AMPN_PIG
ID AMPN_PIG Reviewed; 963 AA.
AC P15145; Q29242;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 4.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Aminopeptidase N {ECO:0000305};
DE Short=AP-N;
DE Short=pAPN;
DE EC=3.4.11.2 {ECO:0000269|PubMed:8963385};
DE AltName: Full=Alanyl aminopeptidase;
DE AltName: Full=Aminopeptidase M;
DE Short=AP-M;
DE AltName: Full=Microsomal aminopeptidase;
DE AltName: Full=gp130;
DE AltName: CD_antigen=CD13;
GN Name=ANPEP;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION (MICROBIAL INFECTION), IDENTIFICATION
RP OF RECEPTOR FUNCTIONAL DOMAINS FOR TGEV INFECTION, SUBCELLULAR LOCATION,
RP AND TOPOLOGY.
RX PubMed=7913510; DOI=10.1128/jvi.68.8.5216-5224.1994;
RA Delmas B., Gelfi J., Kut E., Sjoestroem H., Noren O., Laude H.;
RT "Determinants essential for the transmissible gastroenteritis virus-
RT receptor interaction reside within a domain of aminopeptidase-N that is
RT distinct from the enzymatic site.";
RL J. Virol. 68:5216-5224(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-294.
RX PubMed=2568950; DOI=10.1016/0014-5793(89)81470-x;
RA Olsen J., Sjoestroem H., Noren O.;
RT "Cloning of the pig aminopeptidase N gene. Identification of possible
RT regulatory elements and the exon distribution in relation to the membrane-
RT spanning region.";
RL FEBS Lett. 251:275-281(1989).
RN [3]
RP PROTEIN SEQUENCE OF 2-40.
RX PubMed=1977382; DOI=10.1042/bj2710147;
RA See H., Reithmeier R.A.F.;
RT "Identification and characterization of the major stilbene-
RT disulphonate- and concanavalin A-binding protein of the porcine renal
RT brush-border membrane as aminopeptidase N.";
RL Biochem. J. 271:147-155(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-144.
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
RN [5]
RP CHARACTERIZATION OF TGEV RECEPTOR FUNCTION.
RX PubMed=1350661; DOI=10.1038/357417a0;
RA Delmas B., Gelfi J., L'Haridon R., Vogel L.K., Sjostrom H., Noren O.,
RA Laude H.;
RT "Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus
RT TGEV.";
RL Nature 357:417-420(1992).
RN [6]
RP CHARACTERIZATION OF PRCOV RECEPTOR FUNCTION.
RX PubMed=7911642; DOI=10.1007/978-1-4615-2996-5_45;
RA Delmas B., Gelfi J., Sjostrom H., Noren O., Laude H.;
RT "Further characterization of aminopeptidase-N as a receptor for
RT coronaviruses.";
RL Adv. Exp. Med. Biol. 342:293-298(1993).
RN [7]
RP CATALYTIC ACTIVITY.
RX PubMed=8963385; DOI=10.1007/bf02349634;
RA Terashima H., Bunnett N.W.;
RT "Purification and characterization of aminopeptidase M from muscle and
RT mucosa of the pig intestine.";
RL J. Gastroenterol. 30:696-704(1995).
RN [8]
RP FUNCTION (MICROBIAL INFECTION), AND IDENTIFICATION OF RECEPTOR FUNCTIONAL
RP DOMAINS FOR TGEV INFECTION.
RX PubMed=8985407; DOI=10.1128/jvi.71.1.734-737.1997;
RA Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B.;
RT "Interspecies aminopeptidase-N chimeras reveal species-specific receptor
RT recognition by canine coronavirus, feline infectious peritonitis virus, and
RT transmissible gastroenteritis virus.";
RL J. Virol. 71:734-737(1997).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), AND IDENTIFICATION OF RECEPTOR FUNCTIONAL
RP DOMAINS FOR TGEV INFECTION.
RX PubMed=9634079; DOI=10.1099/0022-1317-79-6-1387;
RA Hegyi A., Kolb A.F.;
RT "Characterization of determinants involved in the feline infectious
RT peritonitis virus receptor function of feline aminopeptidase N.";
RL J. Gen. Virol. 79:1387-1391(1998).
RN [10]
RP SUBUNIT.
RX PubMed=6119979; DOI=10.1042/bj1970573;
RA Benajiba A., Maroux S.;
RT "Subunit structured of pig small-intestinal brush-border aminopeptidase
RT N.";
RL Biochem. J. 197:573-580(1981).
