ELOV6_MOUSE
ID ELOV6_MOUSE Reviewed; 267 AA.
AC Q920L5; Q8CE45;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Elongation of very long chain fatty acids protein 6 {ECO:0000255|HAMAP-Rule:MF_03206, ECO:0000305};
DE EC=2.3.1.199 {ECO:0000255|HAMAP-Rule:MF_03206, ECO:0000269|PubMed:11567032, ECO:0000269|PubMed:17906635};
DE AltName: Full=3-keto acyl-CoA synthase Elovl6 {ECO:0000255|HAMAP-Rule:MF_03206};
DE AltName: Full=ELOVL fatty acid elongase 6 {ECO:0000255|HAMAP-Rule:MF_03206};
DE Short=ELOVL FA elongase 6 {ECO:0000255|HAMAP-Rule:MF_03206};
DE AltName: Full=Fatty acyl-CoA elongase;
DE AltName: Full=Long chain fatty acid elongase;
DE AltName: Full=Myelin-associated SUR4 protein;
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 6 {ECO:0000255|HAMAP-Rule:MF_03206};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 6 {ECO:0000255|HAMAP-Rule:MF_03206};
GN Name=Elovl6 {ECO:0000255|HAMAP-Rule:MF_03206}; Synonyms=Face, Lce, Masr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION BY SREBF1,
RP AND TISSUE SPECIFICITY.
RX PubMed=11567032; DOI=10.1074/jbc.m108413200;
RA Moon Y.-A., Shah N.A., Mohapatra S., Warrington J.A., Horton J.D.;
RT "Identification of a mammalian long chain fatty acyl elongase regulated by
RT sterol regulatory element-binding proteins.";
RL J. Biol. Chem. 276:45358-45366(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY
RP SREBF1.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=12032166;
RA Matsuzaka T., Shimano H., Yahagi N., Yoshikawa T., Amemiya-Kudo M.,
RA Hasty A.H., Okazaki H., Tamura Y., Iizuka Y., Ohashi K., Osuga J.,
RA Takahashi A., Yato S., Sone H., Ishibashi S., Yamada N.;
RT "Cloning and characterization of a mammalian fatty acyl-CoA elongase as a
RT lipogenic enzyme regulated by SREBPs.";
RL J. Lipid Res. 43:911-920(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12084938; DOI=10.1073/pnas.132080999;
RA Nagarajan R., Le N., Mahoney H., Araki T., Milbrandt J.;
RT "Deciphering peripheral nerve myelination by using Schwann cell expression
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8998-9003(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CD-1, and Czech II; TISSUE=Mammary tumor, and Neural stem cell;
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 FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=17906635; DOI=10.1038/nm1662;
RA Matsuzaka T., Shimano H., Yahagi N., Kato T., Atsumi A., Yamamoto T.,
RA Inoue N., Ishikawa M., Okada S., Ishigaki N., Iwasaki H., Iwasaki Y.,
RA Karasawa T., Kumadaki S., Matsui T., Sekiya M., Ohashi K., Hasty A.H.,
RA Nakagawa Y., Takahashi A., Suzuki H., Yatoh S., Sone H., Toyoshima H.,
RA Osuga J., Yamada N.;
RT "Crucial role of a long-chain fatty acid elongase, Elovl6, in obesity-
RT induced insulin resistance.";
RL Nat. Med. 13:1193-1202(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the first and rate-limiting reaction of the four
CC reactions that constitute the long-chain fatty acids elongation cycle.
CC This endoplasmic reticulum-bound enzymatic process allows the addition
CC of 2 carbons to the chain of long- and very long-chain fatty acids
CC (VLCFAs) per cycle. Condensing enzyme that elongates fatty acids with
CC 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs.
CC Catalyzes the synthesis of unsaturated C16 long chain fatty acids and,
CC to a lesser extent, C18:0 and those with low desaturation degree. May
CC participate in the production of saturated and monounsaturated VLCFAs
CC of different chain lengths that are involved in multiple biological
CC processes as precursors of membrane lipids and lipid mediators.
CC {ECO:0000255|HAMAP-Rule:MF_03206, ECO:0000269|PubMed:11567032,
CC ECO:0000269|PubMed:12032166, ECO:0000269|PubMed:17906635}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC EC=2.3.1.199; Evidence={ECO:0000255|HAMAP-Rule:MF_03206,
CC ECO:0000269|PubMed:11567032, ECO:0000269|PubMed:17906635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000269|PubMed:17906635};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + malonyl-CoA = 3-oxooctadecanoyl-CoA
CC + CO2 + CoA; Xref=Rhea:RHEA:35315, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:71407;
CC Evidence={ECO:0000269|PubMed:11567032, ECO:0000269|PubMed:17906635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316;
CC Evidence={ECO:0000269|PubMed:17906635};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(11Z)-
CC octadecenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39675,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:61540, ChEBI:CHEBI:76555;
CC Evidence={ECO:0000269|PubMed:17906635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676;
CC Evidence={ECO:0000269|PubMed:17906635};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H(+) + malonyl-CoA = 3-oxotetradecanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:60140, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:62543;
CC Evidence={ECO:0000269|PubMed:11567032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60141;
CC Evidence={ECO:0000305|PubMed:11567032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA
CC + CO2 + CoA; Xref=Rhea:RHEA:39167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57349,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39168;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = (11Z)-3-
CC oxoicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36511,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57387, ChEBI:CHEBI:74011;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z)-
CC 3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36503,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:57384, ChEBI:CHEBI:74012;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA =
CC (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36523, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:74034,
CC ChEBI:CHEBI:74054; Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC -!- ACTIVITY REGULATION: The reaction is stimulated by the presence of
CC HSD17B12, the enzyme catalyzing the second step of the elongation
CC cycle. {ECO:0000250|UniProtKB:Q9H5J4}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5 at 37 degrees Celsius with hexadecanoyl-CoA as
CC substrate. {ECO:0000269|PubMed:11567032};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_03206, ECO:0000269|PubMed:17906635}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03206, ECO:0000269|PubMed:11567032,
CC ECO:0000269|PubMed:12084938}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03206}.
