AOC3_HUMAN
ID AOC3_HUMAN Reviewed; 763 AA.
AC Q16853; B2RCI5; K7ESB3; L0L8N9; Q45F94;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Membrane primary amine oxidase;
DE EC=1.4.3.21 {ECO:0000269|PubMed:19588076};
DE AltName: Full=Copper amine oxidase;
DE AltName: Full=HPAO;
DE AltName: Full=Semicarbazide-sensitive amine oxidase;
DE Short=SSAO;
DE AltName: Full=Vascular adhesion protein 1;
DE Short=VAP-1;
GN Name=AOC3; Synonyms=VAP1;
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).
RC TISSUE=Placenta;
RX PubMed=8972912; DOI=10.1016/s0378-1119(96)00387-3;
RA Zhang X., McIntire W.S.;
RT "Cloning and sequencing of a copper-containing, topaquinone-containing
RT monoamine oxidase from human placenta.";
RL Gene 179:279-286(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP SELF-ASSOCIATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=9653080; DOI=10.1084/jem.188.1.17;
RA Smith D.J., Salmi M., Bono P., Hellman J., Leu T., Jalkanen S.;
RT "Cloning of vascular adhesion protein 1 reveals a novel multifunctional
RT adhesion molecule.";
RL J. Exp. Med. 188:17-27(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14585497; DOI=10.1016/s0378-1119(03)00753-4;
RA Zhang Q., Mashima Y., Noda S., Imamura Y., Kudoh J., Shimizu N.,
RA Nishiyama T., Umeda S., Oguchi Y., Tanaka Y., Iwata T.;
RT "Characterization of AOC2 gene encoding a copper-binding amine oxidase
RT expressed specifically in retina.";
RL Gene 318:45-53(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=23349812; DOI=10.1371/journal.pone.0054151;
RA Kaitaniemi S., Gron K., Elovaara H., Salmi M., Jalkanen S., Elima K.;
RT "Functional modulation of vascular adhesion protein-1 by a novel splice
RT variant.";
RL PLoS ONE 8:E54151-E54151(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-5; TYR-167; THR-371;
RP SER-408; HIS-426; TRP-441; THR-582; SER-700 AND VAL-749.
RG NIEHS SNPs program;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=PNS;
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 [9]
RP PROTEIN SEQUENCE OF 79-90 AND 123-132.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-592; ASN-618 AND ASN-666.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17400359; DOI=10.1016/j.biochi.2007.02.013;
RA Bour S., Daviaud D., Gres S., Lefort C., Prevot D., Zorzano A.,
RA Wabitsch M., Saulnier-Blache J.-S., Valet P., Carpene C.;
RT "Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and
RT monoamine oxidase in human adipocytes.";
RL Biochimie 89:916-925(2007).
RN [12]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF MET-211;
RP TYR-394 AND LEU-469, AND CATALYTIC ACTIVITY.
RX PubMed=19588076; DOI=10.1007/s00018-009-0076-5;
RA Kaitaniemi S., Elovaara H., Groen K., Kidron H., Liukkonen J., Salminen T.,
RA Salmi M., Jalkanen S., Elima K.;
RT "The unique substrate specificity of human AOC2, a semicarbazide-sensitive
RT amine oxidase.";
RL Cell. Mol. Life Sci. 66:2743-2757(2009).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-137; ASN-294; ASN-592; ASN-618
RP AND ASN-666.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [14]
RP GLYCOSYLATION AT ASN-592.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [15] {ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH CALCIUM; COPPER AND
RP SUBSTRATE, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, AND GLYCOSYLATION AT
RP ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618 AND ASN-666.
RX PubMed=16046623; DOI=10.1110/ps.051438105;
RA Airenne T.T., Nymalm Y., Kidron H., Smith D.J., Pihlavisto M., Salmi M.,
RA Jalkanen S., Johnson M.S., Salminen T.A.;
RT "Crystal structure of the human vascular adhesion protein-1: unique
RT structural features with functional implications.";
RL Protein Sci. 14:1964-1974(2005).
