AMPE_HUMAN
ID AMPE_HUMAN Reviewed; 957 AA.
AC Q07075; Q504U2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Glutamyl aminopeptidase;
DE Short=EAP;
DE EC=3.4.11.7 {ECO:0000269|PubMed:10692253, ECO:0000269|PubMed:23888046};
DE AltName: Full=Aminopeptidase A;
DE Short=AP-A;
DE AltName: Full=Differentiation antigen gp160;
DE AltName: CD_antigen=CD249;
GN Name=ENPEP;
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], PROTEIN SEQUENCE OF 242-251; 300-316 AND
RP 369-377, AND VARIANTS ARG-213 AND ALA-218.
RC TISSUE=Kidney cortex;
RX PubMed=8346219; DOI=10.1073/pnas.90.15.7069;
RA Nanus D.M., Engelstein D., Gastl G.A., Gluck L., Vidal M.J., Morrison M.,
RA Finstad C.L., Bander N.H., Albino A.P.;
RT "Molecular cloning of the human kidney differentiation antigen gp160: human
RT aminopeptidase A.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7069-7073(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-213.
RC TISSUE=Kidney;
RX PubMed=8244382; DOI=10.1006/geno.1993.1386;
RA Li L., Wang J., Cooper M.D.;
RT "cDNA cloning and expression of human glutamyl aminopeptidase
RT (aminopeptidase A).";
RL Genomics 17:657-664(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-213.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-213.
RC TISSUE=Placenta;
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 [5]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10692253; DOI=10.1053/plac.1999.0456;
RA Ino K., Nagasaka T., Okamoto T., Uehara C., Nakazato H., Nakashima N.,
RA Mizutani S.;
RT "Expression of aminopeptidase A in human gestational choriocarcinoma cell
RT lines and tissues.";
RL Placenta 21:63-72(2000).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-607.
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 [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-124; ASN-324; ASN-607; ASN-763
RP AND ASN-773.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9] {ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 76-957 IN COMPLEX WITH SUBSTRATE;
RP CALCIUM AND INHIBITORS, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBUNIT, ACTIVE SITE, METAL-BINDING SITES, SUBSTRATE-BINDING, COFACTOR,
RP SITE, MUTAGENESIS OF THR-356 AND ARG-887, AND GLYCOSYLATION AT ASN-98;
RP ASN-197; ASN-324; ASN-340; ASN-554; ASN-597; ASN-678; ASN-763; ASN-801 AND
RP ASN-828.
RX PubMed=23888046; DOI=10.1074/jbc.m113.494955;
RA Yang Y., Liu C., Lin Y.L., Li F.;
RT "Structural insights into central hypertension regulation by human
RT aminopeptidase A.";
RL J. Biol. Chem. 288:25638-25645(2013).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] THR-887.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Regulates central hypertension through its calcium-modulated
CC preference to cleave N-terminal acidic residues from peptides such as
CC angiotensin II. {ECO:0000305|PubMed:23888046}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal glutamate (and to a lesser extent
CC aspartate) from a peptide.; EC=3.4.11.7;
CC Evidence={ECO:0000269|PubMed:10692253, ECO:0000269|PubMed:23888046};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:23888046};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:23888046};
CC -!- ACTIVITY REGULATION: Substrate specificity is modulated by calcium
CC which enhances the enzymatic activity for cleavage of acidic residues
CC while reducing its activity with basic residues. Inhibited by
CC aminopeptidase inhibitors amastatin and bestatin.
CC {ECO:0000269|PubMed:10692253, ECO:0000269|PubMed:23888046}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:23888046}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10692253};
CC Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in choriocarcinoma cancer cell lines (at
CC protein level) (PubMed:10692253). Expressed by epithelial cells of the
CC proximal tubule cells and the glomerulus of the nephron. Also found in
CC a variety of other tissues. {ECO:0000269|PubMed:10692253}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; L14721; AAA35522.1; -; mRNA.
DR EMBL; L12468; AAA16876.1; -; mRNA.
DR EMBL; AC017068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094770; AAH94770.1; -; mRNA.
DR CCDS; CCDS3691.1; -.
DR PIR; A47531; A47531.
DR RefSeq; NP_001968.3; NM_001977.3.
DR PDB; 4KX7; X-ray; 2.15 A; A=76-957.
DR PDB; 4KX8; X-ray; 2.40 A; A=76-957.
DR PDB; 4KX9; X-ray; 2.25 A; A=76-957.
DR PDB; 4KXA; X-ray; 2.40 A; A=76-957.
DR PDB; 4KXB; X-ray; 2.40 A; A=76-957.
DR PDB; 4KXC; X-ray; 2.40 A; A=76-957.
DR PDB; 4KXD; X-ray; 2.15 A; A=76-957.
DR PDBsum; 4KX7; -.
DR PDBsum; 4KX8; -.
DR PDBsum; 4KX9; -.
DR PDBsum; 4KXA; -.
DR PDBsum; 4KXB; -.
DR PDBsum; 4KXC; -.
