO_0000058587"
FT DOMAIN 1..71
FT /note="U-box"
FT REPEAT 328..367
FT /note="WD 1"
FT REPEAT 372..410
FT /note="WD 2"
FT REPEAT 418..458
FT /note="WD 3"
FT REGION 57..144
FT /note="Required for self-association"
FT REGION 76..134
FT /note="Interaction with CEF1"
FT /evidence="ECO:0000269|PubMed:15601865"
FT CONFLICT 239
FT /note="Missing (in Ref. 1; AAA34912)"
FT /evidence="ECO:0000305"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:2BAY"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:2BAY"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:2BAY"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:2BAY"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:2BAY"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2BAY"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2BAY"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5GMK"
FT HELIX 78..136
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 149..163
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 204..216
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:4ZB4"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:4ZB4"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:4ZB4"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:4ZB4"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:4ZB4"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:4ZB4"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 386..401
FT /evidence="ECO:0007829|PDB:4ZB4"
FT TURN 402..405
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 432..439
FT /evidence="ECO:0007829|PDB:4ZB4"
FT TURN 440..443
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 444..451
FT /evidence="ECO:0007829|PDB:4ZB4"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:5GMK"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 476..482
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 485..491
FT /evidence="ECO:0007829|PDB:4ZB4"
FT STRAND 493..502
FT /evidence="ECO:0007829|PDB:4ZB4"
SQ SEQUENCE 503 AA; 56570 MW; A44D8C7DD6F64185 CRC64;
MLCAISGKVP RRPVLSPKSR TIFEKSLLEQ YVKDTGNDPI TNEPLSIEEI VEIVPSAQQA
SLTESTNSAT LKANYSIPNL LTSLQNEWDA IMLENFKLRS TLDSLTKKLS TVMYERDAAK
LVAAQLLMEK NEDSKDLPKS SQQAVAITRE EFLQGLLQSS RDFVARGKLK APKWPILKNL
ELLQAQNYSR NIKTFPYKEL NKSMYYDKWV CMCRCEDGAL HFTQLKDSKT ITTITTPNPR
TGGEHPAIIS RGPCNRLLLL YPGNQITILD SKTNKVLREI EVDSANEIIY MYGHNEVNTE
YFIWADNRGT IGFQSYEDDS QYIVHSAKSD VEYSSGVLHK DSLLLALYSP DGILDVYNLS
SPDQASSRFP VDEEAKIKEV KFADNGYWMV VECDQTVVCF DLRKDVGTLA YPTYTIPEFK
TGTVTYDIDD SGKNMIAYSN ESNSLTIYKF DKKTKNWTKD EESALCLQSD TADFTDMDVV
CGDGGIAAIL KTNDSFNIVA LTP
