PAQR1_HUMAN
ID PAQR1_HUMAN Reviewed; 375 AA.
AC Q96A54; B3KMB0; Q53HS7; Q53YY6; Q9Y360;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Adiponectin receptor protein 1 {ECO:0000303|PubMed:12802337};
DE AltName: Full=Progestin and adipoQ receptor family member 1 {ECO:0000303|PubMed:16044242};
DE AltName: Full=Progestin and adipoQ receptor family member I;
GN Name=ADIPOR1 {ECO:0000312|HGNC:HGNC:24040};
GN Synonyms=PAQR1 {ECO:0000303|PubMed:16044242}, TESBP1A; ORFNames=CGI-45;
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], AND TISSUE SPECIFICITY.
RX PubMed=16044242; DOI=10.1007/s00239-004-0375-2;
RA Tang Y.T., Hu T., Arterburn M., Boyle B., Bright J.M., Emtage P.C.,
RA Funk W.D.;
RT "PAQR proteins: a novel membrane receptor family defined by an ancient 7-
RT transmembrane pass motif.";
RL J. Mol. Evol. 61:372-380(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sugihara T.;
RT "Cloning and characterization of TESBP1A.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
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 FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND TOPOLOGY.
RX PubMed=12802337; DOI=10.1038/nature01705;
RA Yamauchi T., Kamon J., Ito Y., Tsuchida A., Yokomizo T., Kita S.,
RA Sugiyama T., Miyagishi M., Hara K., Tsunoda M., Murakami K., Ohteki T.,
RA Uchida S., Takekawa S., Waki H., Tsuno N.H., Shibata Y., Terauchi Y.,
RA Froguel P., Tobe K., Koyasu S., Taira K., Kitamura T., Shimizu T.,
RA Nagai R., Kadowaki T.;
RT "Cloning of adiponectin receptors that mediate antidiabetic metabolic
RT effects.";
RL Nature 423:762-769(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 89-375 IN COMPLEX WITH ZINC,
RP FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 161-MET--LEU-167; HIS-191; ASP-208; 229-TYR--SER-231; 291-PHE--VAL-297;
RP HIS-337 AND HIS-341.
RX PubMed=25855295; DOI=10.1038/nature14301;
RA Tanabe H., Fujii Y., Okada-Iwabu M., Iwabu M., Nakamura Y., Hosaka T.,
RA Motoyama K., Ikeda M., Wakiyama M., Terada T., Ohsawa N., Hato M.,
RA Ogasawara S., Hino T., Murata T., Iwata S., Hirata K., Kawano Y.,
RA Yamamoto M., Kimura-Someya T., Shirouzu M., Yamauchi T., Kadowaki T.,
RA Yokoyama S.;
RT "Crystal structures of the human adiponectin receptors.";
RL Nature 520:312-316(2015).
CC -!- FUNCTION: Receptor for ADIPOQ, an essential hormone secreted by
CC adipocytes that regulates glucose and lipid metabolism
CC (PubMed:25855295, PubMed:12802337). Required for normal glucose and fat
CC homeostasis and for maintaining a normal body weight. ADIPOQ-binding
CC activates a signaling cascade that leads to increased AMPK activity,
CC and ultimately to increased fatty acid oxidation, increased glucose
CC uptake and decreased gluconeogenesis. Has high affinity for globular
CC adiponectin and low affinity for full-length adiponectin (By
CC similarity). {ECO:0000250|UniProtKB:Q91VH1,
CC ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:25855295}.
CC -!- SUBUNIT: May form homooligomers and heterooligomers with ADIPOR2
CC (PubMed:12802337). Interacts with APPL2 (via BAR domain); hinders the
CC accessibility of APPL1 to ADIPOR1; negatively regulates adiponectin
CC signaling; ADIPOQ dissociates this interaction and facilitates the
CC recruitment of APPL1 to ADIPOR1. Interacts with APPL1; ADIPOQ enhances
CC this interaction; inhibites adiponectin-stimulated binding of APPL2 to
CC ADIPOR1 (By similarity). {ECO:0000250|UniProtKB:Q91VH1,
CC ECO:0000269|PubMed:12802337}.
CC -!- INTERACTION:
CC Q96A54; Q96A54: ADIPOR1; NbExp=3; IntAct=EBI-1632076, EBI-1632076;
CC Q96A54; Q9UKG1: APPL1; NbExp=6; IntAct=EBI-1632076, EBI-741243;
CC Q96A54; Q0VAB0: TBXA2R; NbExp=3; IntAct=EBI-1632076, EBI-18271435;
CC Q96A54; O00206: TLR4; NbExp=2; IntAct=EBI-1632076, EBI-528701;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12802337,
CC ECO:0000269|PubMed:25855295}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:25855295}.
CC Note=Localized to the cell membrane and intracellular organelles.
CC {ECO:0000269|PubMed:12802337}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:16044242). Highly
CC expressed in heart and skeletal muscle (PubMed:12802337). Expressed at
CC intermediate level in brain, spleen, kidney, liver, placenta, lung and
CC peripheral blood leukocytes (PubMed:12802337). Weakly expressed in
CC colon, thymus and small intestine (PubMed:12802337).
