ID VPS28_HUMAN Reviewed; 221 AA. AC Q9UK41; Q86VK0; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 185. DE RecName: Full=Vacuolar protein sorting-associated protein 28 homolog; DE Short=H-Vps28; DE AltName: Full=ESCRT-I complex subunit VPS28; GN Name=VPS28; 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 [MRNA] (ISOFORM 1). RA Hunt P.R., Pevsner J.; RT "H-vps28, a human homolog of yeast class E protein Vps28p localizes to an RT abnormal compartment in I-cell fibroblasts."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Lung; 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 [4] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11916981; DOI=10.1083/jcb.200112080; RA Bishop N., Horman A., Woodman P.; RT "Mammalian class E vps proteins recognize ubiquitin and act in the removal RT of endosomal protein-ubiquitin conjugates."; RL J. Cell Biol. 157:91-101(2002). RN [5] RP INTERACTION WITH TSG101. RX PubMed=14505570; DOI=10.1016/s0092-8674(03)00714-1; RA von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y., RA Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A., RA Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.; RT "The protein network of HIV budding."; RL Cell 114:701-713(2003). RN [6] RP INTERACTION WITH VPS37B. RX PubMed=15218037; DOI=10.1074/jbc.m405226200; RA Stuchell M.D., Garrus J.E., Mueller B., Stray K.M., Ghaffarian S., RA McKinnon R., Kraeusslich H.-G., Morham S.G., Sundquist W.I.; RT "The human endosomal sorting complex required for transport (ESCRT-I) and RT its role in HIV-1 budding."; RL J. Biol. Chem. 279:36059-36071(2004). RN [7] RP INTERACTION WITH TSG101; VPS37B; VPS37C; MVB12A AND MVB12B, AND RP RECONSTITUTION OF THE ESCRT-I COMPLEX. RX PubMed=18005716; DOI=10.1016/j.chom.2007.06.003; RA Morita E., Sandrin V., Alam S.L., Eckert D.M., Gygi S.P., Sundquist W.I.; RT "Identification of human MVB12 proteins as ESCRT-I subunits that function RT in HIV budding."; RL Cell Host Microbe 2:41-53(2007). RN [8] RP INTERACTION WITH CEP55. RX PubMed=17853893; DOI=10.1038/sj.emboj.7601850; RA Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., RA Sundquist W.I.; RT "Human ESCRT and ALIX proteins interact with proteins of the midbody and RT function in cytokinesis."; RL EMBO J. 26:4215-4227(2007). RN [9] RP INTERACTION WITH VPS36; SNF8 AND VPS25. RX PubMed=18539118; DOI=10.1016/j.devcel.2008.04.004; RA Im Y.J., Hurley J.H.; RT "Integrated structural model and membrane targeting mechanism of the human RT ESCRT-II complex."; RL Dev. Cell 14:902-913(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP IDENTIFICATION IN AN ESCRT-I COMPLEX WITH UBAP1, AND SUBUNIT. RX PubMed=21757351; DOI=10.1016/j.cub.2011.06.028; RA Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A., RA Brownhill K., Bennion J., Pickering-Brown S., Woodman P.; RT "UBAP1 is a component of an endosome-specific ESCRT-I complex that is RT essential for MVB sorting."; RL Curr. Biol. 21:1245-1250(2011). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] RP INTERACTION WITH UBAP1. RX PubMed=30929741; DOI=10.1016/j.ajhg.2019.03.001; RA Farazi Fard M.A., Rebelo A.P., Buglo E., Nemati H., Dastsooz H., RA Gehweiler I., Reich S., Reichbauer J., Quintans B., Ordonez-Ugalde A., RA Cortese A., Courel S., Abreu L., Powell E., Danzi M.C., Martuscelli N.B., RA Bis-Brewer D.M., Tao F., Zarei F., Habibzadeh P., Yavarian M., RA Modarresi F., Silawi M., Tabatabaei Z., Yousefi M., Farpour H.R., RA Kessler C., Mangold E., Kobeleva X., Tournev I., Chamova T., Mueller A.J., RA Haack T.B., Tarnopolsky M., Gan-Or Z., Rouleau G.A., Synofzik M., RA Sobrido M.J., Jordanova A., Schuele R., Zuchner S., Faghihi M.A.; RT "Truncating mutations in UBAP1 cause hereditary spastic paraplegia."; RL Am. J. Hum. Genet. 