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Leucyl-cystinyl aminopeptidase (Cystinyl aminopeptidase) (EC 3.4.11.3) (Insulin-regulated membrane aminopeptidase) (Insulin-responsive aminopeptidase) (IRAP) (Oxytocinase) (OTase) (Placental leucine aminopeptidase) (P-LAP) [Cleaved into: Leucyl-cystinyl aminopeptidase, pregnancy serum form]

 LCAP_HUMAN              Reviewed;        1025 AA.
Q9UIQ6; O00769; Q15145; Q59H76; Q9TNQ2; Q9TNQ3; Q9UIQ7;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 3.
22-NOV-2017, entry version 177.
RecName: Full=Leucyl-cystinyl aminopeptidase;
Short=Cystinyl aminopeptidase;
EC=3.4.11.3;
AltName: Full=Insulin-regulated membrane aminopeptidase;
AltName: Full=Insulin-responsive aminopeptidase;
Short=IRAP;
AltName: Full=Oxytocinase;
Short=OTase;
AltName: Full=Placental leucine aminopeptidase;
Short=P-LAP;
Contains:
RecName: Full=Leucyl-cystinyl aminopeptidase, pregnancy serum form;
Name=LNPEP; Synonyms=OTASE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 160-168; 319-332;
615-624; 635-647; 798-814 AND 870-880, AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=8550619; DOI=10.1074/jbc.271.1.56;
Rogi T., Tsujimoto M., Nakazato H., Mizutani S., Tomoda Y.;
"Human placental leucine aminopeptidase/oxytocinase. A new member of
type II membrane-spanning zinc metallopeptidase family.";
J. Biol. Chem. 271:56-61(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=9177475; DOI=10.1016/S0167-4781(97)00036-5;
Laustsen P.G., Rasmussen T.E., Petersen K., Pedraza-Diaz S.,
Moestrup S.K., Gliemann J., Sottrup-Jensen L., Kristensen T.;
"The complete amino acid sequence of human placental oxytocinase.";
Biochim. Biophys. Acta 1352:1-7(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
PubMed=10759854; DOI=10.1046/j.1432-1327.2000.01234.x;
Rasmussen T.E., Pedraza-Diaz S., Hardre R., Laustsen P.G.,
Carrion A.G., Kristensen T.;
"Structure of the human oxytocinase/insulin-regulated aminopeptidase
gene and localization to chromosome 5q21.";
Eur. J. Biochem. 267:2297-2306(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, CATALYTIC
ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11389728; DOI=10.1046/j.1432-1327.2001.02221.x;
Matsumoto H., Nagasaka T., Hattori A., Rogi T., Tsuruoka N.,
Mizutani S., Tsujimoto M.;
"Expression of placental leucine aminopeptidase/oxytocinase in
neuronal cells and its action on neuronal peptides.";
Eur. J. Biochem. 268:3259-3266(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 206-1025.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 285-301 AND 710-724.
PubMed=8119729; DOI=10.1007/BF00188785;
Falk K., Roetzschke O., Stevanovic S., Jung G., Rammensee H.G.;
"Pool sequencing of natural HLA-DR, DQ, and DP ligands reveals
detailed peptide motifs, constraints of processing, and general
rules.";
Immunogenetics 39:230-242(1994).
[7]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=1731608; DOI=10.1016/0003-9861(92)90007-J;
Tsujimoto M., Mizutani S., Adachi H., Kimura M., Nakazato H.,
Tomoda Y.;
"Identification of human placental leucine aminopeptidase as
oxytocinase.";
Arch. Biochem. Biophys. 292:388-392(1992).
[8]
FUNCTION.
PubMed=11707427; DOI=10.1074/jbc.C100512200;
Albiston A.L., McDowall S.G., Matsacos D., Sim P., Clune E.,
Mustafa T., Lee J., Mendelsohn F.A., Simpson R.J., Connolly L.M.,
Chai S.Y.;
"Evidence that the angiotensin IV (AT(4)) receptor is the enzyme
insulin-regulated aminopeptidase.";
J. Biol. Chem. 276:48623-48626(2001).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-448; ASN-682 AND
ASN-850.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-91, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Release of an N-terminal amino acid, cleaves before
cysteine, leucine as well as other amino acids. Degrades peptide
hormones such as oxytocin, vasopressin and angiotensin III, and
plays a role in maintaining homeostasis during pregnancy. May be
involved in the inactivation of neuronal peptides in the brain.
Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may
be the angiotensin IV receptor in the brain.
{ECO:0000269|PubMed:11389728, ECO:0000269|PubMed:11707427,
ECO:0000269|PubMed:1731608}.
-!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Cys-|-
Xaa-, in which the half-cystine residue is involved in a disulfide
loop, notably in oxytocin or vasopressin. Hydrolysis rates on a
range of aminoacyl arylamides exceed that for the cystinyl
derivative, however. {ECO:0000269|PubMed:11389728,
ECO:0000269|PubMed:1731608}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Homodimer. Binds tankyrases 1 and 2.
-!- INTERACTION:
Q969F0:FATE1; NbExp=3; IntAct=EBI-2805360, EBI-743099;
Q04864:REL; NbExp=3; IntAct=EBI-2805360, EBI-307352;
P15884:TCF4; NbExp=3; IntAct=EBI-2805360, EBI-533224;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11389728};
Single-pass type II membrane protein
{ECO:0000269|PubMed:11389728}. Note=In brain only the membrane-
bound form is found. The protein resides in intracellular vesicles
together with GLUT4 and can then translocate to the cell surface
in response to insulin and/or oxytocin. Localization may be
determined by dileucine internalization motifs, and/or by
interaction with tankyrases.
-!- SUBCELLULAR LOCATION: Leucyl-cystinyl aminopeptidase, pregnancy
serum form: Secreted. Note=During pregnancy serum levels are low
in the first trimester, rise progressively during the second and
third trimester and decrease rapidly after parturition.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1;
IsoId=Q9UIQ6-1; Sequence=Displayed;
Name=2;
IsoId=Q9UIQ6-2; Sequence=VSP_005448;
Name=3;
IsoId=Q9UIQ6-3; Sequence=VSP_005449;
-!- TISSUE SPECIFICITY: Highly expressed in placenta, heart, kidney
and small intestine. Detected at lower levels in neuronal cells in
the brain, in skeletal muscle, spleen, liver, testes and colon.
{ECO:0000269|PubMed:11389728, ECO:0000269|PubMed:8550619,
ECO:0000269|PubMed:9177475}.
-!- PTM: The pregnancy serum form is derived from the membrane-bound
form by proteolytic processing.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:19349973}.
-!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA09436.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAD92120.1; Type=Frameshift; Positions=405; Evidence={ECO:0000305};
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EMBL; D50810; BAA09436.1; ALT_INIT; mRNA.
EMBL; U62768; AAB66672.1; -; mRNA.
EMBL; U62769; AAB66673.1; -; mRNA.
EMBL; AJ131023; CAB61646.1; -; Genomic_DNA.
EMBL; AJ131025; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131026; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131027; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131028; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131029; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131030; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131031; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131032; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131033; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131034; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131035; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131036; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131037; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131038; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131039; CAB61646.1; JOINED; Genomic_DNA.
EMBL; AJ131025; CAB94753.1; -; Genomic_DNA.
EMBL; AJ131026; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AJ131027; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AJ131028; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AJ131029; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AJ131030; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AJ131031; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AJ131032; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AJ131033; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AJ131034; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AJ131035; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AJ131036; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AJ131037; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AJ131038; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AJ131039; CAB94753.1; JOINED; Genomic_DNA.
EMBL; AB208883; BAD92120.1; ALT_FRAME; mRNA.
CCDS; CCDS4087.1; -. [Q9UIQ6-1]
CCDS; CCDS43346.1; -. [Q9UIQ6-2]
PIR; A59383; A59383.
PIR; A59384; A59384.