DR PDBsum; 4KXD; -.
DR AlphaFoldDB; Q07075; -.
DR SMR; Q07075; -.
DR BioGRID; 108342; 6.
DR IntAct; Q07075; 5.
DR STRING; 9606.ENSP00000265162; -.
DR BindingDB; Q07075; -.
DR ChEMBL; CHEMBL3439; -.
DR DrugBank; DB00142; Glutamic acid.
DR MEROPS; M01.003; -.
DR GlyConnect; 1940; 8 N-Linked glycans (6 sites).
DR GlyGen; Q07075; 21 sites, 8 N-linked glycans (6 sites), 5 O-linked glycans (4 sites).
DR iPTMnet; Q07075; -.
DR PhosphoSitePlus; Q07075; -.
DR BioMuta; ENPEP; -.
DR DMDM; 296439445; -.
DR EPD; Q07075; -.
DR jPOST; Q07075; -.
DR MassIVE; Q07075; -.
DR MaxQB; Q07075; -.
DR PaxDb; Q07075; -.
DR PeptideAtlas; Q07075; -.
DR PRIDE; Q07075; -.
DR ProteomicsDB; 58502; -.
DR Antibodypedia; 979; 533 antibodies from 37 providers.
DR DNASU; 2028; -.
DR Ensembl; ENST00000265162.10; ENSP00000265162.5; ENSG00000138792.10.
DR GeneID; 2028; -.
DR KEGG; hsa:2028; -.
DR MANE-Select; ENST00000265162.10; ENSP00000265162.5; NM_001977.4; NP_001968.3.
DR UCSC; uc003iab.5; human.
DR CTD; 2028; -.
DR DisGeNET; 2028; -.
DR GeneCards; ENPEP; -.
DR HGNC; HGNC:3355; ENPEP.
DR HPA; ENSG00000138792; Tissue enhanced (intestine, kidney).
DR MIM; 138297; gene.
DR neXtProt; NX_Q07075; -.
DR OpenTargets; ENSG00000138792; -.
DR PharmGKB; PA27790; -.
DR VEuPathDB; HostDB:ENSG00000138792; -.
DR eggNOG; KOG1046; Eukaryota.
DR GeneTree; ENSGT00940000156946; -.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; Q07075; -.
DR OMA; FSHGAME; -.
DR OrthoDB; 110058at2759; -.
DR PhylomeDB; Q07075; -.
DR TreeFam; TF300395; -.
DR BRENDA; 3.4.11.7; 2681.
DR PathwayCommons; Q07075; -.
DR Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR SignaLink; Q07075; -.
DR BioGRID-ORCS; 2028; 10 hits in 1073 CRISPR screens.
DR ChiTaRS; ENPEP; human.
DR GenomeRNAi; 2028; -.
DR Pharos; Q07075; Tchem.
DR PRO; PR:Q07075; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q07075; protein.
DR Bgee; ENSG00000138792; Expressed in jejunal mucosa and 141 other tissues.
DR ExpressionAtlas; Q07075; baseline and differential.
DR Genevisible; Q07075; HS.
DR GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IDA:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0002003; P:angiotensin maturation; NAS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0007267; P:cell-cell signaling; NAS:UniProtKB.
DR GO; GO:0032835; P:glomerulus development; ISS:UniProtKB.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IBA:GO_Central.
DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR033508; Aminopeptidase_A.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF242; PTHR11533:SF242; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Calcium; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Membrane; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..957
FT /note="Glutamyl aminopeptidase"
FT /id="PRO_0000095095"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..957
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 44..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KXB,
FT ECO:0007744|PDB:4KXD"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23888046,
FT ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA,
FT ECO:0007744|PDB:4KXB"
FT BINDING 357..361
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23888046,
FT ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB,
FT ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7,
FT ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9,
FT ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB,
FT ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7,
FT ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9,
FT ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB,
FT ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7,
FT ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9,
FT ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB,
FT ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD"
FT BINDING 887
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23888046,
FT ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXC,
FT ECO:0007744|PDB:4KXD"
FT SITE 221
FT /note="Binds calcium which modulates its enzyme activity"
FT /evidence="ECO:0000269|PubMed:23888046"
FT SITE 479
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:23888046,
FT ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA,
FT ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC,
FT ECO:0007744|PDB:4KXD"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine; atypical"
FT /evidence="ECO:0000269|PubMed:23888046,
FT ECO:0007744|PDB:4KX7"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23888046,
FT ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8,
FT ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA,
FT ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC,
FT ECO:0007744|PDB:4KXD"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7,
FT ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9,
FT ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB,
FT ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23888046,
FT ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9,
FT ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB,
FT ECO:0007744|PDB:4KXC"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23888046,
FT ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8,
FT ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA,
FT ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23888046,
FT ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KXD"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23888046,
FT ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8,
FT ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA,
FT ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC,
FT ECO:0007744|PDB:4KXD"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7,
FT ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9,
FT ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB,