104:767-773(2019). CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular CC trafficking process. {ECO:0000269|PubMed:11916981}. CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex CC required for transport I) which consists of TSG101, VPS28, a VPS37 CC protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry CC (PubMed:14505570, PubMed:18005716). Interacts with TSG101, VPS37B, CC VPS37C, MVB12A and MVB12B (PubMed:14505570, PubMed:15218037, CC PubMed:18005716). Component of an ESCRT-I complex (endosomal sorting CC complex required for transport I) which consists of TSG101, VPS28, CC VPS37A and UBAP1 in a 1:1:1:1 stoichiometry (PubMed:14505570, CC PubMed:21757351, PubMed:30929741). Interacts with VPS36; the CC interaction mediates the association with the ESCRT-II complex. CC Interacts with SNF8 and VPS25 (PubMed:18539118). Interacts with CEP55 CC (PubMed:17853893). {ECO:0000269|PubMed:14505570, CC ECO:0000269|PubMed:15218037, ECO:0000269|PubMed:17853893, CC ECO:0000269|PubMed:18005716, ECO:0000269|PubMed:18539118, CC ECO:0000269|PubMed:21757351, ECO:0000269|PubMed:30929741}. CC -!- INTERACTION: CC Q9UK41; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-727424, EBI-2548012; CC Q9UK41; Q9H257-2: CARD9; NbExp=4; IntAct=EBI-727424, EBI-11530605; CC Q9UK41; Q9H257-3: CARD9; NbExp=3; IntAct=EBI-727424, EBI-16431743; CC Q9UK41; Q08379: GOLGA2; NbExp=6; IntAct=EBI-727424, EBI-618309; CC Q9UK41; P42858: HTT; NbExp=16; IntAct=EBI-727424, EBI-466029; CC Q9UK41; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-727424, EBI-10182361; CC Q9UK41; Q8WWW0-2: RASSF5; NbExp=3; IntAct=EBI-727424, EBI-960502; CC Q9UK41; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-727424, EBI-3957636; CC Q9UK41; P12757: SKIL; NbExp=4; IntAct=EBI-727424, EBI-2902468; CC Q9UK41; Q16637: SMN2; NbExp=5; IntAct=EBI-727424, EBI-395421; CC Q9UK41; Q16637-3: SMN2; NbExp=3; IntAct=EBI-727424, EBI-395447; CC Q9UK41; Q99081-3: TCF12; NbExp=3; IntAct=EBI-727424, EBI-11952764; CC Q9UK41; P14373: TRIM27; NbExp=3; IntAct=EBI-727424, EBI-719493; CC Q9UK41; Q99816: TSG101; NbExp=10; IntAct=EBI-727424, EBI-346882; CC Q9UK41; Q8N6Y0: USHBP1; NbExp=6; IntAct=EBI-727424, EBI-739895; CC Q9UK41; Q9H9H4: VPS37B; NbExp=6; IntAct=EBI-727424, EBI-4400866; CC Q9UK41; Q8N1B4: VPS52; NbExp=4; IntAct=EBI-727424, EBI-2799833; CC Q9UK41-2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-12146727, EBI-11096309; CC Q9UK41-2; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-12146727, EBI-745073; CC Q9UK41-2; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-12146727, EBI-10749669; CC Q9UK41-2; Q07002: CDK18; NbExp=3; IntAct=EBI-12146727, EBI-746238; CC Q9UK41-2; P10606: COX5B; NbExp=3; IntAct=EBI-12146727, EBI-1053725; CC Q9UK41-2; P55040: GEM; NbExp=3; IntAct=EBI-12146727, EBI-744104; CC Q9UK41-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-12146727, EBI-11742507; CC Q9UK41-2; Q9H7Z3: NRDE2; NbExp=3; IntAct=EBI-12146727, EBI-1042642; CC Q9UK41-2; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-12146727, EBI-398874; CC Q9UK41-2; P54646: PRKAA2; NbExp=3; IntAct=EBI-12146727, EBI-1383852; CC Q9UK41-2; O43741: PRKAB2; NbExp=3; IntAct=EBI-12146727, EBI-1053424; CC Q9UK41-2; Q92529: SHC3; NbExp=3; IntAct=EBI-12146727, EBI-79084; CC Q9UK41-2; P51687: SUOX; NbExp=3; IntAct=EBI-12146727, EBI-3921347; CC Q9UK41-2; Q99816: TSG101; NbExp=6; IntAct=EBI-12146727, EBI-346882; CC Q9UK41-2; Q99598: TSNAX; NbExp=6; IntAct=EBI-12146727, EBI-742638; CC Q9UK41-2; O75604: USP2; NbExp=3; IntAct=EBI-12146727, EBI-743272; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11916981}. Late CC endosome membrane {ECO:0000269|PubMed:11916981}; Peripheral membrane CC protein {ECO:0000269|PubMed:11916981}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UK41-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UK41-2; Sequence=VSP_042028; CC -!