ORML3_HUMAN
ID ORML3_HUMAN Reviewed; 153 AA.
AC Q8N138; B3KS83; Q6UY83;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=ORM1-like protein 3;
GN Name=ORMDL3;
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), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12093374; DOI=10.1186/gb-2002-3-6-research0027;
RA Hjelmqvist L., Tuson M., Marfany G., Herrero E., Balcells S.,
RA Gonzalez-Duarte R.;
RT "ORMDL proteins are a conserved new family of endoplasmic reticulum
RT membrane proteins.";
RL Genome Biol. 3:RESEARCH0027.1-RESEARCH0027.13(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Luoh S.-W., Venkatesan N., Slamon D.J.;
RT "An evolutionarily conserved gene from the HER-2/Neu amplicon defines a
RT novel gene family.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Li H., Yu R., Shen C., Zhou G., Ke R., Lin L., Yang S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Colon;
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 [7]
RP ASSOCIATION OF ORMDL3 EXPRESSION LEVELS WITH SUSCEPTIBILITY TO ASTHMA.
RX PubMed=17611496; DOI=10.1038/nature06014;
RA Moffatt M.F., Kabesch M., Liang L., Dixon A.L., Strachan D., Heath S.,
RA Depner M., von Berg A., Bufe A., Rietschel E., Heinzmann A., Simma B.,
RA Frischer T., Willis-Owen S.A., Wong K.C., Illig T., Vogelberg C.,
RA Weiland S.K., von Mutius E., Abecasis G.R., Farrall M., Gut I.G.,
RA Lathrop G.M., Cookson W.O.;
RT "Genetic variants regulating ORMDL3 expression contribute to the risk of
RT childhood asthma.";
RL Nature 448:470-473(2007).
RN [8]
RP INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA.
RX PubMed=18395550; DOI=10.1016/j.jaci.2008.01.015;
RA Tavendale R., Macgregor D.F., Mukhopadhyay S., Palmer C.N.;
RT "A polymorphism controlling ORMDL3 expression is associated with asthma
RT that is poorly controlled by current medications.";
RL J. Allergy Clin. Immunol. 121:860-863(2008).
RN [9]
RP INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA.
RX PubMed=18760456; DOI=10.1016/j.jaci.2008.06.041;
RA Sleiman P.M., Annaiah K., Imielinski M., Bradfield J.P., Kim C.E.,
RA Frackelton E.C., Glessner J.T., Eckert A.W., Otieno F.G., Santa E.,
RA Thomas K., Smith R.M., Glaberson W., Garris M., Gunnlaugsson S.,
RA Chiavacci R.M., Allen J., Spergel J., Grundmeier R., Grunstein M.M.,
RA Magnusson M., Bisgaard H., Grant S.F., Hakonarson H.;
RT "ORMDL3 variants associated with asthma susceptibility in North Americans
RT of European ancestry.";
RL J. Allergy Clin. Immunol. 122:1225-1227(2008).
RN [10]
RP INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA.
RX PubMed=19133921; DOI=10.1111/j.1398-9995.2008.01912.x;
RA Wu H., Romieu I., Sienra-Monge J.J., Li H., del Rio-Navarro B.E.,
RA London S.J.;
RT "Genetic variation in ORM1-like 3 (ORMDL3) and gasdermin-like (GSDML) and
RT childhood asthma.";
RL Allergy 64:629-635(2009).
RN [11]
RP POSSIBLE FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=19819884; DOI=10.1093/hmg/ddp471;
RA Cantero-Recasens G., Fandos C., Rubio-Moscardo F., Valverde M.A.,
RA Vicente R.;
RT "The asthma-associated ORMDL3 gene product regulates endoplasmic reticulum-
RT mediated calcium signaling and cellular stress.";
RL Hum. Mol. Genet. 19:111-121(2010).
RN [12]
RP FUNCTION, AND INTERACTION WITH SPTLC1.
