VPS39_HUMAN
ID VPS39_HUMAN Reviewed; 886 AA.
AC Q96JC1; O94869; Q71SQ6; Q7Z3V3; Q96B93; Q96RM0;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Vam6/Vps39-like protein {ECO:0000305};
DE AltName: Full=TRAP1-like protein;
DE Short=hVam6p;
GN Name=VPS39 {ECO:0000312|HGNC:HGNC:20593}; Synonyms=KIAA0770, TLP, VAM6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION,
RP HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11448994; DOI=10.1083/jcb.200102142;
RA Caplan S., Hartnell L.M., Aguilar R.C., Naslavsky N., Bonifacino J.S.;
RT "Human Vam6p promotes lysosome clustering and fusion in vivo.";
RL J. Cell Biol. 154:109-122(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Dell'Angelica E.C.;
RT "A human homolog of yeast Vps39.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Endometrial tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 101-886 (ISOFORMS 1/2).
RC TISSUE=Lung, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, INTERACTION WITH ACVR2B; SMAD4; TGFBR1 AND TGFBR2, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12941698; DOI=10.1093/emboj/cdg428;
RA Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M., Karpova T.S.,
RA McNally J.G., Roberts A.B.;
RT "TLP, a novel modulator of TGF-beta signaling, has opposite effects on
RT Smad2- and Smad3-dependent signaling.";
RL EMBO J. 22:4465-4477(2003).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [11]
RP REVIEW ON THE HOPS AND CORVET COMPLEXES.
RX PubMed=23351085; DOI=10.1111/febs.12151;
RA Solinger J.A., Spang A.;
RT "Tethering complexes in the endocytic pathway: CORVET and HOPS.";
RL FEBS J. 280:2743-2757(2013).
RN [12]
RP INTERACTION WITH VPS11.
RX PubMed=23901104; DOI=10.1073/pnas.1307074110;
RA Graham S.C., Wartosch L., Gray S.R., Scourfield E.J., Deane J.E.,
RA Luzio J.P., Owen D.J.;
RT "Structural basis of Vps33A recruitment to the human HOPS complex by
RT Vps16.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:13345-13350(2013).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23167963; DOI=10.1111/tra.12027;
RA Pols M.S., ten Brink C., Gosavi P., Oorschot V., Klumperman J.;
RT "The HOPS proteins hVps41 and hVps39 are required for homotypic and
RT heterotypic late endosome fusion.";
RL Traffic 14:219-232(2013).
RN [14]
RP SUBUNIT, AND INTERACTION WITH PLEKHM2.
RX PubMed=25908847; DOI=10.1242/jcs.162651;
RA Khatter D., Raina V.B., Dwivedi D., Sindhwani A., Bahl S., Sharma M.;
RT "The small GTPase Arl8b regulates assembly of the mammalian HOPS complex on
RT lysosomes.";
RL J. Cell Sci. 128:1746-1761(2015).
RN [15]
RP FUNCTION, AND FUNCTION OF THE HOPS COMPLEX.
RX PubMed=25783203; DOI=10.1111/tra.12283;
RA Wartosch L., Guenesdogan U., Graham S.C., Luzio J.P.;
RT "Recruitment of VPS33A to HOPS by VPS16 Is Required for Lysosome Fusion
RT with Endosomes and Autophagosomes.";
RL Traffic 16:727-742(2015).
RN [16]
RP INTERACTION WITH STX17.
RX PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035;
RA Miao G., Zhang Y., Chen D., Zhang H.;
RT "The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy
RT by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1.";
RL Mol. Cell 0:0-0(2019).
RN [17]
RP FUNCTION, AND INTERACTION WITH SARS-COV-2 ORF3A PROTEIN (MICROBIAL
RP INFECTION).
RX PubMed=33422265; DOI=10.1016/j.devcel.2020.12.010;
RA Miao G., Zhao H., Li Y., Ji M., Chen Y., Shi Y., Bi Y., Wang P., Zhang H.;
RT "ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated
RT assembly of the SNARE complex required for autolysosome formation.";
RL Dev. Cell 56:427-442(2020).
CC -!- FUNCTION: Regulator of TGF-beta/activin signaling, inhibiting
CC SMAD3- and activating SMAD2-dependent transcription. Acts by
CC interfering with SMAD3/SMAD4 complex formation, this would lead to
CC inhibition of SMAD3-dependent transcription and relieve SMAD3
CC inhibition of SMAD2-dependent promoters, thus increasing SMAD2-
CC dependent transcription. Does not affect TGF-beta-induced SMAD2 or
CC SMAD3 phosphorylation, nor SMAD2/SMAD4 complex formation.