- SIMILARITY: Belongs to the VPS28 family. {ECO:0000255|PROSITE- CC ProRule:PRU00642, ECO:0000255|PROSITE-ProRule:PRU00645}. 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; AF182844; AAF00499.1; -; mRNA. DR EMBL; AF205589; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC006485; AAH06485.1; -; mRNA. DR EMBL; BC019321; AAH19321.1; -; mRNA. DR EMBL; BC050713; AAH50713.1; -; mRNA. DR CCDS; CCDS34967.1; -. [Q9UK41-2] DR CCDS; CCDS6425.1; -. [Q9UK41-1] DR RefSeq; NP_057292.1; NM_016208.3. [Q9UK41-1] DR RefSeq; NP_898880.1; NM_183057.2. [Q9UK41-2] DR PDB; 6VME; X-ray; 2.19 A; E/U/V/W/X/Y=1-122. DR PDBsum; 6VME; -. DR AlphaFoldDB; Q9UK41; -. DR BMRB; Q9UK41; -. DR SMR; Q9UK41; -. DR BioGRID; 119341; 118. DR ComplexPortal; CPX-2505; ESCRT-I complex, VPS37B-MVB12A variant. DR ComplexPortal; CPX-7146; ESCRT-I complex, VPS37A-MVB12B variant. DR ComplexPortal; CPX-7147; ESCRT-I complex, VPS37C-MVB12A variant. DR ComplexPortal; CPX-7148; ESCRT-I complex, VPS37D-MVB12A variant. DR ComplexPortal; CPX-7162; ESCRT-I complex, VPS37A-MVB12A variant. DR ComplexPortal; CPX-7164; ESCRT-I complex, VPS37B-MVB12B variant. DR ComplexPortal; CPX-7166; ESCRT-I complex, VPS37C-MVB12B variant. DR ComplexPortal; CPX-7167; ESCRT-I complex, VPS37D-MVB12B variant. DR ComplexPortal; CPX-7181; ESCRT-I complex, VPS37A-UBAP1 variant. DR ComplexPortal; CPX-7201; ESCRT-I complex, VPS37B-UBAP1 variant. DR ComplexPortal; CPX-7202; ESCRT-I complex, VPS37C-UBAP1 variant. DR ComplexPortal; CPX-7203; ESCRT-I complex, VPS37D-UBAP1 variant. DR CORUM; Q9UK41; -. DR IntAct; Q9UK41; 70. DR MINT; Q9UK41; -. DR STRING; 9606.ENSP00000366565; -. DR GlyGen; Q9UK41; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UK41; -. DR MetOSite; Q9UK41; -. DR PhosphoSitePlus; Q9UK41; -. DR SwissPalm; Q9UK41; -. DR BioMuta; VPS28; -. DR DMDM; 13124619; -. DR EPD; Q9UK41; -. DR jPOST; Q9UK41; -. DR MassIVE; Q9UK41; -. DR MaxQB; Q9UK41; -. DR PaxDb; 9606-ENSP00000366565; -. DR PeptideAtlas; Q9UK41; -. DR ProteomicsDB; 84715; -. [Q9UK41-1] DR ProteomicsDB; 84716; -. [Q9UK41-2] DR Pumba; Q9UK41; -. DR TopDownProteomics; Q9UK41-1; -. [Q9UK41-1] DR Antibodypedia; 14872; 231 antibodies from 32 providers. DR DNASU; 51160; -. DR Ensembl; ENST00000292510.6; ENSP00000292510.3; ENSG00000160948.14. [Q9UK41-1] DR Ensembl; ENST00000377348.6; ENSP00000366565.2; ENSG00000160948.14. [Q9UK41-2] DR Ensembl; ENST00000526054.5; ENSP00000434064.1; ENSG00000160948.14. [Q9UK41-1] DR Ensembl; ENST00000529182.5; ENSP00000434556.1; ENSG00000160948.14. [Q9UK41-2] DR Ensembl; ENST00000642202.1; ENSP00000494521.1; ENSG00000285339.2. [Q9UK41-2] DR Ensembl; ENST00000642867.1; ENSP00000496519.1; ENSG00000285339.2. [Q9UK41-1] DR Ensembl; ENST00000643186.2; ENSP00000496693.1; ENSG00000285339.2. [Q9UK41-1] DR Ensembl; ENST00000646588.1; ENSP00000495408.1; ENSG00000285339.2. [Q9UK41-2] DR GeneID; 51160; -. DR KEGG; hsa:51160; -. DR MANE-Select; ENST00000292510.6; ENSP00000292510.3; NM_016208.4; NP_057292.1. DR UCSC; uc003zcs.2; human. [Q9UK41-1] DR AGR; HGNC:18178; -. DR CTD; 51160; -. DR DisGeNET; 51160; -. DR GeneCards; VPS28; -. DR HGNC; HGNC:18178; VPS28. DR HPA; ENSG00000160948; Low tissue specificity. DR MIM; 611952; gene. DR neXtProt; NX_Q9UK41; -. DR OpenTargets; ENSG00000160948; -. DR PharmGKB; PA38512; -. DR VEuPathDB; HostDB:ENSG00000160948; -. DR