RX PubMed=20182505; DOI=10.1038/nature08787;
RA Breslow D.K., Collins S.R., Bodenmiller B., Aebersold R., Simons K.,
RA Shevchenko A., Ejsing C.S., Weissman J.S.;
RT "Orm family proteins mediate sphingolipid homeostasis.";
RL Nature 463:1048-1053(2010).
CC -!- FUNCTION: Negative regulator of sphingolipid synthesis. May indirectly
CC regulate endoplasmic reticulum-mediated Ca(+2) signaling.
CC {ECO:0000269|PubMed:20182505}.
CC -!- SUBUNIT: Interacts with SPTLC1. {ECO:0000269|PubMed:20182505}.
CC -!- INTERACTION:
CC Q8N138; Q13520: AQP6; NbExp=3; IntAct=EBI-721750, EBI-13059134;
CC Q8N138; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-721750, EBI-11343438;
CC Q8N138; Q8IYJ2-2: C10orf67; NbExp=3; IntAct=EBI-721750, EBI-13381098;
CC Q8N138; Q8IU89: CERS3; NbExp=3; IntAct=EBI-721750, EBI-18202821;
CC Q8N138; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-721750, EBI-745535;
CC Q8N138; Q15125: EBP; NbExp=3; IntAct=EBI-721750, EBI-3915253;
CC Q8N138; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-721750, EBI-18535450;
CC Q8N138; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-721750, EBI-781551;
CC Q8N138; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-721750, EBI-18304435;
CC Q8N138; O00258: GET1; NbExp=3; IntAct=EBI-721750, EBI-18908258;
CC Q8N138; Q96P66: GPR101; NbExp=3; IntAct=EBI-721750, EBI-17935713;
CC Q8N138; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-721750, EBI-13345167;
CC Q8N138; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-721750, EBI-18053395;
CC Q8N138; O95279: KCNK5; NbExp=3; IntAct=EBI-721750, EBI-3934936;
CC Q8N138; O95214: LEPROTL1; NbExp=3; IntAct=EBI-721750, EBI-750776;
CC Q8N138; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-721750, EBI-3923617;
CC Q8N138; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-721750, EBI-11337973;
CC Q8N138; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-721750, EBI-10192441;
CC Q8N138; Q99942: RNF5; NbExp=3; IntAct=EBI-721750, EBI-348482;
CC Q8N138; Q03395: ROM1; NbExp=3; IntAct=EBI-721750, EBI-9395257;
CC Q8N138; Q14973: SLC10A1; NbExp=3; IntAct=EBI-721750, EBI-3923031;
CC Q8N138; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-721750, EBI-17295964;
CC Q8N138; P30825: SLC7A1; NbExp=3; IntAct=EBI-721750, EBI-4289564;
CC Q8N138; O15269: SPTLC1; NbExp=3; IntAct=EBI-721750, EBI-1044323;
CC Q8N138; Q8N9I0: SYT2; NbExp=3; IntAct=EBI-721750, EBI-8032987;
CC Q8N138; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-721750, EBI-10982110;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12093374, ECO:0000269|PubMed:19819884}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12093374,
CC ECO:0000269|PubMed:19819884}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N138-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N138-4; Sequence=VSP_016052;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in adult and fetal
CC heart, brain, lung, liver, skeletal muscle and kidney. Expressed in
CC adult pancreas and placenta and in fetal spleen abd thymus.
CC {ECO:0000269|PubMed:12093374}.
CC -!- DISEASE: Asthma (ASTHMA) [MIM:600807]: The most common chronic disease
CC affecting children and young adults. It is a complex genetic disorder
CC with a heterogeneous phenotype, largely attributed to the interactions
CC among many genes and between these genes and the environment. It is
CC characterized by recurrent attacks of paroxysmal dyspnea, with wheezing
CC due to spasmodic contraction of the bronchi.
CC {ECO:0000269|PubMed:18395550, ECO:0000269|PubMed:18760456,
CC ECO:0000269|PubMed:19133921}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: SNPs on 17q21 locus that are associated with childhood
CC asthma also show a consistent and strong association with transcript
CC levels of ORMDL3, indicating that genetic variants regulating ORMDL3
CC expression are determinants of susceptibility to childhood asthma.