RN [11]
RP SULFATION.
RX PubMed=3121301; DOI=10.1002/j.1460-2075.1987.tb02592.x;
RA Danielsen E.M.;
RT "Tyrosine sulfation, a post-translational modification of microvillar
RT enzymes in the small intestinal enterocyte.";
RL EMBO J. 6:2891-2896(1987).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 36-963 IN COMPLEX WITH PORCINE
RP RESPIRATORY CORONAVIRUS S PROTEIN, SUBUNIT, COFACTOR, ZINC-BINDING SITES,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-82; ASN-124; ASN-229; ASN-237;
RP ASN-314; ASN-328; ASN-506; ASN-622; ASN-646 AND ASN-736.
RX PubMed=22876187; DOI=10.1371/journal.ppat.1002859;
RA Reguera J., Santiago C., Mudgal G., Ordono D., Enjuanes L.,
RA Casasnovas J.M.;
RT "Structural bases of coronavirus attachment to host aminopeptidase N and
RT its inhibition by neutralizing antibodies.";
RL PLoS Pathog. 8:E1002859-E1002859(2012).
CC -!- FUNCTION: Broad specificity aminopeptidase which plays a role in the
CC final digestion of peptides generated from hydrolysis of proteins by
CC gastric and pancreatic proteases. Also involved in the processing of
CC various peptides including peptide hormones, such as angiotensin III
CC and IV, neuropeptides, and chemokines. May also be involved the
CC cleavage of peptides bound to major histocompatibility complex class II
CC molecules of antigen presenting cells. May have a role in angiogenesis
CC and promote cholesterol crystallization (By similarity). It is able to
CC degrade Leu-enkephalin and Met-enkephalin but not cholecystokinin CCK8,
CC neuromedin C (GRP-10), somatostatin-14, substance P and vasoactive
CC intestinal peptide (PubMed:8963385). May have a role in amino acid
CC transport by acting as binding partner of amino acid transporter
CC SLC6A19 and regulating its activity (By similarity).
CC {ECO:0000250|UniProtKB:P15144, ECO:0000250|UniProtKB:P97449,
CC ECO:0000269|PubMed:8963385}.
CC -!- FUNCTION: (Microbial infection) In case of porcine transmissible
CC gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus
CC (PRCoV) infections, serves as a receptor for TGEV and PRCoV spike
CC glycoprotein in a species-specific manner. {ECO:0000269|PubMed:1350661,
CC ECO:0000269|PubMed:7911642, ECO:0000269|PubMed:7913510,
CC ECO:0000269|PubMed:8985407, ECO:0000269|PubMed:9634079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000269|PubMed:8963385};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:22876187};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22876187};
CC -!- SUBUNIT: Homodimer. Interacts with SLC6A19 (By similarity).
CC {ECO:0000250|UniProtKB:P97449, ECO:0000269|PubMed:22876187,
CC ECO:0000269|PubMed:6119979}.
CC -!- SUBUNIT: (Microbial infection) Interacts with TGEV and PRCoV spike
CC glycoprotein. {ECO:0000269|PubMed:22876187, ECO:0000269|PubMed:7913510,
CC ECO:0000269|PubMed:8985407, ECO:0000269|PubMed:9634079}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7913510};
CC Single-pass type II membrane protein {ECO:0000305|PubMed:7913510}.
CC Note=Also found as a soluble form. {ECO:0000250|UniProtKB:P15144}.
CC -!- PTM: Sulfated. {ECO:0000269|PubMed:3121301}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P15144}.
CC -!- PTM: May undergo proteolysis and give rise to a soluble form.
CC {ECO:0000250|UniProtKB:P15144}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; Z29522; CAA82641.1; -; mRNA.
DR EMBL; X16088; CAA34216.1; ALT_TERM; Genomic_DNA.
DR EMBL; F14846; CAA23291.1; -; mRNA.
DR PIR; A53984; A53984.
DR RefSeq; NP_999442.1; NM_214277.1.
DR PDB; 4F5C; X-ray; 3.20 A; A/B=36-963.
DR PDB; 4FKE; X-ray; 1.85 A; A=62-963.
DR PDB; 4FKH; X-ray; 2.05 A; A=62-963.
DR PDB; 4FKK; X-ray; 2.60 A; A=62-963.
DR PDB; 4HOM; X-ray; 1.90 A; A=63-963.
DR PDB; 4NAQ; X-ray; 2.10 A; A=64-963.