CC -!- FUNCTION: Cell adhesion protein that participates in lymphocyte
CC extravasation and recirculation by mediating the binding of lymphocytes
CC to peripheral lymph node vascular endothelial cells in an L-selectin-
CC independent fashion. Has semicarbazide-sensitive (SSAO) monoamine
CC oxidase activity. May play a role in adipogenesis.
CC {ECO:0000269|PubMed:17400359, ECO:0000269|PubMed:19588076,
CC ECO:0000269|PubMed:23349812, ECO:0000269|PubMed:9653080}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
CC Evidence={ECO:0000269|PubMed:19588076};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:16046623};
CC Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:16046623};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:16046623};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:16046623};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000269|PubMed:16046623};
CC Note=Contains 1 topaquinone per subunit. {ECO:0000269|PubMed:16046623};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.94 mM for 2-phenylethylamine {ECO:0000269|PubMed:19588076};
CC KM=0.67 mM for methylamine {ECO:0000269|PubMed:19588076};
CC -!- SUBUNIT: Homodimer; disulfide-linked. Can heterodimerize with isoform 2
CC leading to reduced surface expression. Forms a heterodimer with AOC2.
CC {ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:19588076,
CC ECO:0000269|PubMed:23349812}.
CC -!- INTERACTION:
CC Q16853; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-3921628, EBI-11343438;
CC Q16853; O95484: CLDN9; NbExp=3; IntAct=EBI-3921628, EBI-18341636;
CC Q16853; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-3921628, EBI-18013275;
CC Q16853; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-3921628, EBI-6942903;
CC Q16853; Q6PI48: DARS2; NbExp=3; IntAct=EBI-3921628, EBI-3917045;
CC Q16853; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-3921628, EBI-12142257;
CC Q16853; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-3921628, EBI-18053395;
CC Q16853; P42858: HTT; NbExp=3; IntAct=EBI-3921628, EBI-466029;
CC Q16853; O43765: SGTA; NbExp=3; IntAct=EBI-3921628, EBI-347996;
CC Q16853; Q16623: STX1A; NbExp=3; IntAct=EBI-3921628, EBI-712466;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9653080};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:9653080}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q16853-1; Sequence=Displayed;
CC Name=2; Synonyms=VAP-1Delta3;
CC IsoId=Q16853-2; Sequence=VSP_053751, VSP_053752;
CC Name=3;
CC IsoId=Q16853-3; Sequence=VSP_055201;
CC -!- TISSUE SPECIFICITY: Strongly expressed on the high endothelial venules
CC of peripheral lymph nodes and on hepatic endothelia. Also highly
CC expressed in appendix, lung and small intestine. Expressed also in
CC adipose tissue, in bone marrow, colon, heart, kidney, ovary, pancreas,
CC placenta, prostate, skeletal muscle, spleen and testis. Isoform 2 seems
CC to be the predominant transcript in fetal kidneys, fetal cartilage and
CC fetal tonsils. The highest relative expression of isoform 2 occurs in
CC skeletal muscle, heart, pancreas, kidney, and lung.
CC {ECO:0000269|PubMed:17400359, ECO:0000269|PubMed:23349812,
CC ECO:0000269|PubMed:9653080}.
CC -!- INDUCTION: Up-regulated during in vitro adipocyte differentiation.
CC {ECO:0000269|PubMed:17400359}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000269|PubMed:16046623}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:16046623,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
CC ECO:0000269|PubMed:19159218}.
CC -!- MISCELLANEOUS: [Isoform 2]: Devoid of the semicarbazide-sensitive amine
CC oxidase (SSAO) activity. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/aoc3/";
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DR EMBL; U39447; AAC50919.1; -; mRNA.
DR EMBL; AF067406; AAC25170.1; -; mRNA.
DR EMBL; AB050502; BAB18866.1; -; Genomic_DNA.