CC -!- SIMILARITY: Belongs to the ORM family. {ECO:0000305}.
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DR EMBL; AF395708; AAM43507.1; -; mRNA.
DR EMBL; AF373101; AAN76521.1; -; mRNA.
DR EMBL; AF373102; AAN76522.1; -; mRNA.
DR EMBL; AK074811; BAC11223.1; -; mRNA.
DR EMBL; AY357943; AAQ57273.1; -; mRNA.
DR EMBL; AK075212; BAC11476.1; -; mRNA.
DR EMBL; AK093063; BAG52645.1; -; mRNA.
DR EMBL; CH471152; EAW60617.1; -; Genomic_DNA.
DR EMBL; BC017087; AAH17087.1; -; mRNA.
DR EMBL; BC071833; AAH71833.1; -; mRNA.
DR CCDS; CCDS11355.1; -. [Q8N138-1]
DR RefSeq; NP_001307730.1; NM_001320801.1. [Q8N138-1]
DR RefSeq; NP_001307731.1; NM_001320802.1. [Q8N138-1]
DR RefSeq; NP_001307732.1; NM_001320803.1. [Q8N138-1]
DR RefSeq; NP_644809.1; NM_139280.3. [Q8N138-1]
DR RefSeq; XP_016880835.1; XM_017025346.1.
DR RefSeq; XP_016880836.1; XM_017025347.1.
DR RefSeq; XP_016880837.1; XM_017025348.1.
DR PDB; 6M4N; EM; 3.80 A; C/G=1-153.
DR PDB; 6M4O; EM; 3.40 A; A=1-153.
DR PDB; 7CQI; EM; 3.20 A; A=1-153.
DR PDB; 7CQK; EM; 3.30 A; A=1-153.
DR PDB; 7K0M; EM; 2.90 A; D/H=1-153.
DR PDB; 7K0N; EM; 3.10 A; D/H=1-153.
DR PDB; 7K0O; EM; 3.10 A; D/H=1-153.
DR PDB; 7K0P; EM; 3.10 A; D/H=1-153.
DR PDB; 7K0Q; EM; 3.30 A; D=1-153.
DR PDBsum; 6M4N; -.
DR PDBsum; 6M4O; -.
DR PDBsum; 7CQI; -.
DR PDBsum; 7CQK; -.
DR PDBsum; 7K0M; -.
DR PDBsum; 7K0N; -.
DR PDBsum; 7K0O; -.
DR PDBsum; 7K0P; -.
DR PDBsum; 7K0Q; -.
DR AlphaFoldDB; Q8N138; -.
DR SMR; Q8N138; -.
DR BioGRID; 125114; 60.
DR CORUM; Q8N138; -.
DR DIP; DIP-48687N; -.
DR IntAct; Q8N138; 35.
DR STRING; 9606.ENSP00000377724; -.
DR iPTMnet; Q8N138; -.
DR PhosphoSitePlus; Q8N138; -.
DR BioMuta; ORMDL3; -.
DR DMDM; 74728486; -.
DR EPD; Q8N138; -.
DR jPOST; Q8N138; -.
DR MassIVE; Q8N138; -.
DR MaxQB; Q8N138; -.
DR PaxDb; Q8N138; -.
DR PeptideAtlas; Q8N138; -.
DR PRIDE; Q8N138; -.
DR ProteomicsDB; 71543; -. [Q8N138-1]
DR ProteomicsDB; 71544; -. [Q8N138-4]
DR TopDownProteomics; Q8N138-1; -. [Q8N138-1]
DR Antibodypedia; 54876; 117 antibodies from 22 providers.
DR DNASU; 94103; -.
DR Ensembl; ENST00000304046.7; ENSP00000304858.2; ENSG00000172057.10. [Q8N138-1]
DR Ensembl; ENST00000394169.5; ENSP00000377724.1; ENSG00000172057.10. [Q8N138-1]
DR Ensembl; ENST00000579695.5; ENSP00000464693.1; ENSG00000172057.10. [Q8N138-1]
DR Ensembl; ENST00000584220.5; ENSP00000464455.1; ENSG00000172057.10. [Q8N138-4]
DR GeneID; 94103; -.