eggNOG; KOG3284; Eukaryota. DR GeneTree; ENSGT00390000007486; -. DR HOGENOM; CLU_076417_2_0_1; -. DR InParanoid; Q9UK41; -. DR OMA; CDEFPTV; -. DR OrthoDB; 5486880at2759; -. DR PhylomeDB; Q9UK41; -. DR TreeFam; TF313364; -. DR PathwayCommons; Q9UK41; -. DR Reactome; R-HSA-162588; Budding and maturation of HIV virion. DR Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins. DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT). DR Reactome; R-HSA-9610379; HCMV Late Events. DR Reactome; R-HSA-9615710; Late endosomal microautophagy. DR SignaLink; Q9UK41; -. DR BioGRID-ORCS; 51160; 839 hits in 1172 CRISPR screens. DR ChiTaRS; VPS28; human. DR GeneWiki; VPS28; -. DR GenomeRNAi; 51160; -. DR Pharos; Q9UK41; Tbio. DR PRO; PR:Q9UK41; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q9UK41; Protein. DR Bgee; ENSG00000160948; Expressed in right uterine tube and 101 other cell types or tissues. DR ExpressionAtlas; Q9UK41; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB. DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central. DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB. DR GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL. DR GO; GO:0090148; P:membrane fission; NAS:ComplexPortal. DR GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL. DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB. DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:UniProtKB. DR GO; GO:2000397; P:positive regulation of ubiquitin-dependent endocytosis; IMP:UniProtKB. DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central. DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB. DR GO; GO:0039702; P:viral budding via host ESCRT complex; TAS:ParkinsonsUK-UCL. DR Gene3D; 1.20.120.1130; -; 1. DR Gene3D; 1.20.1440.200; -; 1. DR InterPro; IPR037202; ESCRT_assembly_dom. DR InterPro; IPR007143; Vps28. DR InterPro; IPR017899; VPS28_C. DR InterPro; IPR037206; VPS28_C_sf. DR InterPro; IPR017898; VPS28_N. DR InterPro; IPR038358; VPS28_N_sf. DR PANTHER; PTHR12937; VACUOLAR PROTEIN SORTING 28, ISOFORM 2 VPS28; 1. DR PANTHER; PTHR12937:SF0; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 28 HOMOLOG; 1. DR Pfam; PF03997; VPS28; 1. DR PIRSF; PIRSF017535; VPS28; 1. DR SUPFAM; SSF140111; Endosomal sorting complex assembly domain; 1. DR SUPFAM; SSF140427; VPS28 C-terminal domain-like; 1. DR PROSITE; PS51310; VPS28_C; 1. DR PROSITE; PS51313; VPS28_N; 1. DR Genevisible; Q9UK41; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; Endosome; KW Membrane; Protein transport; Reference proteome; Transport. FT CHAIN 1..221 FT /note="Vacuolar protein sorting-associated protein 28 FT homolog" FT /id="PRO_0000120951" FT DOMAIN 13..120 FT /note="VPS28 N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00645" FT DOMAIN 124..220 FT /note="VPS28 C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00642" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:25944712" FT VAR_SEQ 184..221 FT /note="LQTLSGMSASDELDDSQVRQMLFDLESAYNAFNRFLHA -> WVSLPARQSP FT AVPETLPARRSPAVPLRPSAPTCPVLHSQAADPERHVGVR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_042028" FT HELIX 30..57 FT /evidence="ECO:0007829|PDB:6VME" FT HELIX 63..84 FT /evidence="ECO:0007829|PDB:6VME" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:6VME" FT HELIX 92..98 FT /evidence="ECO:0007829|PDB:6VME" FT HELIX 104..112 FT /evidence="ECO:0007829|PDB:6VME" SQ SEQUENCE 221 AA; 25425 MW; B2E1697B82D02AB8 CRC64; MFHGIPATPG IGAPGNKPEL YEEVKLYKNA REREKYDNMA ELFAVVKTMQ ALEKAYIKDC VSPSEYTAAC SRLLVQYKAA FRQVQGSEIS SIDEFCRKFR LDCPLAMERI KEDRPITIKD DKGNLNRCIA DVVSLFITVM DKLRLEIRAM DEIQPDLREL METMHRMSHL PPDFEGRQTV SQWLQTLSGM SASDELDDSQ VRQMLFDLES AYNAFNRFLH A //