FT ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23888046,
FT ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8,
FT ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA,
FT ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC,
FT ECO:0007744|PDB:4KXD"
FT CARBOHYD 828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23888046,
FT ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8,
FT ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA,
FT ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC,
FT ECO:0007744|PDB:4KXD"
FT VARIANT 213
FT /note="Q -> R (in dbSNP:rs10004516)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15815621, ECO:0000269|PubMed:8244382,
FT ECO:0000269|PubMed:8346219"
FT /id="VAR_030359"
FT VARIANT 218
FT /note="V -> A (in dbSNP:rs1126483)"
FT /evidence="ECO:0000269|PubMed:8346219"
FT /id="VAR_030360"
FT VARIANT 437
FT /note="R -> H (in dbSNP:rs34949711)"
FT /id="VAR_057056"
FT VARIANT 861
FT /note="S -> R (in dbSNP:rs35812243)"
FT /id="VAR_057057"
FT VARIANT 887
FT /note="R -> T (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036047"
FT MUTAGEN 356
FT /note="T->V: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:23888046"
FT MUTAGEN 887
FT /note="R->A: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:23888046"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 97..109
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 114..125
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 138..148
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:4KXD"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 200..210
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 213..221
FT /evidence="ECO:0007829|PDB:4KX7"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 241..250
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 261..276
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 313..319
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 320..336
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 346..353
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:4KX7"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 381..397
FT /evidence="ECO:0007829|PDB:4KX7"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 413..430
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 436..443
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 445..451
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 467..472
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 476..493
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 495..508
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 516..527
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 531..535
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 545..550
FT /evidence="ECO:0007829|PDB:4KX7"
FT TURN 551..553
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 554..559
FT /evidence="ECO:0007829|PDB:4KX7"
FT TURN 574..577
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 581..587
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 590..596
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:4KX7"
FT STRAND 625..630
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 633..646
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 647..649
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 652..667
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 673..678
FT /evidence="ECO:0007829|PDB:4KX7"
FT TURN 679..682
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 683..685
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 689..705
FT /evidence="ECO:0007829|PDB:4KX7"
FT TURN 706..708
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 712..731
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 739..754
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 758..771
FT /evidence="ECO:0007829|PDB:4KX7"
FT TURN 780..782
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 783..794
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 797..809
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 813..823
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 829..838
FT /evidence="ECO:0007829|PDB:4KX7"
FT TURN 842..844
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 847..849
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 850..858
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 863..873
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 875..882
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 887..891
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 892..896
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 902..914
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 919..921
FT /evidence="ECO:0007829|PDB:4KX7"
FT HELIX 922..953
FT /evidence="ECO:0007829|PDB:4KX7"
SQ SEQUENCE 957 AA; 109244 MW; AB6407432A45A7C6 CRC64;
MNFAEREGSK RYCIQTKHVA ILCAVVVGVG LIVGLAVGLT RSCDSSGDGG PGTAPAPSHL
PSSTASPSGP PAQDQDICPA SEDESGQWKN FRLPDFVNPV HYDLHVKPLL EEDTYTGTVS
ISINLSAPTR YLWLHLRETR ITRLPELKRP SGDQVQVRRC FEYKKQEYVV VEAEEELTPS
SGDGLYLLTM EFAGWLNGSL VGFYRTTYTE NGQVKSIVAT DHEPTDARKS FPCFDEPNKK
ATYTISITHP KEYGALSNMP VAKEESVDDK WTRTTFEKSV PMSTYLVCFA VHQFDSVKRI
SNSGKPLTIY VQPEQKHTAE YAANITKSVF DYFEEYFAMN YSLPKLDKIA IPDFGTGAME
NWGLITYRET NLLYDPKESA SSNQQRVATV VAHELVHQWF GNIVTMDWWE DLWLNEGFAS
FFEFLGVNHA ETDWQMRDQM LLEDVLPVQE DDSLMSSHPI IVTVTTPDEI TSVFDGISYS
KGSSILRMLE DWIKPENFQK GCQMYLEKYQ FKNAKTSDFW AALEEASRLP VKEVMDTWTR
QMGYPVLNVN GVKNITQKRF LLDPRANPSQ PPSDLGYTWN IPVKWTEDNI TSSVLFNRSE
KEGITLNSSN PSGNAFLKIN PDHIGFYRVN YEVATWDSIA TALSLNHKTF SSADRASLID
DAFALARAQL LDYKVALNLT KYLKREENFL PWQRVISAVT YIISMFEDDK ELYPMIEEYF
QGQVKPIADS LGWNDAGDHV TKLLRSSVLG FACKMGDREA LNNASSLFEQ WLNGTVSLPV
NLRLLVYRYG MQNSGNEISW NYTLEQYQKT SLAQEKEKLL YGLASVKNVT LLSRYLDLLK
DTNLIKTQDV FTVIRYISYN SYGKNMAWNW IQLNWDYLVN RYTLNNRNLG RIVTIAEPFN
TELQLWQMES FFAKYPQAGA GEKPREQVLE TVKNNIEWLK QHRNTIREWF FNLLESG
