HERP1_HUMAN
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 03-AUG-2022, entry version 194.
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.
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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; 22.
DR MINT; Q15011; -.
DR STRING; 9606.ENSP00000409555; -.
DR iPTMnet; Q15011; -.
DR PhosphoSitePlus; Q15011; -.
DR BioMuta; HERPUD1; -.
DR DMDM; 3123034; -.
DR EPD; Q15011; -.
DR jPOST; Q15011; -.
DR MassIVE; Q15011; -.
DR MaxQB; Q15011; -.
DR PaxDb; Q15011; -.
DR PeptideAtlas; Q15011; -.
DR PRIDE; Q15011; -.
DR ProteomicsDB; 20293; -.
DR ProteomicsDB; 60361; -. [Q15011-1]
DR ProteomicsDB; 60362; -. [Q15011-2]
DR ProteomicsDB; 60363; -. [Q15011-3]
DR Antibodypedia; 28691; 293 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 CTD; 9709; -.
DR DisGeNET; 9709; -.
DR GeneCards; HERPUD1; -.
DR HGNC; HGNC:13744; HERPUD1.
DR HPA; ENSG00000051108; Low tissue specificity.
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; PEVQHNQ; -.
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; 15 hits in 1075 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 203 other tissues.
DR ExpressionAtlas; Q15011; baseline and differential.
DR Genevisible; Q15011; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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 InterPro; IPR039751; HERPUD1/2.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR12943; PTHR12943; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
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