DR EMBL; JX020506; AGB67480.1; -; mRNA.
DR EMBL; AK025727; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK315129; BAG37582.1; -; mRNA.
DR EMBL; DQ143944; AAZ38716.1; -; Genomic_DNA.
DR EMBL; AC016889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050549; AAH50549.1; -; mRNA.
DR CCDS; CCDS11444.1; -. [Q16853-1]
DR CCDS; CCDS62198.1; -. [Q16853-3]
DR CCDS; CCDS74071.1; -. [Q16853-2]
DR PIR; JC5234; JC5234.
DR RefSeq; NP_001264660.1; NM_001277731.1. [Q16853-2]
DR RefSeq; NP_001264661.1; NM_001277732.1. [Q16853-3]
DR RefSeq; NP_003725.1; NM_003734.3. [Q16853-1]
DR PDB; 1PU4; X-ray; 3.20 A; A/B=1-763.
DR PDB; 1US1; X-ray; 2.90 A; A/B=1-763.
DR PDB; 2C10; X-ray; 2.50 A; A/B/C/D=29-763.
DR PDB; 2C11; X-ray; 2.90 A; A/B/C/D=29-763.
DR PDB; 2Y73; X-ray; 2.60 A; A/B=1-763.
DR PDB; 2Y74; X-ray; 2.95 A; A/B=1-763.
DR PDB; 3ALA; X-ray; 2.90 A; A/B/C/D/E/F/G=33-763.
DR PDB; 4BTW; X-ray; 2.80 A; A/B=27-763.
DR PDB; 4BTX; X-ray; 2.78 A; A/B=27-763.
DR PDB; 4BTY; X-ray; 3.10 A; A/B=27-763.
DR PDBsum; 1PU4; -.
DR PDBsum; 1US1; -.
DR PDBsum; 2C10; -.
DR PDBsum; 2C11; -.
DR PDBsum; 2Y73; -.
DR PDBsum; 2Y74; -.
DR PDBsum; 3ALA; -.
DR PDBsum; 4BTW; -.
DR PDBsum; 4BTX; -.
DR PDBsum; 4BTY; -.
DR AlphaFoldDB; Q16853; -.
DR SMR; Q16853; -.
DR BioGRID; 114192; 58.
DR IntAct; Q16853; 19.
DR STRING; 9606.ENSP00000312326; -.
DR BindingDB; Q16853; -.
DR ChEMBL; CHEMBL3437; -.
DR DrugBank; DB04334; 6-hydroxydopa quinone.
DR DrugBank; DB01275; Hydralazine.
DR DrugBank; DB00780; Phenelzine.
DR DrugCentral; Q16853; -.
DR GuidetoPHARMACOLOGY; 2767; -.
DR GlyConnect; 1502; 9 N-Linked glycans (4 sites).
DR GlyGen; Q16853; 8 sites, 8 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q16853; -.
DR PhosphoSitePlus; Q16853; -.
DR BioMuta; AOC3; -.
DR DMDM; 2501336; -.
DR jPOST; Q16853; -.
DR MassIVE; Q16853; -.
DR PaxDb; Q16853; -.
DR PeptideAtlas; Q16853; -.
DR PRIDE; Q16853; -.
DR ProteomicsDB; 61105; -. [Q16853-1]
DR ABCD; Q16853; 8 sequenced antibodies.
DR Antibodypedia; 611; 435 antibodies from 39 providers.
DR DNASU; 8639; -.
DR Ensembl; ENST00000308423.7; ENSP00000312326.1; ENSG00000131471.7. [Q16853-1]
DR Ensembl; ENST00000591562.1; ENSP00000468632.1; ENSG00000131471.7. [Q16853-3]
DR Ensembl; ENST00000613571.1; ENSP00000484312.1; ENSG00000131471.7. [Q16853-2]
DR Ensembl; ENST00000617500.4; ENSP00000477686.1; ENSG00000131471.7. [Q16853-3]
DR GeneID; 8639; -.