DR PDB; 4NZ8; X-ray; 2.00 A; A=64-963.
DR PDB; 4OU3; X-ray; 1.95 A; A=63-963.
DR PDB; 5LDS; X-ray; 2.00 A; A/B/C/D=36-963.
DR PDB; 5LG6; X-ray; 2.50 A; A/B=36-963.
DR PDB; 5Z65; X-ray; 2.65 A; A=62-963.
DR PDB; 6BUY; X-ray; 2.10 A; A=63-963.
DR PDB; 6BV0; X-ray; 1.86 A; A=63-963.
DR PDB; 6BV1; X-ray; 2.00 A; A=63-963.
DR PDB; 6BV2; X-ray; 2.14 A; A=63-963.
DR PDB; 6BV3; X-ray; 2.20 A; A=63-963.
DR PDB; 6BV4; X-ray; 2.02 A; A=63-963.
DR PDBsum; 4F5C; -.
DR PDBsum; 4FKE; -.
DR PDBsum; 4FKH; -.
DR PDBsum; 4FKK; -.
DR PDBsum; 4HOM; -.
DR PDBsum; 4NAQ; -.
DR PDBsum; 4NZ8; -.
DR PDBsum; 4OU3; -.
DR PDBsum; 5LDS; -.
DR PDBsum; 5LG6; -.
DR PDBsum; 5Z65; -.
DR PDBsum; 6BUY; -.
DR PDBsum; 6BV0; -.
DR PDBsum; 6BV1; -.
DR PDBsum; 6BV2; -.
DR PDBsum; 6BV3; -.
DR PDBsum; 6BV4; -.
DR AlphaFoldDB; P15145; -.
DR SMR; P15145; -.
DR STRING; 9823.ENSSSCP00000029051; -.
DR BindingDB; P15145; -.
DR ChEMBL; CHEMBL2590; -.
DR DrugCentral; P15145; -.
DR MEROPS; M01.001; -.
DR iPTMnet; P15145; -.
DR PaxDb; P15145; -.
DR PeptideAtlas; P15145; -.
DR PRIDE; P15145; -.
DR ABCD; P15145; 31 sequenced antibodies.
DR GeneID; 397520; -.
DR KEGG; ssc:397520; -.
DR CTD; 290; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; P15145; -.
DR OrthoDB; 110058at2759; -.
DR SABIO-RK; P15145; -.
DR PRO; PR:P15145; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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: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; 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 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; Angiogenesis; Cell membrane;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
KW Host-virus interaction; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Receptor; Reference proteome; Signal-anchor;
KW Sulfation; Transmembrane; Transmembrane helix; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1977382"
FT CHAIN 2..963
FT /note="Aminopeptidase N"
FT /id="PRO_0000095083"
FT TOPO_DOM 2..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:7913510"
FT TRANSMEM 9..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..963
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7913510"
FT REGION 33..64
FT /note="Cytosolic Ser/Thr-rich junction"
FT REGION 65..963
FT /note="Metalloprotease"
FT REGION 717..813
FT /note="Interaction with TGEV spike glycoprotein"
FT /evidence="ECO:0000269|PubMed:7913510,
FT ECO:0000269|PubMed:8985407, ECO:0000269|PubMed:9634079"
FT ACT_SITE 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 347..351
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22876187,
FT ECO:0007744|PDB:4F5C"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22876187,
FT ECO:0007744|PDB:4F5C"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22876187,
FT ECO:0007744|PDB:4F5C"
FT SITE 472
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT MOD_RES 171
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22876187,
FT ECO:0007744|PDB:4F5C"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22876187,
FT ECO:0007744|PDB:4F5C"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22876187,
FT ECO:0007744|PDB:4F5C"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22876187,
FT ECO:0007744|PDB:4F5C"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22876187,
FT ECO:0007744|PDB:4F5C"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22876187,
FT ECO:0007744|PDB:4F5C"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22876187,
FT ECO:0007744|PDB:4F5C"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22876187,
FT ECO:0007744|PDB:4F5C"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22876187,
FT ECO:0007744|PDB:4F5C"
FT CARBOHYD 736
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22876187,
FT ECO:0007744|PDB:4F5C"
FT DISULFID 758..765
FT /evidence="ECO:0000269|PubMed:22876187"
FT DISULFID 795..831
FT /evidence="ECO:0000269|PubMed:22876187"
FT CONFLICT 82
FT /note="N -> F (in Ref. 1; CAA82641 and 2; CAA34216)"
FT /evidence="ECO:0000305"
FT CONFLICT 107..108
FT /note="LL -> FI (in Ref. 4; CAA23291)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="E -> G (in Ref. 4; CAA23291)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="T -> N (in Ref. 4; CAA23291)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="S -> F (in Ref. 4; CAA23291)"
FT /evidence="ECO:0000305"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 74..87
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 98..111
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:4FKK"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:4FKE"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 170..180