RefSeq; NP_005566.2; NM_005575.2. [Q9UIQ6-1]
RefSeq; NP_787116.2; NM_175920.3. [Q9UIQ6-2]
UniGene; Hs.527199; -.
UniGene; Hs.656905; -.
PDB; 4P8Q; X-ray; 3.02 A; A/B=155-1025.
PDB; 4PJ6; X-ray; 2.96 A; A/B=155-1025.
PDB; 4Z7I; X-ray; 3.31 A; A/B=155-1025.
PDB; 5C97; X-ray; 3.37 A; A/B=155-1025.
PDB; 5JHQ; X-ray; 3.20 A; E/F/G/H/I/J/K/L=92-107.
PDB; 5MJ6; X-ray; 2.53 A; A/B=155-1025.
PDBsum; 4P8Q; -.
PDBsum; 4PJ6; -.
PDBsum; 4Z7I; -.
PDBsum; 5C97; -.
PDBsum; 5JHQ; -.
PDBsum; 5MJ6; -.
ProteinModelPortal; Q9UIQ6; -.
SMR; Q9UIQ6; -.
BioGrid; 110196; 45.
ELM; Q9UIQ6; -.
IntAct; Q9UIQ6; 24.
STRING; 9606.ENSP00000231368; -.
BindingDB; Q9UIQ6; -.
ChEMBL; CHEMBL2693; -.
GuidetoPHARMACOLOGY; 1570; -.
MEROPS; M01.011; -.
iPTMnet; Q9UIQ6; -.
PhosphoSitePlus; Q9UIQ6; -.
SwissPalm; Q9UIQ6; -.
BioMuta; LNPEP; -.
DMDM; 145559489; -.
EPD; Q9UIQ6; -.
PaxDb; Q9UIQ6; -.
PeptideAtlas; Q9UIQ6; -.
PRIDE; Q9UIQ6; -.
DNASU; 4012; -.
Ensembl; ENST00000231368; ENSP00000231368; ENSG00000113441. [Q9UIQ6-1]
Ensembl; ENST00000395770; ENSP00000379117; ENSG00000113441. [Q9UIQ6-2]
GeneID; 4012; -.
KEGG; hsa:4012; -.
UCSC; uc003kmv.2; human. [Q9UIQ6-1]
CTD; 4012; -.
DisGeNET; 4012; -.
EuPathDB; HostDB:ENSG00000113441.15; -.
GeneCards; LNPEP; -.
H-InvDB; HIX0005054; -.
HGNC; HGNC:6656; LNPEP.
HPA; HPA043642; -.
MIM; 151300; gene.
neXtProt; NX_Q9UIQ6; -.
OpenTargets; ENSG00000113441; -.
PharmGKB; PA30418; -.
eggNOG; KOG1046; Eukaryota.
eggNOG; COG0308; LUCA.
GeneTree; ENSGT00760000119082; -.
HOVERGEN; HBG108296; -.
InParanoid; Q9UIQ6; -.
KO; K01257; -.
OMA; MMKTWTL; -.
OrthoDB; EOG091G01GH; -.
PhylomeDB; Q9UIQ6; -.
TreeFam; TF300395; -.
Reactome; R-HSA-1236977; Endosomal/Vacuolar pathway.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SABIO-RK; Q9UIQ6; -.
ChiTaRS; LNPEP; human.
GeneWiki; Cystinyl_aminopeptidase; -.
GenomeRNAi; 4012; -.
PMAP-CutDB; Q9UIQ6; -.
PRO; PR:Q9UIQ6; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113441; -.
CleanEx; HS_LNPEP; -.
Genevisible; Q9UIQ6; HS.
GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031905; C:early endosome lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005622; C:intracellular; IDA:HGNC.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
GO; GO:0004177; F:aminopeptidase activity; EXP:Reactome.
GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
GO; GO:0042277; F:peptide binding; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0007565; P:female pregnancy; TAS:ProtInc.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0008217; P:regulation of blood pressure; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
CDD; cd09601; M1_APN_2; 1.
InterPro; IPR034017; Cystinyl_aminopeptidase.
InterPro; IPR024571; ERAP1-like_C_dom.