DR KEGG; hsa:8639; -.
DR MANE-Select; ENST00000308423.7; ENSP00000312326.1; NM_003734.4; NP_003725.1.
DR UCSC; uc002ibv.6; human. [Q16853-1]
DR CTD; 8639; -.
DR DisGeNET; 8639; -.
DR GeneCards; AOC3; -.
DR HGNC; HGNC:550; AOC3.
DR HPA; ENSG00000131471; Tissue enhanced (adipose).
DR MIM; 603735; gene.
DR neXtProt; NX_Q16853; -.
DR OpenTargets; ENSG00000131471; -.
DR PharmGKB; PA24840; -.
DR VEuPathDB; HostDB:ENSG00000131471; -.
DR eggNOG; KOG1186; Eukaryota.
DR GeneTree; ENSGT00950000183207; -.
DR HOGENOM; CLU_015739_1_0_1; -.
DR InParanoid; Q16853; -.
DR OMA; CMFEIDK; -.
DR OrthoDB; 1320015at2759; -.
DR PhylomeDB; Q16853; -.
DR TreeFam; TF314750; -.
DR BRENDA; 1.4.3.21; 2681.
DR PathwayCommons; Q16853; -.
DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR SABIO-RK; Q16853; -.
DR SignaLink; Q16853; -.
DR BioGRID-ORCS; 8639; 11 hits in 1063 CRISPR screens.
DR ChiTaRS; AOC3; human.
DR EvolutionaryTrace; Q16853; -.
DR GeneWiki; AOC3; -.
DR GenomeRNAi; 8639; -.
DR Pharos; Q16853; Tchem.
DR PRO; PR:Q16853; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q16853; protein.
DR Bgee; ENSG00000131471; Expressed in blood vessel layer and 176 other tissues.
DR ExpressionAtlas; Q16853; baseline and differential.
DR Genevisible; Q16853; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:CACAO.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO.
DR GO; GO:0005794; C:Golgi apparatus; IDA:CACAO.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0048038; F:quinone binding; IDA:UniProtKB.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR GO; GO:1902283; P:negative regulation of primary amine oxidase activity; IDA:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB.
DR Gene3D; 2.70.98.20; -; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR InterPro; IPR015800; Cu_amine_oxidase_N2.
DR InterPro; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638; PTHR10638; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR PRINTS; PR00766; CUDAOXIDASE.
DR SUPFAM; SSF49998; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Copper; Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Signal-anchor; TPQ;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..763
FT /note="Membrane primary amine oxidase"
FT /id="PRO_0000064102"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..763
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 386
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT ACT_SITE 471
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2Y73"
FT BINDING 384..394
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:4BTY"
FT BINDING 468..473
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 520
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:16046623,
FT ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:3ALA, ECO:0007744|PDB:4BTW,
FT ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY"
FT BINDING 522
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:16046623,
FT ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:3ALA, ECO:0007744|PDB:4BTW,
FT ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY"
FT BINDING 529
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:3ALA, ECO:0007744|PDB:4BTW,
FT ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:3ALA, ECO:0007744|PDB:4BTW,
FT ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY"
FT BINDING 531
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:3ALA, ECO:0007744|PDB:4BTW,
FT ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY"
FT BINDING 572
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:3ALA, ECO:0007744|PDB:4BTW,
FT ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY"
FT BINDING 638
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C11"
FT BINDING 641
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:4BTW"
FT BINDING 663
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:3ALA, ECO:0007744|PDB:4BTW,
FT ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY"
FT BINDING 665
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:3ALA, ECO:0007744|PDB:4BTW,
FT ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY"
FT BINDING 667
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:3ALA, ECO:0007744|PDB:4BTW,
FT ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY"
FT BINDING 673
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:3ALA, ECO:0007744|PDB:4BTW,
