ID   UCP1_HUMAN              Reviewed;         307 AA.
AC   P25874; Q13218; Q4KMZ3; Q68G66;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 3.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Mitochondrial brown fat uncoupling protein 1 {ECO:0000305};
DE            Short=UCP 1 {ECO:0000305};
DE   AltName: Full=Solute carrier family 25 member 7 {ECO:0000303|PubMed:23266187};
DE   AltName: Full=Thermogenin {ECO:0000250|UniProtKB:P04575};
GN   Name=UCP1 {ECO:0000312|HGNC:HGNC:12517};
GN   Synonyms=SLC25A7 {ECO:0000303|PubMed:23266187}, UCP
GN   {ECO:0000303|PubMed:2380264};
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].
RX   PubMed=2380264; DOI=10.1002/jcb.240430306;
RA   Cassard A.M., Bouillaud F., Mattei M.-G., Hentz E., Raimbault S.,
RA   Thomas M., Ricquier D.;
RT   "Human uncoupling protein gene: structure, comparison with rat gene, and
RT   assignment to the long arm of chromosome 4.";
RL   J. Cell. Biochem. 43:255-264(1990).
RN   [2]
RP   SEQUENCE REVISION.
RA   Bouillaud F.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brown adipose tissue;
RA   Bouillaud F., Ricquier D., Raimbault S.;
RT   "Sequence of the cDNA coding for the human uncoupling protein UCP.";
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-196, AND TISSUE SPECIFICITY.
RC   TISSUE=Brown adipose tissue;
RX   PubMed=3165741; DOI=10.1042/cs0750021;
RA   Bouillaud F., Villarroya F., Hentz E., Raimbault S., Cassard A.M.,
RA   Ricquier D.;
RT   "Detection of brown adipose tissue uncoupling protein mRNA in adult
RT   patients by a human genomic probe.";
RL   Clin. Sci. 75:21-27(1988).
RN   [7]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND SUBUNIT.
RX   PubMed=24196960; DOI=10.1074/jbc.m113.509935;
RA   Hoang T., Smith M.D., Jelokhani-Niaraki M.;
RT   "Expression, folding, and proton transport activity of human uncoupling
RT   protein-1 (UCP1) in lipid membranes: evidence for associated functional
RT   forms.";
RL   J. Biol. Chem. 288:36244-36258(2013).
RN   [8]
RP   NOMENCLATURE.
RX   PubMed=23266187; DOI=10.1016/j.mam.2012.05.005;
RA   Palmieri F.;
RT   "The mitochondrial transporter family SLC25: identification, properties and
RT   physiopathology.";
RL   Mol. Aspects Med. 34:465-484(2013).
RN   [9]
RP   VARIANT LEU-229.
RX   PubMed=11317671; DOI=10.1007/s001250051629;
RA   Mori H., Okazawa H., Iwamoto K., Maeda E., Hashiramoto M., Kasuga M.;
RT   "A polymorphism in the 5' untranslated region and a Met229-->Leu variant in
RT   exon 5 of the human UCP1 gene are associated with susceptibility to type II
RT   diabetes mellitus.";
RL   Diabetologia 44:373-376(2001).
RN   [10]
RP   VARIANT THR-64.
RX   PubMed=12756473; DOI=10.1007/s00109-003-0431-1;
RA   Herrmann S.M., Wang J.G., Staessen J.A., Kertmen E., Schmidt-Petersen K.,
RA   Zidek W., Paul M., Brand E.;
RT   "Uncoupling protein 1 and 3 polymorphisms are associated with waist-to-hip
RT   ratio.";
RL   J. Mol. Med. 81:327-332(2003).
RN   [11]
RP   FUNCTION, TRANSPORTER ACTIVITY, LONG-CHAIN FATTY ACID BINDING, MUTAGENESIS
RP   OF LYS-38; ARG-54; LYS-56 AND LYS-269, AND ACTIVITY REGULATION.
RX   PubMed=28781081; DOI=10.1016/j.str.2017.07.005;
RA   Zhao L., Wang S., Zhu Q., Wu B., Liu Z., Ouyang B., Chou J.J.;
RT   "Specific Interaction of the Human Mitochondrial Uncoupling Protein 1 with
RT   Free Long-Chain Fatty Acid.";
RL   Structure 25:1371-1379(2017).