DR KEGG; hsa:94103; -.
DR MANE-Select; ENST00000304046.7; ENSP00000304858.2; NM_139280.4; NP_644809.1.
DR UCSC; uc002htj.3; human. [Q8N138-1]
DR CTD; 94103; -.
DR DisGeNET; 94103; -.
DR GeneCards; ORMDL3; -.
DR HGNC; HGNC:16038; ORMDL3.
DR HPA; ENSG00000172057; Tissue enhanced (liver).
DR MIM; 600807; phenotype.
DR MIM; 610075; gene.
DR neXtProt; NX_Q8N138; -.
DR OpenTargets; ENSG00000172057; -.
DR PharmGKB; PA32821; -.
DR VEuPathDB; HostDB:ENSG00000172057; -.
DR eggNOG; KOG3319; Eukaryota.
DR GeneTree; ENSGT00950000183178; -.
DR HOGENOM; CLU_072117_3_0_1; -.
DR InParanoid; Q8N138; -.
DR OMA; RYSTHWE; -.
DR PhylomeDB; Q8N138; -.
DR TreeFam; TF323369; -.
DR PathwayCommons; Q8N138; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q8N138; -.
DR BioGRID-ORCS; 94103; 16 hits in 1080 CRISPR screens.
DR ChiTaRS; ORMDL3; human.
DR GenomeRNAi; 94103; -.
DR Pharos; Q8N138; Tbio.
DR PRO; PR:Q8N138; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8N138; protein.
DR Bgee; ENSG00000172057; Expressed in right lobe of liver and 177 other tissues.
DR ExpressionAtlas; Q8N138; baseline and differential.
DR Genevisible; Q8N138; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0035339; C:SPOTS complex; IDA:UniProtKB.
DR GO; GO:0090156; P:cellular sphingolipid homeostasis; IBA:GO_Central.
DR GO; GO:0006672; P:ceramide metabolic process; IMP:UniProtKB.
DR GO; GO:0061744; P:motor behavior; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; IMP:MGI.
DR GO; GO:1900060; P:negative regulation of ceramide biosynthetic process; IMP:MGI.
DR GO; GO:1904221; P:negative regulation of serine C-palmitoyltransferase activity; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:MGI.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:MGI.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; IEA:Ensembl.
DR InterPro; IPR007203; ORMDL.
DR InterPro; IPR029883; ORML3.
DR PANTHER; PTHR12665; PTHR12665; 1.
DR PANTHER; PTHR12665:SF11; PTHR12665:SF11; 1.
DR Pfam; PF04061; ORMDL; 1.
DR PIRSF; PIRSF018147; ORMDL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Asthma; Endoplasmic reticulum;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..153
FT /note="ORM1-like protein 3"
FT /id="PRO_0000215639"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..94
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 43..58
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_016052"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:7K0M"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:7K0M"
FT HELIX 22..38
FT /evidence="ECO:0007829|PDB:7K0M"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:7K0Q"
FT HELIX 45..65
FT /evidence="ECO:0007829|PDB:7K0M"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:7K0Q"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:7CQI"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:7K0P"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:7K0N"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:7K0M"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:7K0M"
FT HELIX 97..116
FT /evidence="ECO:0007829|PDB:7K0M"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:7K0M"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:7K0M"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:7K0M"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:7K0M"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:7K0M"
SQ SEQUENCE 153 AA; 17495 MW; 3EF483CA5C03EC2E CRC64;
MNVGTAHSEV NPNTRVMNSR GIWLSYVLAI GLLHIVLLSI PFVSVPVVWT LTNLIHNMGM
YIFLHTVKGT PFETPDQGKA RLLTHWEQMD YGVQFTASRK FLTITPIVLY FLTSFYTKYD
QIHFVLNTVS LMSVLIPKLP QLHGVRIFGI NKY