InterPro; IPR034016; M1_APN-typ.
InterPro; IPR001930; Peptidase_M1.
InterPro; IPR014782; Peptidase_M1_N.
PANTHER; PTHR11533; PTHR11533; 1.
PANTHER; PTHR11533:SF42; PTHR11533:SF42; 1.
Pfam; PF11838; ERAP1_C; 1.
Pfam; PF01433; Peptidase_M1; 1.
PRINTS; PR00756; ALADIPTASE.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Aminopeptidase;
Cell membrane; Complete proteome; Direct protein sequencing;
Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
Phosphoprotein; Polymorphism; Protease; Reference proteome; Secreted;
Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
CHAIN 1 1025 Leucyl-cystinyl aminopeptidase.
/FTId=PRO_0000095114.
CHAIN 155 1025 Leucyl-cystinyl aminopeptidase, pregnancy
serum form.
/FTId=PRO_0000292264.
TOPO_DOM 1 110 Cytoplasmic. {ECO:0000255}.
TRANSMEM 111 131 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 132 1025 Extracellular. {ECO:0000255}.
REGION 96 101 Tankyrase binding.
REGION 428 432 Substrate binding. {ECO:0000250}.
MOTIF 53 54 Dileucine internalization motif.
{ECO:0000255}.
MOTIF 76 77 Dileucine internalization motif.
{ECO:0000255}.
ACT_SITE 465 465 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 464 464 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 468 468 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 487 487 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
BINDING 295 295 Substrate. {ECO:0000250}.
SITE 154 155 Cleavage; to produce pregnancy serum
form.
SITE 549 549 Transition state stabilizer.
{ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 70 70 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8C129}.
MOD_RES 80 80 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 374 374 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 525 525 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 578 578 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 598 598 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 664 664 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 682 682 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 760 760 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 834 834 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 850 850 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 989 989 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 19 Missing (in isoform 3).
{ECO:0000303|PubMed:11389728}.
/FTId=VSP_005449.
VAR_SEQ 1 14 Missing (in isoform 2).
{ECO:0000303|PubMed:11389728,
ECO:0000303|PubMed:9177475}.
/FTId=VSP_005448.
VARIANT 86 86 S -> P (in dbSNP:rs3797799).
/FTId=VAR_031616.
VARIANT 594 594 N -> I (in dbSNP:rs12520455).
/FTId=VAR_051567.
VARIANT 763 763 A -> T (in dbSNP:rs2303138).
/FTId=VAR_012812.
VARIANT 913 913 S -> T (in dbSNP:rs17087233).
/FTId=VAR_051568.
VARIANT 963 963 I -> V (in dbSNP:rs11746232).
/FTId=VAR_031617.
CONFLICT 66 66 D -> V (in Ref. 3; CAB61646/CAB94753).
{ECO:0000305}.
CONFLICT 301 301 S -> L (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 386 386 K -> N (in Ref. 2; AAB66672/AAB66673 and
3; CAB61646/CAB94753). {ECO:0000305}.
CONFLICT 892 892 K -> Q (in Ref. 1; BAA09436).
{ECO:0000305}.
CONFLICT 944 944 F -> L (in Ref. 1; BAA09436).
{ECO:0000305}.
STRAND 165 167 {ECO:0000244|PDB:5MJ6}.
STRAND 170 184 {ECO:0000244|PDB:5MJ6}.
TURN 185 188 {ECO:0000244|PDB:5MJ6}.
STRAND 189 202 {ECO:0000244|PDB:5MJ6}.
STRAND 204 210 {ECO:0000244|PDB:5MJ6}.
STRAND 215 223 {ECO:0000244|PDB:5MJ6}.
TURN 224 226 {ECO:0000244|PDB:5MJ6}.
STRAND 233 237 {ECO:0000244|PDB:5MJ6}.
HELIX 238 240 {ECO:0000244|PDB:5MJ6}.
STRAND 242 251 {ECO:0000244|PDB:5MJ6}.
STRAND 256 266 {ECO:0000244|PDB:5MJ6}.