CC   -!- FUNCTION: Mitochondrial protein responsible for thermogenic
CC       respiration, a specialized capacity of brown adipose tissue and beige
CC       fat that participates in non-shivering adaptive thermogenesis to
CC       temperature and diet variations and more generally to the regulation of
CC       energy balance (By similarity). Functions as a long-chain fatty
CC       acid/LCFA and proton symporter, simultaneously transporting one LCFA
CC       and one proton through the inner mitochondrial membrane
CC       (PubMed:24196960, PubMed:28781081). However, LCFAs remaining associated
CC       with the transporter via their hydrophobic tails, it results in an
CC       apparent transport of protons activated by LCFAs. Thereby, dissipates
CC       the mitochondrial proton gradient and converts the energy of substrate
CC       oxydation into heat instead of ATP. Regulates the production of
CC       reactive oxygen species/ROS by mitochondria (By similarity).
CC       {ECO:0000250|UniProtKB:P12242, ECO:0000269|PubMed:24196960,
CC       ECO:0000269|PubMed:28781081}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378;
CC         Evidence={ECO:0000269|PubMed:24196960, ECO:0000269|PubMed:28781081};
CC   -!- ACTIVITY REGULATION: Has no constitutive proton transporter activity
CC       and has to be activated by long-chain fatty acids/LCFAs
CC       (PubMed:28781081). Inhibited by purine nucleotides (PubMed:28781081).
CC       Both purine nucleotides and LCFAs bind the cytosolic side of the
CC       transporter and directly compete to activate or inhibit it
CC       (PubMed:28781081). Activated by noradrenaline and reactive oxygen
CC       species. Despite lacking canonical translational encoding for
CC       selenocysteine, a small pool of the protein has been observed to
CC       selectively incorporate selenocysteine at 'Cys-254'. Selenocysteine-
CC       modified protein is highly sensitive to redox modification and may
CC       constitute a pool of protein highly sensitive to activation by elevated
CC       levels of reactive oxygen species (ROS). {ECO:0000250|UniProtKB:P12242,
CC       ECO:0000269|PubMed:28781081}.
CC   -!- SUBUNIT: Most probably functions as a monomer. Binds one purine
CC       nucleotide per monomer (By similarity). However, has also been
CC       suggested to function as a homodimer or a homotetramer
CC       (PubMed:24196960). Tightly associates with cardiolipin in the
CC       mitochondrion inner membrane; may stabilize and regulate its activity
CC       (PubMed:24196960). {ECO:0000250|UniProtKB:W5PSH7,
CC       ECO:0000269|PubMed:24196960}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P12242}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Brown adipose tissue. {ECO:0000269|PubMed:3165741}.
CC   -!- PTM: May undergo sulfenylation upon cold exposure. May increase the
CC       sensitivity of UCP1 thermogenic function to the activation by
CC       noradrenaline probably through structural effects.
CC       {ECO:0000250|UniProtKB:P12242}.
CC   -!- PTM: May undergo ubiquitin-mediated proteasomal degradation.
CC       {ECO:0000250|UniProtKB:P04633}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=A touch of warmth - Issue
CC       195 of September 2017;
CC       URL="https://web.expasy.org/spotlight/back_issues/195/";
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DR   EMBL; X51952; CAA36214.1; -; Genomic_DNA.
DR   EMBL; X51953; CAA36214.1; JOINED; Genomic_DNA.
DR   EMBL; X51954; CAA36214.1; JOINED; Genomic_DNA.
DR   EMBL; X51955; CAA36214.1; JOINED; Genomic_DNA.
DR   EMBL; U28480; AAA85271.1; -; mRNA.
DR   EMBL; AC108019; AAY41026.1; -; Genomic_DNA.
DR   EMBL; BC069556; AAH69556.1; -; mRNA.
DR   EMBL; BC098168; AAH98168.1; -; mRNA.
DR   EMBL; BC098258; AAH98258.1; -; mRNA.
DR   CCDS; CCDS3753.1; -.
DR   PIR; G01858; G01858.
DR   RefSeq; NP_068605.1; NM_021833.4.
DR   PDB; 8G8W; EM; 3.80 A; A=2-307.
DR   PDB; 8HBV; EM; 2.51 A; A=1-307.
DR   PDB; 8HBW; EM; 2.57 A; A=1-307.
DR   PDB; 8J1N; EM; 2.51 A; A=1-307.
DR   PDBsum; 8G8W; -.
DR   PDBsum; 8HBV; -.