CC -!- TISSUE SPECIFICITY: Highly expressed in adrenal gland, liver, white
CC adipose tissue (WAT), adult and fetal brain, cerebellum, spinal cord,
CC testis, skin and peripheral nerve; where lipogenesis and
CC steroidogenesis are active. Weakly expressed in kidney, heart, skeletal
CC muscle, lung, and spleen. {ECO:0000269|PubMed:11567032,
CC ECO:0000269|PubMed:12032166, ECO:0000269|PubMed:12084938}.
CC -!- INDUCTION: By SREBF1. {ECO:0000269|PubMed:11567032,
CC ECO:0000269|PubMed:12032166}.
CC -!- PTM: N-Glycosylated. {ECO:0000255|HAMAP-Rule:MF_03206}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice lacking Elovl6 are
CC partially viable and surviving animals are fertile. Mutant mice appear
CC grossly normal and slightly but significantly leaner than wild-type
CC littermates. Hepatic concentrations of stearate (C18:0) and oleate
CC (C18:1n-9) are lowered, whereas those of palmitate (C16:0) and
CC palmitoleate (C16:1n7) are increased. Elovl6 deletion abrogates the
CC development of diet-induced insulin resistance.
CC {ECO:0000269|PubMed:17906635}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03206}.
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DR EMBL; AY053453; AAL14239.1; -; mRNA.
DR EMBL; AB072039; BAB68544.1; -; mRNA.
DR EMBL; AF480860; AAM13450.1; -; mRNA.
DR EMBL; AK029029; BAC26252.1; -; mRNA.
DR EMBL; AK167373; BAE39469.1; -; mRNA.
DR EMBL; BC051041; AAH51041.1; -; mRNA.
DR EMBL; BC098492; AAH98492.1; -; mRNA.
DR EMBL; BC100576; AAI00577.1; -; mRNA.
DR CCDS; CCDS38632.1; -.
DR RefSeq; NP_569717.1; NM_130450.2.
DR AlphaFoldDB; Q920L5; -.
DR SMR; Q920L5; -.
DR STRING; 10090.ENSMUSP00000071351; -.
DR BindingDB; Q920L5; -.
DR ChEMBL; CHEMBL5726; -.
DR SwissLipids; SLP:000000454; -.
DR GlyGen; Q920L5; 1 site.
DR PhosphoSitePlus; Q920L5; -.
DR EPD; Q920L5; -.
DR MaxQB; Q920L5; -.
DR PaxDb; Q920L5; -.
DR PeptideAtlas; Q920L5; -.
DR PRIDE; Q920L5; -.
DR ProteomicsDB; 277823; -.
DR Antibodypedia; 26395; 203 antibodies from 33 providers.
DR DNASU; 170439; -.
DR Ensembl; ENSMUST00000071402; ENSMUSP00000071351; ENSMUSG00000041220.
DR Ensembl; ENSMUST00000199910; ENSMUSP00000142832; ENSMUSG00000041220.
DR GeneID; 170439; -.
DR KEGG; mmu:170439; -.
DR UCSC; uc008rid.1; mouse.
DR CTD; 79071; -.
DR MGI; MGI:2156528; Elovl6.
DR VEuPathDB; HostDB:ENSMUSG00000041220; -.
DR eggNOG; KOG3072; Eukaryota.
DR GeneTree; ENSGT01050000244965; -.
DR InParanoid; Q920L5; -.
DR OMA; PISWVPI; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q920L5; -.
DR TreeFam; TF106467; -.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 170439; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Elovl6; mouse.
DR PRO; PR:Q920L5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q920L5; protein.
DR Bgee; ENSMUSG00000041220; Expressed in skin of external ear and 258 other tissues.
DR ExpressionAtlas; Q920L5; baseline and differential.
DR Genevisible; Q920L5; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0009923; C:fatty acid elongase complex; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:MGI.
DR GO; GO:0009922; F:fatty acid elongase activity; ISO:MGI.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030497; P:fatty acid elongation; IDA:MGI.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IBA:GO_Central.
DR GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IBA:GO_Central.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; ISS:UniProtKB.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_03206; VLCF_elongase_6; 1.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033675; ELOVL6.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR PANTHER; PTHR11157:SF125; PTHR11157:SF125; 1.
DR Pfam; PF01151; ELO; 1.
DR PROSITE; PS01188; ELO; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Glycoprotein; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..267
FT /note="Elongation of very long chain fatty acids protein 6"
FT /id="PRO_0000282846"
FT TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT CONFLICT 144
FT /note="H -> Q (in Ref. 4; BAC26252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 31610 MW; 4026C9CB33FDDD23 CRC64;
MNMSVLTLQE YEFEKQFNEN EAIQWMQENW KKSFLFSALY AAFIFGGRHL MNKRAKFELR
KPLVLWSLTL AVFSIFGALR TGAYMLYILM TKGLKQSVCD QSFYNGPVSK FWAYAFVLSK
APELGDTIFI ILRKQKLIFL HWYHHITVLL YSWYSYKDMV AGGGWFMTMN YGVHAVMYSY
YALRAAGFRV SRKFAMFITL SQITQMLMGC VINYLVFNWM QHDNDQCYSH FQNIFWSSLM
YLSYLVLFCH FFFEAYIGKV KKATKAE
