ID HERP1_HUMAN Reviewed; 391 AA. AC Q15011; E9PGD1; O60644; Q6IAN8; Q96D92; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 203. DE RecName: Full=Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein; DE AltName: Full=Methyl methanesulfonate (MMF)-inducible fragment protein 1; GN Name=HERPUD1; Synonyms=HERP, KIAA0025, MIF1; 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), INDUCTION, SUBCELLULAR LOCATION, RP AND MEMBRANE TOPOLOGY. RC TISSUE=Umbilical vein endothelial cell; RX PubMed=10922362; DOI=10.1074/jbc.m002063200; RA Kokame K., Agarwala K.L., Kato H., Miyata T.; RT "Herp, a new ubiquitin-like membrane protein induced by endoplasmic RT reticulum stress."; RL J. Biol. Chem. 275:32846-32853(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7584026; DOI=10.1093/dnares/1.1.27; RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., RA Nagase T., Seki N., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. I. The RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of RT randomly sampled cDNA clones from human immature myeloid cell line KG-1."; RL DNA Res. 1:27-35(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11112790; DOI=10.1074/jbc.m010486200; RA Kokame K., Kato H., Miyata T.; RT "Identification of ERSE-II, a new cis-acting element responsible for the RT ATF6-dependent mammalian unfolded protein response."; RL J. Biol. Chem. 276:9199-9205(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Brain, Eye, Placenta, 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 [8] RP INTERACTION WITH PSEN1 AND PSEN2. RX PubMed=11799129; DOI=10.1074/jbc.m112372200; RA Sai X., Kawamura Y., Kokame K., Yamaguchi H., Shiraishi H., Suzuki R., RA Suzuki T., Kawaichi M., Miyata T., Kitamura T., De Strooper B., RA Yanagisawa K., Komano H.; RT "Endoplasmic reticulum stress-inducible protein, Herp, enhances presenilin- RT mediated generation of amyloid beta-protein."; RL J. Biol. Chem. 277:12915-12920(2002). RN [9] RP CHARACTERIZATION. RC TISSUE=Skin fibroblast; RX PubMed=10708769; DOI=10.1016/s0014-5793(00)01253-9; RA van Laar T., Schouten T., Hoogervorst E., van Eck M., van der Eb A.J., RA Terleth C.; RT "The novel MMS-inducible gene Mif1/KIAA0025 is a target of the unfolded RT protein response pathway."; RL FEBS Lett. 469:123-131(2000). RN [10] RP FUNCTION, AND INTERACTION WITH SYVN1. RX PubMed=16289116; DOI=10.1016/j.jmb.2005.10.020; RA Schulze A., Standera S., Buerger E., Kikkert M., van Voorden S., Wiertz E., RA Koning F., Kloetzel P.-M., Seeger M.; RT "The ubiquitin-domain protein HERP forms a complex with components of the RT endoplasmic reticulum associated degradation pathway."; RL J. Mol. Biol. 354:1021-1027(2005). RN [11] RP INDUCTION. RX PubMed=16940180; DOI=10.1128/mcb.01046-06; RA Liang G., Audas T.E., Li Y., Cockram G.P., Dean J.D., Martyn A.C., RA Kokame K., Lu R.; RT "Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress RT response protein Herp through an ER stress response element."; RL Mol. Cell. Biol. 26:7999-8010(2006). RN [12] RP FUNCTION, AND INTERACTION WITH UBQLN1; UBQLN2 AND UBQLN4. RX PubMed=18307982; DOI=10.1016/j.bbrc.2008.02.086; RA Kim T.Y., Kim E., Yoon S.K., Yoon J.B.; RT "Herp enhances ER-associated protein degradation by recruiting RT ubiquilins."; RL Biochem. Biophys. Res. Commun. 