FT ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY"
FT BINDING 674
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:3ALA, ECO:0007744|PDB:4BTW,
FT ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY"
FT BINDING 684
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:16046623,
FT ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:3ALA, ECO:0007744|PDB:4BTW,
FT ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY"
FT MOD_RES 471
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0007744|PDB:1PU4"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16046623,
FT ECO:0000269|PubMed:19159218, ECO:0007744|PDB:1PU4,
FT ECO:0007744|PDB:1US1, ECO:0007744|PDB:2C10,
FT ECO:0007744|PDB:2C11, ECO:0007744|PDB:2Y73,
FT ECO:0007744|PDB:2Y74, ECO:0007744|PDB:3ALA,
FT ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX,
FT ECO:0007744|PDB:4BTY"
FT CARBOHYD 212
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305|PubMed:16046623"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16046623,
FT ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:3ALA, ECO:0007744|PDB:4BTW,
FT ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16046623,
FT ECO:0000269|PubMed:19159218, ECO:0007744|PDB:2C10,
FT ECO:0007744|PDB:2C11, ECO:0007744|PDB:4BTY"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16046623,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218, ECO:0007744|PDB:2C10,
FT ECO:0007744|PDB:2C11, ECO:0007744|PDB:2Y73,
FT ECO:0007744|PDB:2Y74, ECO:0007744|PDB:3ALA,
FT ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX,
FT ECO:0007744|PDB:4BTY"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16046623,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
FT ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16046623,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
FT ECO:0007744|PDB:2C10, ECO:0007744|PDB:2C11,
FT ECO:0007744|PDB:2Y73, ECO:0007744|PDB:2Y74,
FT ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX,
FT ECO:0007744|PDB:4BTY"
FT DISULFID 198..199
FT /evidence="ECO:0000269|PubMed:16046623"
FT DISULFID 404..430
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 734..741
FT /evidence="ECO:0000269|PubMed:16046623"
FT DISULFID 748
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:16046623"
FT VAR_SEQ 1..543
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055201"
FT VAR_SEQ 630..634
FT /note="YQLAV -> IWWPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:23349812"
FT /id="VSP_053751"
FT VAR_SEQ 635..763
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:23349812"
FT /id="VSP_053752"
FT VARIANT 5
FT /note="T -> R (in dbSNP:rs33954211)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025035"
FT VARIANT 78
FT /note="R -> Q (in dbSNP:rs402680)"
FT /id="VAR_052603"
FT VARIANT 167
FT /note="H -> Y (in dbSNP:rs2228470)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025027"
FT VARIANT 171
FT /note="V -> M (in dbSNP:rs408038)"
FT /id="VAR_052604"
FT VARIANT 203
FT /note="H -> R (in dbSNP:rs630079)"
FT /id="VAR_052605"
FT VARIANT 317
FT /note="Y -> H (in dbSNP:rs438287)"
FT /id="VAR_012064"
FT VARIANT 329
FT /note="R -> Q (in dbSNP:rs2229595)"
FT /id="VAR_024343"
FT VARIANT 371
FT /note="I -> T (in dbSNP:rs35097308)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025028"
FT VARIANT 408
FT /note="A -> S (in dbSNP:rs35643019)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025029"
FT VARIANT 426
FT /note="R -> H (in dbSNP:rs33986943)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025030"
FT VARIANT 441
FT /note="R -> W (in dbSNP:rs2229596)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025031"
FT VARIANT 582
FT /note="A -> T (in dbSNP:rs34987927)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025032"
FT VARIANT 700
FT /note="G -> S (in dbSNP:rs477207)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025033"
FT VARIANT 749
FT /note="A -> V (in dbSNP:rs34012919)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025034"
FT MUTAGEN 211
FT /note="M->V: Increased activity towards 2-phenylethylamine,
FT and decreased activity towards methylamine; when associated
FT with N-394 and G-469."
FT /evidence="ECO:0000269|PubMed:19588076"
FT MUTAGEN 394
FT /note="Y->N: Increased activity towards 2-phenylethylamine,
FT and decreased activity towards methylamine; when associated
FT with V-211 and G-469."