STRAND 268 280 {ECO:0000244|PDB:5MJ6}.
STRAND 282 284 {ECO:0000244|PDB:5C97}.
STRAND 286 293 {ECO:0000244|PDB:5MJ6}.
TURN 295 298 {ECO:0000244|PDB:5MJ6}.
HELIX 299 302 {ECO:0000244|PDB:5MJ6}.
STRAND 308 310 {ECO:0000244|PDB:4PJ6}.
STRAND 313 322 {ECO:0000244|PDB:5MJ6}.
STRAND 325 331 {ECO:0000244|PDB:5MJ6}.
STRAND 333 338 {ECO:0000244|PDB:5MJ6}.
STRAND 343 348 {ECO:0000244|PDB:5MJ6}.
STRAND 353 355 {ECO:0000244|PDB:4PJ6}.
HELIX 356 358 {ECO:0000244|PDB:5MJ6}.
STRAND 361 364 {ECO:0000244|PDB:5MJ6}.
STRAND 367 373 {ECO:0000244|PDB:5MJ6}.
STRAND 376 382 {ECO:0000244|PDB:5MJ6}.
HELIX 384 390 {ECO:0000244|PDB:5MJ6}.
HELIX 391 408 {ECO:0000244|PDB:5MJ6}.
STRAND 415 424 {ECO:0000244|PDB:5MJ6}.
STRAND 426 430 {ECO:0000244|PDB:5MJ6}.
STRAND 435 439 {ECO:0000244|PDB:5MJ6}.
HELIX 440 442 {ECO:0000244|PDB:5MJ6}.
TURN 447 449 {ECO:0000244|PDB:5MJ6}.
HELIX 452 468 {ECO:0000244|PDB:5MJ6}.
TURN 472 474 {ECO:0000244|PDB:5MJ6}.
STRAND 475 479 {ECO:0000244|PDB:5MJ6}.
HELIX 480 483 {ECO:0000244|PDB:5MJ6}.
HELIX 484 501 {ECO:0000244|PDB:5MJ6}.
HELIX 503 505 {ECO:0000244|PDB:5MJ6}.
HELIX 508 522 {ECO:0000244|PDB:5MJ6}.
STRAND 523 526 {ECO:0000244|PDB:4Z7I}.
HELIX 537 542 {ECO:0000244|PDB:5MJ6}.
HELIX 546 562 {ECO:0000244|PDB:5MJ6}.
HELIX 565 579 {ECO:0000244|PDB:5MJ6}.
STRAND 582 584 {ECO:0000244|PDB:5MJ6}.
HELIX 586 597 {ECO:0000244|PDB:5MJ6}.
STRAND 600 602 {ECO:0000244|PDB:4P8Q}.
HELIX 603 612 {ECO:0000244|PDB:5MJ6}.
STRAND 613 615 {ECO:0000244|PDB:5MJ6}.
STRAND 617 624 {ECO:0000244|PDB:5MJ6}.
STRAND 627 634 {ECO:0000244|PDB:5MJ6}.
STRAND 654 662 {ECO:0000244|PDB:5MJ6}.
STRAND 663 665 {ECO:0000244|PDB:4PJ6}.
STRAND 667 674 {ECO:0000244|PDB:5MJ6}.
STRAND 676 682 {ECO:0000244|PDB:5MJ6}.
STRAND 687 693 {ECO:0000244|PDB:5MJ6}.
HELIX 694 696 {ECO:0000244|PDB:5MJ6}.
STRAND 698 704 {ECO:0000244|PDB:5MJ6}.
HELIX 706 718 {ECO:0000244|PDB:5MJ6}.
HELIX 720 722 {ECO:0000244|PDB:5MJ6}.
HELIX 725 741 {ECO:0000244|PDB:5MJ6}.
STRAND 742 744 {ECO:0000244|PDB:5C97}.
HELIX 746 753 {ECO:0000244|PDB:5MJ6}.
HELIX 754 758 {ECO:0000244|PDB:5MJ6}.
HELIX 762 782 {ECO:0000244|PDB:5MJ6}.