CC {ECO:0000269|PubMed:12941698}.
CC -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking to
CC lysosomal compartments including the endocytic membrane transport and
CC autophagic pathways. Acts as a component of the putative HOPS endosomal
CC tethering complex which is proposed to be involved in the Rab5-to-Rab7
CC endosome conversion probably implicating MON1A/B, and via binding
CC SNAREs and SNARE complexes to mediate tethering and docking events
CC during SNARE-mediated membrane fusion. The HOPS complex is proposed to
CC be recruited to Rab7 on the late endosomal membrane and to regulate
CC late endocytic, phagocytic and autophagic traffic towards lysosomes
CC (PubMed:23351085). Involved in homotypic vesicle fusions between late
CC endosomes and in heterotypic fusions between late endosomes and
CC lysosomes (PubMed:11448994, PubMed:23351085, PubMed:23167963). Required
CC for fusion of endosomes and autophagosomes with lysosomes
CC (PubMed:25783203). {ECO:0000269|PubMed:11448994,
CC ECO:0000269|PubMed:23167963, ECO:0000269|PubMed:25783203,
CC ECO:0000269|PubMed:33422265, ECO:0000305|PubMed:23351085}.
CC -!- SUBUNIT: Homooligomer (PubMed:11448994). Interacts with TGFBR2 and,
CC less efficiently, with TGFBR1; interaction with TGFBR2 is independent
CC of the receptor kinase activity and of the presence of TGF-beta. Also
CC interacts with ACVR2B, but not with BMPR2. Interacts with SMAD4,
CC preferentially following TGF-beta treatment. Does not interact with
CC SAMD2 or SMAD3 (PubMed:12941698). Component of the putative homotypic
CC fusion and vacuole protein sorting (HOPS) complex; the core of which
CC composed of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, is
CC associated with VPS39 and VPS41 (PubMed:23351085, PubMed:23901104,
CC PubMed:25908847, PubMed:33422265). Interacts with PLEKHM2; involved in
CC VPS39 recruitment to ARL8B-containing lysosomes (PubMed:25908847).
CC Associates with adaptor protein complex 3 (AP-3) and clathrin:AP-3
CC complexes (By similarity). Interacts with STX17; this interaction is
CC increased in the absence of TMEM39A (PubMed:31806350).
CC {ECO:0000250|UniProtKB:Q8R5L3, ECO:0000269|PubMed:11448994,
CC ECO:0000269|PubMed:12941698, ECO:0000269|PubMed:23901104,
CC ECO:0000269|PubMed:25908847, ECO:0000269|PubMed:31806350,
CC ECO:0000269|PubMed:33422265, ECO:0000305|PubMed:23351085,
CC ECO:0000305|PubMed:25908847}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus-2/SARS-
CC CoV-2 ORF3A protein; the interaction is direct and sequestrates VPS39,
CC thereby preventing HOPS complex from interacting with the
CC autophagosomal SNARE protein STX17 (PubMed:33422265). ORF3A enhances
CC the interaction of VPS39 with VPS11 and VPS18, while its interaction
CC with the VPS16:VPS33A module is attenuated (PubMed:23167963).
CC {ECO:0000269|PubMed:23167963, ECO:0000269|PubMed:33422265}.
CC -!- INTERACTION:
CC Q96JC1; P51149: RAB7A; NbExp=2; IntAct=EBI-1050197, EBI-1056089;
CC Q96JC1; P56962: STX17; NbExp=2; IntAct=EBI-1050197, EBI-2797775;
CC Q96JC1; Q9P253: VPS18; NbExp=2; IntAct=EBI-1050197, EBI-1053363;
CC Q96JC1; P0DTC3: 3a; Xeno; NbExp=15; IntAct=EBI-1050197, EBI-25475894;
CC Q96JC1-2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-11962886, EBI-1105213;
CC Q96JC1-2; Q9H270: VPS11; NbExp=4; IntAct=EBI-11962886, EBI-373380;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Lysosome membrane
CC {ECO:0000269|PubMed:11448994, ECO:0000269|PubMed:17897319,
CC ECO:0000269|PubMed:23167963}; Peripheral membrane protein
CC {ECO:0000305|PubMed:11448994}. Late endosome membrane
CC {ECO:0000269|PubMed:11448994, ECO:0000269|PubMed:23167963}; Peripheral
CC membrane protein {ECO:0000305|PubMed:11448994}. Note=Colocalizes with
CC TGFBR1 and TGFBR2 in cytoplasmic vesicular structures and most
CC prominently in cortical vesicles. {ECO:0000269|PubMed:12941698}.