FT /evidence="ECO:0000269|PubMed:19588076"
FT MUTAGEN 469
FT /note="L->G: Increased activity towards 2-phenylethylamine,
FT and decreased activity towards methylamine; when associated
FT with V-211 and N-394."
FT /evidence="ECO:0000269|PubMed:19588076"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:3ALA"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:2C10"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:2C11"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 274..282
FT /evidence="ECO:0007829|PDB:2C10"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:4BTW"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:4BTW"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 329..342
FT /evidence="ECO:0007829|PDB:2C10"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 346..354
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 357..372
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:2C10"
FT TURN 391..394
FT /evidence="ECO:0007829|PDB:2C10"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 408..421
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 423..445
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 451..468
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 471..479
FT /evidence="ECO:0007829|PDB:2C10"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:4BTY"
FT STRAND 485..493
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 506..512
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 520..530
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 534..551
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 554..569
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 572..575
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 577..581
FT /evidence="ECO:0007829|PDB:4BTW"
FT STRAND 585..594
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 600..608
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 617..619
FT /evidence="ECO:0007829|PDB:2C11"
FT HELIX 622..629
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 630..636
FT /evidence="ECO:0007829|PDB:2C10"
FT TURN 647..651
FT /evidence="ECO:0007829|PDB:2Y73"
FT STRAND 653..655
FT /evidence="ECO:0007829|PDB:1US1"
FT HELIX 660..663
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 670..684
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 688..690
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 700..713
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 715..718
FT /evidence="ECO:0007829|PDB:2C10"
FT STRAND 723..729
FT /evidence="ECO:0007829|PDB:2C10"
FT TURN 734..736
FT /evidence="ECO:0007829|PDB:2C10"
FT HELIX 738..741
FT /evidence="ECO:0007829|PDB:2Y73"
FT HELIX 742..745
FT /evidence="ECO:0007829|PDB:2C10"
SQ SEQUENCE 763 AA; 84622 MW; 58AD55605EC9D228 CRC64;
MNQKTILVLL ILAVITIFAL VCVLLVGRGG DGGEPSQLPH CPSVSPSAQP WTHPGQSQLF
ADLSREELTA VMRFLTQRLG PGLVDAAQAR PSDNCVFSVE LQLPPKAAAL AHLDRGSPPP
AREALAIVFF GRQPQPNVSE LVVGPLPHPS YMRDVTVERH GGPLPYHRRP VLFQEYLDID
QMIFNRELPQ ASGLLHHCCF YKHRGRNLVT MTTAPRGLQS GDRATWFGLY YNISGAGFFL
HHVGLELLVN HKALDPARWT IQKVFYQGRY YDSLAQLEAQ FEAGLVNVVL IPDNGTGGSW
SLKSPVPPGP APPLQFYPQG PRFSVQGSRV ASSLWTFSFG LGAFSGPRIF DVRFQGERLV
YEISLQEALA IYGGNSPAAM TTRYVDGGFG MGKYTTPLTR GVDCPYLATY VDWHFLLESQ
APKTIRDAFC VFEQNQGLPL RRHHSDLYSH YFGGLAETVL VVRSMSTLLN YDYVWDTVFH
PSGAIEIRFY ATGYISSAFL FGATGKYGNQ VSEHTLGTVH THSAHFKVDL DVAGLENWVW
AEDMVFVPMA VPWSPEHQLQ RLQVTRKLLE MEEQAAFLVG SATPRYLYLA SNHSNKWGHP
RGYRIQMLSF AGEPLPQNSS MARGFSWERY QLAVTQRKEE EPSSSSVFNQ NDPWAPTVDF
SDFINNETIA GKDLVAWVTA GFLHIPHAED IPNTVTVGNG VGFFLRPYNF FDEDPSFYSA
DSIYFRGDQD AGACEVNPLA CLPQAAACAP DLPAFSHGGF SHN