CC {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:16044242}.
CC -!- DOMAIN: The N-terminus is cytoplasmic and the C-terminus is
CC extracellular, contrary to what is observed for G-protein coupled
CC receptors. Unlike G-protein coupled receptors, transmembrane helices
CC are not kinked or tilted relative to the plane of the membrane.
CC {ECO:0000269|PubMed:12802337}.
CC -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34040.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ADIPOR1ID44512ch1q32.html";
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; AY424279; AAR08367.1; -; mRNA.
DR EMBL; AF125179; AAQ13552.1; -; mRNA.
DR EMBL; AF151803; AAD34040.1; ALT_FRAME; mRNA.
DR EMBL; AK001484; BAG50922.1; -; mRNA.
DR EMBL; AK222503; BAD96223.1; -; mRNA.
DR EMBL; CH471067; EAW91450.1; -; Genomic_DNA.
DR EMBL; BC001594; AAH01594.1; -; mRNA.
DR EMBL; BC010743; AAH10743.1; -; mRNA.
DR CCDS; CCDS1430.1; -.
DR RefSeq; NP_001277482.1; NM_001290553.1.
DR RefSeq; NP_001277486.1; NM_001290557.1.
DR RefSeq; NP_001277558.1; NM_001290629.1.
DR RefSeq; NP_057083.2; NM_015999.5.
DR PDB; 5LXG; X-ray; 2.73 A; A=89-375.
DR PDB; 6KRZ; X-ray; 3.05 A; A/B/C=89-375.
DR PDB; 6KS0; X-ray; 2.79 A; A=89-375.
DR PDBsum; 5LXG; -.
DR PDBsum; 6KRZ; -.
DR PDBsum; 6KS0; -.
DR AlphaFoldDB; Q96A54; -.
DR SMR; Q96A54; -.
DR BioGRID; 119283; 53.
DR DIP; DIP-48622N; -.
DR IntAct; Q96A54; 28.
DR MINT; Q96A54; -.
DR STRING; 9606.ENSP00000341785; -.
DR BindingDB; Q96A54; -.
DR ChEMBL; CHEMBL3392946; -.
DR TCDB; 1.C.113.1.9; the hemolysin iii (hly iii) family.
DR iPTMnet; Q96A54; -.
DR PhosphoSitePlus; Q96A54; -.
DR BioMuta; ADIPOR1; -.
DR DMDM; 38372248; -.
DR EPD; Q96A54; -.
DR jPOST; Q96A54; -.
DR MassIVE; Q96A54; -.
DR MaxQB; Q96A54; -.
DR PaxDb; Q96A54; -.
DR PeptideAtlas; Q96A54; -.
DR PRIDE; Q96A54; -.
DR ProteomicsDB; 75913; -.
DR ABCD; Q96A54; 1 sequenced antibody.
DR Antibodypedia; 34534; 420 antibodies from 37 providers.
DR DNASU; 51094; -.
DR Ensembl; ENST00000340990.10; ENSP00000341785.5; ENSG00000159346.13.
DR GeneID; 51094; -.
DR KEGG; hsa:51094; -.
DR MANE-Select; ENST00000340990.10; ENSP00000341785.5; NM_015999.6; NP_057083.2.
DR UCSC; uc001gyq.7; human.
DR CTD; 51094; -.
DR DisGeNET; 51094; -.
DR GeneCards; ADIPOR1; -.
DR HGNC; HGNC:24040; ADIPOR1.
DR HPA; ENSG00000159346; Low tissue specificity.
DR MIM; 607945; gene.
DR neXtProt; NX_Q96A54; -.
DR OpenTargets; ENSG00000159346; -.
DR PharmGKB; PA134861801; -.
DR VEuPathDB; HostDB:ENSG00000159346; -.
DR eggNOG; KOG0748; Eukaryota.
DR GeneTree; ENSGT00940000154563; -.
DR HOGENOM; CLU_023075_1_0_1; -.
DR InParanoid; Q96A54; -.
DR OMA; DYCGIAM; -.
DR OrthoDB; 1524940at2759; -.
DR PhylomeDB; Q96A54; -.
DR TreeFam; TF313640; -.
DR PathwayCommons; Q96A54; -.
DR Reactome; R-HSA-163680; AMPK inhibits chREBP transcriptional activation activity.
DR SignaLink; Q96A54; -.
DR SIGNOR; Q96A54; -.
DR BioGRID-ORCS; 51094; 19 hits in 1079 CRISPR screens.
DR ChiTaRS; ADIPOR1; human.
DR GeneWiki; ADIPOR1; -.
DR GenomeRNAi; 51094; -.
DR Pharos; Q96A54; Tbio.
DR PRO; PR:Q96A54; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96A54; protein.
DR Bgee; ENSG00000159346; Expressed in blood and 204 other tissues.
DR ExpressionAtlas; Q96A54; baseline and differential.
DR Genevisible; Q96A54; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0097003; F:adipokinetic hormone receptor activity; IDA:UniProtKB.