HELIX 785 804 {ECO:0000244|PDB:5MJ6}.
STRAND 808 810 {ECO:0000244|PDB:5MJ6}.
HELIX 814 829 {ECO:0000244|PDB:5MJ6}.
HELIX 835 847 {ECO:0000244|PDB:5MJ6}.
TURN 848 850 {ECO:0000244|PDB:5MJ6}.
TURN 857 859 {ECO:0000244|PDB:5MJ6}.
HELIX 860 867 {ECO:0000244|PDB:5MJ6}.
HELIX 871 881 {ECO:0000244|PDB:5MJ6}.
HELIX 887 897 {ECO:0000244|PDB:5MJ6}.
HELIX 903 915 {ECO:0000244|PDB:5MJ6}.
STRAND 917 919 {ECO:0000244|PDB:4PJ6}.
HELIX 921 923 {ECO:0000244|PDB:5MJ6}.
HELIX 924 933 {ECO:0000244|PDB:5MJ6}.
HELIX 935 947 {ECO:0000244|PDB:5MJ6}.
HELIX 949 955 {ECO:0000244|PDB:5MJ6}.
HELIX 961 969 {ECO:0000244|PDB:5MJ6}.
TURN 970 973 {ECO:0000244|PDB:5MJ6}.
HELIX 977 988 {ECO:0000244|PDB:5MJ6}.
HELIX 992 995 {ECO:0000244|PDB:5MJ6}.
HELIX 998 1024 {ECO:0000244|PDB:5MJ6}.
SEQUENCE 1025 AA; 117349 MW; F84C0EA9D48DC2C0 CRC64;
MEPFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG SRLLVRGLGE
HEMEEDEEDY ESSAKLLGMS FMNRSSGLRN SATGYRQSPD GACSVPSART MVVCAFVIVV
AVSVIMVIYL LPRCTFTKEG CHKKNQSIGL IQPFATNGKL FPWAQIRLPT AVVPLRYELS
LHPNLTSMTF RGSVTISVQA LQVTWNIILH STGHNISRVT FMSAVSSQEK QAEILEYAYH
GQIAIVAPEA LLAGHNYTLK IEYSANISSS YYGFYGFSYT DESNEKKYFA ATQFEPLAAR
SAFPCFDEPA FKATFIIKII RDEQYTALSN MPKKSSVVLD DGLVQDEFSE SVKMSTYLVA
FIVGEMKNLS QDVNGTLVSI YAVPEKIGQV HYALETTVKL LEFFQNYFEI QYPLKKLDLV
AIPDFEAGAM ENWGLLTFRE ETLLYDSNTS SMADRKLVTK IIAHELAHQW FGNLVTMKWW
NDLWLNEGFA TFMEYFSLEK IFKELSSYED FLDARFKTMK KDSLNSSHPI SSSVQSSEQI
EEMFDSLSYF KGSSLLLMLK TYLSEDVFQH AVVLYLHNHS YASIQSDDLW DSFNEVTNQT
LDVKRMMKTW TLQKGFPLVT VQKKGKELFI QQERFFLNMK PEIQPSDTSY LWHIPLSYVT
EGRNYSKYQS VSLLDKKSGV INLTEEVLWV KVNINMNGYY IVHYADDDWE ALIHQLKINP
YVLSDKDRAN LINNIFELAG LGKVPLKRAF DLINYLGNEN HTAPITEALF QTDLIYNLLE
KLGYMDLASR LVTRVFKLLQ NQIQQQTWTD EGTPSMRELR SALLEFACTH NLGNCSTTAM
KLFDDWMASN GTQSLPTDVM TTVFKVGAKT DKGWSFLLGK YISIGSEAEK NKILEALASS
EDVRKLYWLM KSSLNGDNFR TQKLSFIIRT VGRHFPGHLL AWDFVKENWN KLVQKFPLGS
YTIQNIVAGS TYLFSTKTHL SEVQAFFENQ SEATFRLRCV QEALEVIQLN IQWMEKNLKS
LTWWL


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