DR   PDBsum; 8HBW; -.
DR   PDBsum; 8J1N; -.
DR   AlphaFoldDB; P25874; -.
DR   EMDB; EMD-34644; -.
DR   EMDB; EMD-34645; -.
DR   EMDB; EMD-35928; -.
DR   SMR; P25874; -.
DR   BioGRID; 113197; 4.
DR   IntAct; P25874; 1.
DR   STRING; 9606.ENSP00000262999; -.
DR   TCDB; 2.A.29.3.2; the mitochondrial carrier (mc) family.
DR   iPTMnet; P25874; -.
DR   PhosphoSitePlus; P25874; -.
DR   BioMuta; UCP1; -.
DR   DMDM; 71153184; -.
DR   jPOST; P25874; -.
DR   MassIVE; P25874; -.
DR   PaxDb; 9606-ENSP00000262999; -.
DR   PeptideAtlas; P25874; -.
DR   ProteomicsDB; 54299; -.
DR   Antibodypedia; 16250; 505 antibodies from 38 providers.
DR   DNASU; 7350; -.
DR   Ensembl; ENST00000262999.4; ENSP00000262999.3; ENSG00000109424.4.
DR   GeneID; 7350; -.
DR   KEGG; hsa:7350; -.
DR   MANE-Select; ENST00000262999.4; ENSP00000262999.3; NM_021833.5; NP_068605.1.
DR   UCSC; uc011chj.3; human.
DR   AGR; HGNC:12517; -.
DR   CTD; 7350; -.
DR   DisGeNET; 7350; -.
DR   GeneCards; UCP1; -.
DR   HGNC; HGNC:12517; UCP1.
DR   HPA; ENSG00000109424; Tissue enhanced (adrenal).
DR   MIM; 113730; gene.
DR   neXtProt; NX_P25874; -.
DR   OpenTargets; ENSG00000109424; -.
DR   PharmGKB; PA37164; -.
DR   VEuPathDB; HostDB:ENSG00000109424; -.
DR   eggNOG; KOG0753; Eukaryota.
DR   GeneTree; ENSGT00940000160382; -.
DR   HOGENOM; CLU_015166_14_2_1; -.
DR   InParanoid; P25874; -.
DR   OMA; NCAMKMF; -.
DR   OrthoDB; 1832865at2759; -.
DR   PhylomeDB; P25874; -.
DR   TreeFam; TF323211; -.
DR   PathwayCommons; P25874; -.
DR   Reactome; R-HSA-167826; The fatty acid cycling model.
DR   Reactome; R-HSA-167827; The proton buffering model.
DR   SignaLink; P25874; -.
DR   SIGNOR; P25874; -.
DR   BioGRID-ORCS; 7350; 12 hits in 1152 CRISPR screens.
DR   GeneWiki; Thermogenin; -.
DR   GenomeRNAi; 7350; -.
DR   Pharos; P25874; Tbio.
DR   PRO; PR:P25874; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P25874; Protein.
DR   Bgee; ENSG00000109424; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 52 other cell types or tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:1901612; F:cardiolipin binding; ISS:UniProtKB.
DR   GO; GO:0019003; F:GDP binding; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:Ensembl.
DR   GO; GO:0036041; F:long-chain fatty acid binding; IDA:UniProtKB.
DR   GO; GO:0017077; F:oxidative phosphorylation uncoupler activity; ISS:UniProtKB.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0032555; F:purine ribonucleotide binding; ISS:UniProtKB.
DR   GO; GO:0022857; F:transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:1990845; P:adaptive thermogenesis; ISS:UniProtKB.
DR   GO; GO:0050873; P:brown fat cell differentiation; ISS:HGNC-UCL.
DR   GO; GO:0070417; P:cellular response to cold; IEA:Ensembl.
DR   GO; GO:1903495; P:cellular response to dehydroepiandrosterone; IEA:Ensembl.
DR   GO; GO:0071398; P:cellular response to fatty acid; ISS:UniProtKB.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; ISS:UniProtKB.
DR   GO; GO:0034614; P:cellular response to reactive oxygen species; ISS:UniProtKB.
DR   GO; GO:0002024; P:diet induced thermogenesis; IEA:Ensembl.
DR   GO; GO:1990542; P:mitochondrial transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:1902600; P:proton transmembrane transport; IDA:UniProtKB.
DR   GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0009409; P:response to cold; IBA:GO_Central.