CC -!- SUBCELLULAR LOCATION: Note=(Microbial infection) Sequestrated at the
CC late endosome by SARS coronavirus-2/SARS-CoV-2 ORF3A protein.
CC {ECO:0000269|PubMed:33422265}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96JC1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96JC1-2; Sequence=VSP_004075;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in heart,
CC skeletal muscle, kidney, pancreas, brain, placenta and spleen.
CC {ECO:0000269|PubMed:11448994, ECO:0000269|PubMed:12941698}.
CC -!- SIMILARITY: Belongs to the VAM6/VPS39 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34490.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF280814; AAK72222.1; -; mRNA.
DR EMBL; AF334400; AAK58862.1; -; Genomic_DNA.
DR EMBL; AF281052; AAQ05978.1; -; mRNA.
DR EMBL; AB018313; BAA34490.2; ALT_INIT; mRNA.
DR EMBL; BX537404; CAD97646.1; -; mRNA.
DR EMBL; AC036103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471125; EAW92536.1; -; Genomic_DNA.
DR EMBL; BC015817; AAH15817.2; -; mRNA.
DR EMBL; BC068559; AAH68559.1; -; mRNA.
DR CCDS; CCDS10083.1; -. [Q96JC1-2]
DR CCDS; CCDS73710.1; -. [Q96JC1-1]
DR RefSeq; NP_001288067.1; NM_001301138.1. [Q96JC1-1]
DR RefSeq; NP_056104.2; NM_015289.3. [Q96JC1-2]
DR PDB; 6ZE9; X-ray; 2.90 A; A/B/C=851-886.
DR PDBsum; 6ZE9; -.
DR AlphaFoldDB; Q96JC1; -.
DR SMR; Q96JC1; -.
DR BioGRID; 116925; 43.
DR ComplexPortal; CPX-6212; HOPS tethering complex.
DR CORUM; Q96JC1; -.
DR IntAct; Q96JC1; 33.
DR MINT; Q96JC1; -.
DR STRING; 9606.ENSP00000335193; -.
DR iPTMnet; Q96JC1; -.
DR PhosphoSitePlus; Q96JC1; -.
DR BioMuta; VPS39; -.
DR DMDM; 66774218; -.
DR EPD; Q96JC1; -.
DR jPOST; Q96JC1; -.
DR MassIVE; Q96JC1; -.
DR MaxQB; Q96JC1; -.
DR PaxDb; Q96JC1; -.
DR PeptideAtlas; Q96JC1; -.
DR PRIDE; Q96JC1; -.
DR ProteomicsDB; 76939; -. [Q96JC1-1]
DR ProteomicsDB; 76940; -. [Q96JC1-2]
DR Antibodypedia; 23540; 106 antibodies from 25 providers.
DR DNASU; 23339; -.
DR Ensembl; ENST00000318006.10; ENSP00000326534.5; ENSG00000166887.16. [Q96JC1-2]
DR Ensembl; ENST00000348544.4; ENSP00000335193.5; ENSG00000166887.16. [Q96JC1-1]
DR GeneID; 23339; -.
DR KEGG; hsa:23339; -.
DR MANE-Select; ENST00000318006.10; ENSP00000326534.5; NM_015289.5; NP_056104.2. [Q96JC1-2]
DR UCSC; uc001zpc.4; human. [Q96JC1-1]
DR CTD; 23339; -.
DR DisGeNET; 23339; -.
DR GeneCards; VPS39; -.
DR HGNC; HGNC:20593; VPS39.
DR HPA; ENSG00000166887; Low tissue specificity.
DR MIM; 612188; gene.
DR neXtProt; NX_Q96JC1; -.
DR OpenTargets; ENSG00000166887; -.
DR PharmGKB; PA134945163; -.
DR VEuPathDB; HostDB:ENSG00000166887; -.
DR eggNOG; KOG2063; Eukaryota.
DR GeneTree; ENSGT00530000063596; -.
DR HOGENOM; CLU_004190_1_1_1; -.
DR InParanoid; Q96JC1; -.
DR OMA; LFRLPNF; -.
DR OrthoDB; 291710at2759; -.
DR PhylomeDB; Q96JC1; -.
DR TreeFam; TF105803; -.
DR PathwayCommons; Q96JC1; -.
DR Reactome; R-HSA-9754560; SARS-CoV-2 modulates autophagy.
DR SignaLink; Q96JC1; -.
DR SIGNOR; Q96JC1; -.
DR BioGRID-ORCS; 23339; 115 hits in 1099 CRISPR screens.
DR ChiTaRS; VPS39; human.
DR GeneWiki; VPS39; -.
DR GenomeRNAi; 23339; -.
DR Pharos; Q96JC1; Tbio.