DR GO; GO:0055100; F:adiponectin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0033211; P:adiponectin-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:0019395; P:fatty acid oxidation; IDA:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0033210; P:leptin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:BHF-UCL.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:BHF-UCL.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IMP:BHF-UCL.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:0010906; P:regulation of glucose metabolic process; ISS:UniProtKB.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR InterPro; IPR004254; AdipoR/HlyIII-related.
DR PANTHER; PTHR20855; PTHR20855; 1.
DR Pfam; PF03006; HlyIII; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Fatty acid metabolism; Lipid metabolism;
KW Membrane; Metal-binding; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..375
FT /note="Adiponectin receptor protein 1"
FT /id="PRO_0000218827"
FT TOPO_DOM 1..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 137..157
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 158..170
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 171..191
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 192..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 204..224
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 225..234
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 235..255
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 256..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 265..285
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 286..298
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 299..319
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 320..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 338..358
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 359..375
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25855295"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25855295"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25855295"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25855295"
FT MUTAGEN 161..167
FT /note="MYFMAPL->SGSSGGS: Decreases activation of AMPK in
FT response to ADIPOQ binding; when associated with 229-G--G-
FT 231 and 291-S--S-297."
FT /evidence="ECO:0000269|PubMed:25855295"
FT MUTAGEN 191
FT /note="H->A: Decreases activation of AMPK in response to
FT ADIPOQ binding; when associated with A-208; A-337 and A-
FT 341."
FT /evidence="ECO:0000269|PubMed:25855295"
FT MUTAGEN 208
FT /note="D->A: Decreases activation of AMPK in response to
FT ADIPOQ binding; when associated with A-191; A-337 and A-
FT 341."
FT /evidence="ECO:0000269|PubMed:25855295"
FT MUTAGEN 229..231
FT /note="YCS->GGG: Decreases activation of AMPK in response
FT to ADIPOQ binding; when associated with 161-S--S-167 and
FT 291-S--S-297."
FT /evidence="ECO:0000269|PubMed:25855295"
FT MUTAGEN 291..297
FT /note="FVKATTV->SSSGGGS: Decreases activation of AMPK in
FT response to ADIPOQ binding; when associated with 161-S--S-
FT 167 and 229-G--G-231."
FT /evidence="ECO:0000269|PubMed:25855295"
FT MUTAGEN 337
FT /note="H->A: Decreases activation of AMPK in response to
FT ADIPOQ binding; when associated with A-191; A-208 and A-
FT 341."
FT /evidence="ECO:0000269|PubMed:25855295"
FT MUTAGEN 341
FT /note="H->A: Decreases activation of AMPK in response to
FT ADIPOQ binding; when associated with A-191; A-208 and A-
FT 337."
FT /evidence="ECO:0000269|PubMed:25855295"
FT CONFLICT 183
FT /note="C -> W (in Ref. 4; BAG50922)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="F -> Y (in Ref. 5; BAD96223)"
FT /evidence="ECO:0000305"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:5LXG"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:5LXG"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:5LXG"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5LXG"
FT HELIX 135..156
FT /evidence="ECO:0007829|PDB:5LXG"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:5LXG"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:5LXG"
FT HELIX 169..192
FT /evidence="ECO:0007829|PDB:5LXG"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6KS0"
FT HELIX 198..227
FT /evidence="ECO:0007829|PDB:5LXG"
FT HELIX 232..254
FT /evidence="ECO:0007829|PDB:5LXG"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:5LXG"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6KS0"
FT HELIX 266..277
FT /evidence="ECO:0007829|PDB:5LXG"
FT HELIX 279..289
FT /evidence="ECO:0007829|PDB:5LXG"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:5LXG"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:6KRZ"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:5LXG"
FT HELIX 304..319
FT /evidence="ECO:0007829|PDB:5LXG"
FT TURN 320..325
FT /evidence="ECO:0007829|PDB:5LXG"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:5LXG"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:5LXG"
FT HELIX 336..364
FT /evidence="ECO:0007829|PDB:5LXG"
SQ SEQUENCE 375 AA; 42616 MW; 1CC0300A7D178EB0 CRC64;
MSSHKGSVVA QGNGAPASNR EADTVELAEL GPLLEEKGKR VIANPPKAEE EQTCPVPQEE
EEEVRVLTLP LQAHHAMEKM EEFVYKVWEG RWRVIPYDVL PDWLKDNDYL LHGHRPPMPS
FRACFKSIFR IHTETGNIWT HLLGFVLFLF LGILTMLRPN MYFMAPLQEK VVFGMFFLGA
VLCLSFSWLF HTVYCHSEKV SRTFSKLDYS GIALLIMGSF VPWLYYSFYC SPQPRLIYLS
IVCVLGISAI IVAQWDRFAT PKHRQTRAGV FLGLGLSGVV PTMHFTIAEG FVKATTVGQM
GWFFLMAVMY ITGAGLYAAR IPERFFPGKF DIWFQSHQIF HVLVVAAAFV HFYGVSNLQE
FRYGLEGGCT DDTLL