DR   GO; GO:0031667; P:response to nutrient levels; ISS:UniProtKB.
DR   GO; GO:0009266; P:response to temperature stimulus; ISS:UniProtKB.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   PANTHER; PTHR45618:SF19; MITOCHONDRIAL BROWN FAT UNCOUPLING PROTEIN 1; 1.
DR   PANTHER; PTHR45618; MITOCHONDRIAL DICARBOXYLATE CARRIER-RELATED; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00784; MTUNCOUPLING.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
DR   Genevisible; P25874; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Diabetes mellitus; Ion channel; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Obesity; Oxidation;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..307
FT                   /note="Mitochondrial brown fat uncoupling protein 1"
FT                   /id="PRO_0000090657"
FT   TOPO_DOM        1..10
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P04633"
FT   TRANSMEM        11..32
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..73
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P04633"
FT   TRANSMEM        74..96
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..116
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P04633"
FT   TRANSMEM        117..133
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..178
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P04633"
FT   TRANSMEM        179..195
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        196..212
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P04633"
FT   TRANSMEM        213..232
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        233..266
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P04633"
FT   TRANSMEM        267..289
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..307
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P04633"
FT   REPEAT          11..102
FT                   /note="Solcar 1"
FT   REPEAT          111..201
FT                   /note="Solcar 2"
FT   REPEAT          210..295
FT                   /note="Solcar 3"
FT   BINDING         56
FT                   /ligand="fatty acid 16:0"
FT                   /ligand_id="ChEBI:CHEBI:78123"
FT                   /evidence="ECO:0000305|PubMed:28781081"
FT   BINDING         269
FT                   /ligand="fatty acid 16:0"
FT                   /ligand_id="ChEBI:CHEBI:78123"
FT                   /evidence="ECO:0000305|PubMed:28781081"
FT   MOD_RES         254
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000250|UniProtKB:P12242"
FT   VARIANT         64
FT                   /note="A -> T (in dbSNP:rs45539933)"
FT                   /evidence="ECO:0000269|PubMed:12756473"
FT                   /id="VAR_022840"
FT   VARIANT         229
FT                   /note="M -> L (risk factor for type II diabetes mellitus;
FT                   dbSNP:rs2270565)"
FT                   /evidence="ECO:0000269|PubMed:11317671"
FT                   /id="VAR_022841"
FT   MUTAGEN         38
FT                   /note="K->S: Does not affect H(+) transmembrane transport
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:28781081"
FT   MUTAGEN         54
FT                   /note="R->S: Does not affect H(+) transmembrane transport
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:28781081"
FT   MUTAGEN         56
FT                   /note="K->S: Severely reduced H(+) transmembrane transport
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:28781081"
FT   MUTAGEN         269
FT                   /note="K->S: Severely reduced H(+) transmembrane transport
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:28781081"
FT   CONFLICT        21
FT                   /note="G -> P (in Ref. 1; CAA36214)"
FT                   /evidence="ECO:0000305"
FT   HELIX           13..42
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   TURN            43..46
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   HELIX           58..69
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   TURN            72..77
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   HELIX           78..105
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   TURN            106..108
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   HELIX           113..143
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   STRAND          146..149
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   HELIX           157..168
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   HELIX           171..174
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   HELIX           177..204
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   HELIX           212..242
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   HELIX           251..262
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   HELIX           266..268
FT                   /evidence="ECO:0007829|PDB:8HBV"
FT   HELIX           271..297
FT                   /evidence="ECO:0007829|PDB:8HBV"
SQ   SEQUENCE   307 AA;  33005 MW;  BCC99AB27171FC67 CRC64;
     MGGLTASDVH PTLGVQLFSA GIAACLADVI TFPLDTAKVR LQVQGECPTS SVIRYKGVLG
     TITAVVKTEG RMKLYSGLPA GLQRQISSAS LRIGLYDTVQ EFLTAGKETA PSLGSKILAG
     LTTGGVAVFI GQPTEVVKVR LQAQSHLHGI KPRYTGTYNA YRIIATTEGL TGLWKGTTPN
     LMRSVIINCT ELVTYDLMKE AFVKNNILAD DVPCHLVSAL IAGFCATAMS SPVDVVKTRF
     INSPPGQYKS VPNCAMKVFT NEGPTAFFKG LVPSFLRLGS WNVIMFVCFE QLKRELSKSR
     QTMDCAT
//