369:741-746(2008). RN [13] RP INTERACTION WITH UBXN6. RX PubMed=18656546; DOI=10.1016/j.biocel.2008.06.008; RA Madsen L., Andersen K.M., Prag S., Moos T., Semple C.A., Seeger M., RA Hartmann-Petersen R.; RT "Ubxd1 is a novel co-factor of the human p97 ATPase."; RL Int. J. Biochem. Cell Biol. 40:2927-2942(2008). RN [14] 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP FUNCTION, AND IDENTIFICATION IN THE HRD1 COMPLEX. RX PubMed=28827405; DOI=10.1242/jcs.206847; RA Schulz J., Avci D., Queisser M.A., Gutschmidt A., Dreher L.S., Fenech E.J., RA Volkmar N., Hayashi Y., Hoppe T., Christianson J.C.; RT "Conserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex RT formation for ER-associated degradation (ERAD)."; RL J. Cell Sci. 130:3322-3335(2017). RN [18] RP STRUCTURE BY NMR OF 10-90. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the UBL-domain of HERP."; RL Submitted (NOV-2004) to the PDB data bank. CC -!- FUNCTION: Component of the endoplasmic reticulum quality control (ERQC) CC system also called ER-associated degradation (ERAD) involved in CC ubiquitin-dependent degradation of misfolded endoplasmic reticulum CC proteins (PubMed:16289116, PubMed:28827405). Could enhance presenilin- CC mediated amyloid-beta protein 40 generation. Binds to ubiquilins and CC this interaction is required for efficient degradation of CD3D via the CC ERAD pathway (PubMed:18307982). {ECO:0000269|PubMed:16289116, CC ECO:0000269|PubMed:18307982, ECO:0000269|PubMed:28827405}. CC -!- SUBUNIT: Interacts with PSEN1 and PSEN2 (PubMed:11799129). Interacts CC with UBXN6 (PubMed:18656546). Interacts with UBQLN1, UBQLN2 and UBQLN4 CC (PubMed:18307982). Component of the HRD1 complex, which comprises at CC least SYNV1/HRD1, FAM8A1, HERPUD1/HERP, OS9, SEL1L and UBE2J1. FAM8A1 CC binding to SYNV1 may promote recruitment of HERPUD1 to the HRD1 complex CC (PubMed:16289116, PubMed:28827405). {ECO:0000269|PubMed:11799129, CC ECO:0000269|PubMed:16289116, ECO:0000269|PubMed:18307982, CC ECO:0000269|PubMed:18656546, ECO:0000269|PubMed:28827405}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:10922362}; Multi-pass membrane protein CC {ECO:0000269|PubMed:10922362}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=1; CC IsoId=Q15011-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15011-2; Sequence=VSP_006708; CC Name=3; CC IsoId=Q15011-3; Sequence=VSP_006708, VSP_006709; CC Name=4; CC IsoId=Q15011-4; Sequence=VSP_047333; CC -!- TISSUE SPECIFICITY: Widely expressed; in the brain, expression seems to CC be restricted to neurons and vascular smooth muscle cells. Present in CC activated microglia in senile plaques in the brain of patients with CC Alzheimer disease. CC -!- INDUCTION: Up-regulated by endoplasmic reticulum stress and CREB3. CC {ECO:0000269|PubMed:10922362, ECO:0000269|PubMed:16940180}. CC -!- MISCELLANEOUS: Although the precise topology is not known, experimental CC data suggest that both the N- and C-termini face the cytosol. 