DR PRO; PR:Q96JC1; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q96JC1; protein.
DR Bgee; ENSG00000166887; Expressed in right uterine tube and 199 other tissues.
DR ExpressionAtlas; Q96JC1; baseline and differential.
DR Genevisible; Q96JC1; HS.
DR GO; GO:0030123; C:AP-3 adaptor complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030897; C:HOPS complex; IDA:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:1902501; C:lysosomal HOPS complex; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0061909; P:autophagosome-lysosome fusion; IDA:UniProtKB.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0034058; P:endosomal vesicle fusion; IDA:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:1902774; P:late endosome to lysosome transport; IDA:UniProtKB.
DR GO; GO:0035542; P:regulation of SNARE complex assembly; IC:ComplexPortal.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR032914; Vam6/VPS39/TRAP1.
DR InterPro; IPR019452; VPS39/TGF_beta_rcpt-assoc_1.
DR InterPro; IPR019453; VPS39/TGF_beta_rcpt-assoc_2.
DR PANTHER; PTHR12894; PTHR12894; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF10366; Vps39_1; 1.
DR Pfam; PF10367; Vps39_2; 1.
DR SMART; SM00036; CNH; 1.
DR PROSITE; PS50236; CHCR; 1.
DR PROSITE; PS50219; CNH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autophagy; Cytoplasm; Endosome;
KW Host-virus interaction; Lysosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..886
FT /note="Vam6/Vps39-like protein"
FT /id="PRO_0000065901"
FT DOMAIN 15..294
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REPEAT 573..750
FT /note="CHCR"
FT VAR_SEQ 47..58
FT /note="VPADVASPESGS -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:9872452,
FT ECO:0000303|Ref.2"
FT /id="VSP_004075"
FT CONFLICT 135
FT /note="R -> Q (in Ref. 1; AAK72222)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="D -> G (in Ref. 5; CAD97646)"
FT /evidence="ECO:0000305"
FT CONFLICT 846
FT /note="I -> T (in Ref. 5; CAD97646)"
FT /evidence="ECO:0000305"
FT STRAND 851..858
FT /evidence="ECO:0007829|PDB:6ZE9"
FT STRAND 865..867
FT /evidence="ECO:0007829|PDB:6ZE9"
FT STRAND 871..877
FT /evidence="ECO:0007829|PDB:6ZE9"
FT HELIX 883..885
FT /evidence="ECO:0007829|PDB:6ZE9"
SQ SEQUENCE 886 AA; 101809 MW; E5A40A3C787EB112 CRC64;
MHDAFEPVPI LEKLPLQIDC LAAWEEWLLV GTKQGHLLLY RIRKDVVPAD VASPESGSCN
RFEVTLEKSN KNFSKKIQQI HVVSQFKILV SLLENNIYVH DLLTFQQITT VSKAKGASLF
TCDLQHTETG EEVLRMCVAV KKKLQLYFWK DREFHELQGD FSVPDVPKSM AWCENSICVG
FKRDYYLIRV DGKGSIKELF PTGKQLEPLV APLADGKVAV GQDDLTVVLN EEGICTQKCA
LNWTDIPVAM EHQPPYIIAV LPRYVEIRTF EPRLLVQSIE LQRPRFITSG GSNIIYVASN
HFVWRLIPVP MATQIQQLLQ DKQFELALQL AEMKDDSDSE KQQQIHHIKN LYAFNLFCQK
RFDESMQVFA KLGTDPTHVM GLYPDLLPTD YRKQLQYPNP LPVLSGAELE KAHLALIDYL
TQKRSQLVKK LNDSDHQSST SPLMEGTPTI KSKKKLLQII DTTLLKCYLH TNVALVAPLL
RLENNHCHIE ESEHVLKKAH KYSELIILYE KKGLHEKALQ VLVDQSKKAN SPLKGHERTV
QYLQHLGTEN LHLIFSYSVW VLRDFPEDGL KIFTEDLPEV ESLPRDRVLG FLIENFKGLA
IPYLEHIIHV WEETGSRFHN CLIQLYCEKV QGLMKEYLLS FPAGKTPVPA GEEEGELGEY
RQKLLMFLEI SSYYDPGRLI CDFPFDGLLE ERALLLGRMG KHEQALFIYV HILKDTRMAE
EYCHKHYDRN KDGNKDVYLS LLRMYLSPPS IHCLGPIKLE LLEPKANLQA ALQVLELHHS
KLDTTKALNL LPANTQINDI RIFLEKVLEE NAQKKRFNQV LKNLLHAEFL RVQEERILHQ
QVKCIITEEK VCMVCKKKIG NSAFARYPNG VVVHYFCSKE VNPADT