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 183..195
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:4FKE"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:4F5C"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:5LDS"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:4F5C"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:4FKE"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 310..326
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 332..341
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:5LDS"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:4FKE"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 371..386
FT /evidence="ECO:0007829|PDB:4FKE"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:4FKE"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 402..420
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:5LDS"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 435..442
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 460..464
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 469..486
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 488..502
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 509..521
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:5LDS"
FT HELIX 532..540
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 546..550
FT /evidence="ECO:0007829|PDB:4FKE"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 556..561
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 564..567
FT /evidence="ECO:0007829|PDB:4F5C"
FT TURN 575..578
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 607..609
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 617..620
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 628..631
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 633..645
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 647..649
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 652..667
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 673..678
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 679..685
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 689..706
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 712..733
FT /evidence="ECO:0007829|PDB:4FKE"
FT TURN 734..738
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 744..759
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 763..777
FT /evidence="ECO:0007829|PDB:4FKE"
FT TURN 787..789
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 790..800
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 803..815
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 819..829
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 835..844
FT /evidence="ECO:0007829|PDB:4FKE"
FT TURN 848..850
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 853..855
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 856..865
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 869..880
FT /evidence="ECO:0007829|PDB:4FKE"
FT TURN 882..886
FT /evidence="ECO:0007829|PDB:4FKE"
FT STRAND 887..890
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 895..903
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 909..919
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 920..922
FT /evidence="ECO:0007829|PDB:4FKK"
FT STRAND 923..925
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 928..930
FT /evidence="ECO:0007829|PDB:4FKE"
FT HELIX 933..962
FT /evidence="ECO:0007829|PDB:4FKE"
SQ SEQUENCE 963 AA; 108832 MW; 0C55FDD2CE1F3E10 CRC64;
MAKGFYISKA LGILGILLGV AAVATIIALS VVYAQEKNKN AEHVPQAPTS PTITTTAAIT
LDQSKPWNRY RLPTTLLPDS YNVTLRPYLT PNADGLYIFK GKSIVRLLCQ EPTDVIIIHS
KKLNYTTQGH MVVLRGVGDS QVPEIDRTEL VELTEYLVVH LKGSLQPGHM YEMESEFQGE
LADDLAGFYR SEYMEGNVKK VLATTQMQST DARKSFPCFD EPAMKATFNI TLIHPNNLTA
LSNMPPKGSS TPLAEDPNWS VTEFETTPVM STYLLAYIVS EFQSVNETAQ NGVLIRIWAR
PNAIAEGHGM YALNVTGPIL NFFANHYNTS YPLPKSDQIA LPDFNAGAME NWGLVTYREN
ALLFDPQSSS ISNKERVVTV IAHELAHQWF GNLVTLAWWN DLWLNEGFAS YVEYLGADHA
EPTWNLKDLI VPGDVYRVMA VDALASSHPL TTPAEEVNTP AQISEMFDSI SYSKGASVIR
MLSNFLTEDL FKEGLASYLH AFAYQNTTYL DLWEHLQKAV DAQTSIRLPD TVRAIMDRWT
LQMGFPVITV DTKTGNISQK HFLLDSESNV TRSSAFDYLW IVPISSIKNG VMQDHYWLRD
VSQAQNDLFK TASDDWVLLN VNVTGYFQVN YDEDNWRMIQ HQLQTNLSVI PVINRAQVIY
DSFNLATAHM VPVTLALDNT LFLNGEKEYM PWQAALSSLS YFSLMFDRSE VYGPMKKYLR
KQVEPLFQHF ETLTKNWTER PENLMDQYSE INAISTACSN GLPQCENLAK TLFDQWMSDP
ENNPIHPNLR STIYCNAIAQ GGQDQWDFAW GQLQQAQLVN EADKLRSALA CSNEVWLLNR
YLGYTLNPDL IRKQDATSTI NSIASNVIGQ PLAWDFVQSN WKKLFQDYGG GSFSFSNLIQ
GVTRRFSSEF ELQQLEQFKK NNMDVGFGSG TRALEQALEK TKANIKWVKE NKEVVLNWFI
EHS