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; AB034989; BAB07891.1; -; mRNA. DR EMBL; D14695; BAA03521.1; -; mRNA. DR EMBL; AF055001; AAC09355.1; -; mRNA. DR EMBL; AF055003; AAC09357.1; -; mRNA. DR EMBL; AB034990; BAB19010.1; -; Genomic_DNA. DR EMBL; CR457116; CAG33397.1; -; mRNA. DR EMBL; AC012181; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000086; AAH00086.1; -; mRNA. DR EMBL; BC008320; AAH08320.1; -; mRNA. DR EMBL; BC009739; AAH09739.1; -; mRNA. DR EMBL; BC032673; AAH32673.1; -; mRNA. DR CCDS; CCDS10771.1; -. [Q15011-1] DR CCDS; CCDS45492.1; -. [Q15011-2] DR RefSeq; NP_001010989.1; NM_001010989.2. [Q15011-2] DR RefSeq; NP_001259032.1; NM_001272103.1. DR RefSeq; NP_055500.1; NM_014685.3. [Q15011-1] DR PDB; 1WGD; NMR; -; A=10-90. DR PDBsum; 1WGD; -. DR AlphaFoldDB; Q15011; -. DR SMR; Q15011; -. DR BioGRID; 115060; 51. DR DIP; DIP-46662N; -. DR IntAct; Q15011; 23. DR MINT; Q15011; -. DR STRING; 9606.ENSP00000409555; -. DR iPTMnet; Q15011; -. DR PhosphoSitePlus; Q15011; -. DR SwissPalm; Q15011; -. DR BioMuta; HERPUD1; -. DR DMDM; 3123034; -. DR EPD; Q15011; -. DR jPOST; Q15011; -. DR MassIVE; Q15011; -. DR MaxQB; Q15011; -. DR PaxDb; 9606-ENSP00000409555; -. DR PeptideAtlas; Q15011; -. DR ProteomicsDB; 20293; -. DR ProteomicsDB; 60361; -. [Q15011-1] DR ProteomicsDB; 60362; -. [Q15011-2] DR ProteomicsDB; 60363; -. [Q15011-3] DR Pumba; Q15011; -. DR Antibodypedia; 28691; 324 antibodies from 33 providers. DR DNASU; 9709; -. DR Ensembl; ENST00000300302.9; ENSP00000300302.5; ENSG00000051108.15. [Q15011-2] DR Ensembl; ENST00000344114.8; ENSP00000340931.4; ENSG00000051108.15. [Q15011-3] DR Ensembl; ENST00000379792.6; ENSP00000369118.2; ENSG00000051108.15. [Q15011-4] DR Ensembl; ENST00000439977.7; ENSP00000409555.2; ENSG00000051108.15. [Q15011-1] DR GeneID; 9709; -. DR KEGG; hsa:9709; -. DR MANE-Select; ENST00000439977.7; ENSP00000409555.2; NM_014685.4; NP_055500.1. DR UCSC; uc002eke.3; human. [Q15011-1] DR AGR; HGNC:13744; -. DR CTD; 9709; -. DR DisGeNET; 9709; -. DR GeneCards; HERPUD1; -. DR HGNC; HGNC:13744; HERPUD1. DR HPA; ENSG00000051108; Low tissue specificity. DR MalaCards; HERPUD1; -. DR MIM; 608070; gene. DR neXtProt; NX_Q15011; -. DR OpenTargets; ENSG00000051108; -. DR PharmGKB; PA29252; -. DR VEuPathDB; HostDB:ENSG00000051108; -. DR eggNOG; KOG4583; Eukaryota. DR GeneTree; ENSGT00390000017671; -. DR HOGENOM; CLU_1194535_0_0_1; -. DR InParanoid; Q15011; -. DR OMA; MSTAWVF; -. DR OrthoDB; 5406902at2759; -. DR PhylomeDB; Q15011; -. DR TreeFam; TF324319; -. DR PathwayCommons; Q15011; -. DR Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress. DR SignaLink; Q15011; -. DR SIGNOR; Q15011; -. DR BioGRID-ORCS; 9709; 17 hits in 1154 CRISPR screens. DR ChiTaRS; HERPUD1; human. DR EvolutionaryTrace; Q15011; -. DR GeneWiki; HERPUD1; -. DR GenomeRNAi; 9709; -. DR Pharos; Q15011; Tbio. DR PRO; PR:Q15011; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q15011; Protein. DR Bgee; ENSG00000051108; Expressed in body of pancreas and 205 other cell types or tissues. DR ExpressionAtlas; Q15011; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:Ensembl. DR GO; GO:1990037; C:Lewy body core; IDA:ParkinsonsUK-UCL. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:ParkinsonsUK-UCL. DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IEA:Ensembl. DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IDA:ParkinsonsUK-UCL. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central. DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL. DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IGI:ParkinsonsUK-UCL. DR GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:1904294; P:positive regulation of ERAD pathway; IDA:ParkinsonsUK-UCL. DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IDA:ParkinsonsUK-UCL. DR GO; GO:0045047; P:protein targeting to ER; IEA:Ensembl. DR GO; GO:1903069; P:regulation of ER-associated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0031396; P:regulation of protein ubiquitination; IEA:Ensembl. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; TAS:ParkinsonsUK-UCL. DR GO; GO:0006986; P:response to unfolded protein; IEP:UniProtKB. DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR CDD; cd17118; Ubl_HERP1; 1. DR InterPro; IPR039751; HERPUD1/2. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR12943:SF7; HOMOCYSTEINE-RESPONSIVE ENDOPLASMIC RETICULUM-RESIDENT UBIQUITIN-LIKE DOMAIN MEMBER 1 PROTEIN; 1. DR PANTHER; PTHR12943; HOMOCYSTEINE-RESPONSIVE ENDOPLASMIC RETICULUM-RESIDENT UNIQUITIN-LIKE DOMAIN HERPUD PROTEIN FAMILY MEMBER; 1. DR Pfam; PF00240; ubiquitin; 1. DR SMART; SM00213; UBQ; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. DR Genevisible; Q15011; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Endoplasmic reticulum; KW Membrane; Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix; Unfolded protein response. FT CHAIN 1..391 FT /note="Homocysteine-responsive endoplasmic reticulum- FT resident ubiquitin-like domain member 1 protein" FT /id="PRO_0000114920" FT TOPO_DOM 1..263 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 264..284 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 285..289 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 290..310 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 311..391 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 10..72 FT /note="Ubiquitin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT REGION 100..126 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 115..200 FT /note="Interaction with UBQLN1" FT /evidence="ECO:0000269|PubMed:18307982" FT REGION 170..190 FT /note="Interaction with SYVN1" FT /evidence="ECO:0000269|PubMed:28827405" FT REGION 318..359 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 327..341 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 342..356 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 135 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 75..99 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_047333" FT VAR_SEQ 76 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_006708" FT VAR_SEQ 145..302 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_006709" FT VARIANT 50 FT /note="R -> H (in dbSNP:rs2217332)" FT /id="VAR_024277" FT STRAND 11..15 FT /evidence="ECO:0007829|PDB:1WGD" FT STRAND 17..20 FT /evidence="ECO:0007829|PDB:1WGD" FT STRAND 24..27 FT /evidence="ECO:0007829|PDB:1WGD" FT HELIX 34..44 FT /evidence="ECO:0007829|PDB:1WGD" FT TURN 51..53 FT /evidence="ECO:0007829|PDB:1WGD" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:1WGD" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:1WGD" FT HELIX 69..72 FT /evidence="ECO:0007829|PDB:1WGD" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:1WGD" FT STRAND 79..85 FT /evidence="ECO:0007829|PDB:1WGD" SQ SEQUENCE 391 AA; 43720 MW; 3CA827DC7EF0ED22 CRC64; MESETEPEPV TLLVKSPNQR HRDLELSGDR GWSVGHLKAH LSRVYPERPR PEDQRLIYSG KLLLDHQCLR DLLPKQEKRH VLHLVCNVKS PSKMPEINAK VAESTEEPAG SNRGQYPEDS SSDGLRQREV LRNLSSPGWE NISRPEAAQQ AFQGLGPGFS GYTPYGWLQL SWFQQIYARQ YYMQYLAATA ASGAFVPPPS AQEIPVVSAP APAPIHNQFP AENQPANQNA APQVVVNPGA NQNLRMNAQG GPIVEEDDEI NRDWLDWTYS AATFSVFLSI LYFYSSLSRF LMVMGATVVM YLHHVGWFPF RPRPVQNFPN DGPPPDVVNQ DPNNNLQEGT DPETEDPNHL PPDRDVLDGE QTSPSFMSTA WLVFKTFFAS LLPEGPPAIA N //