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Aminopeptidase N (AP-N) (pAPN) (EC 3.4.11.2) (Alanyl aminopeptidase) (Aminopeptidase M) (AP-M) (Microsomal aminopeptidase) (gp130) (CD antigen CD13)

 AMPN_PIG                Reviewed;         963 AA.
P15145; Q29242;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
06-FEB-2013, sequence version 4.
05-DEC-2018, entry version 150.
RecName: Full=Aminopeptidase N {ECO:0000305};
Short=AP-N;
Short=pAPN;
EC=3.4.11.2 {ECO:0000269|PubMed:8963385};
AltName: Full=Alanyl aminopeptidase;
AltName: Full=Aminopeptidase M;
Short=AP-M;
AltName: Full=Microsomal aminopeptidase;
AltName: Full=gp130;
AltName: CD_antigen=CD13;
Name=ANPEP;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION (MICROBIAL INFECTION),
IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR TGEV INFECTION,
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=7913510;
Delmas B., Gelfi J., Kut E., Sjoestroem H., Noren O., Laude H.;
"Determinants essential for the transmissible gastroenteritis virus-
receptor interaction reside within a domain of aminopeptidase-N that
is distinct from the enzymatic site.";
J. Virol. 68:5216-5224(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-294.
PubMed=2568950; DOI=10.1016/0014-5793(89)81470-X;
Olsen J., Sjoestroem H., Noren O.;
"Cloning of the pig aminopeptidase N gene. Identification of possible
regulatory elements and the exon distribution in relation to the
membrane-spanning region.";
FEBS Lett. 251:275-281(1989).
[3]
PROTEIN SEQUENCE OF 2-40.
PubMed=1977382; DOI=10.1042/bj2710147;
See H., Reithmeier R.A.F.;
"Identification and characterization of the major stilbene-
disulphonate- and concanavalin A-binding protein of the porcine renal
brush-border membrane as aminopeptidase N.";
Biochem. J. 271:147-155(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-144.
TISSUE=Small intestine;
PubMed=8672129; DOI=10.1007/s003359900153;
Winteroe A.K., Fredholm M., Davies W.;
"Evaluation and characterization of a porcine small intestine cDNA
library: analysis of 839 clones.";
Mamm. Genome 7:509-517(1996).
[5]
CHARACTERIZATION OF TGEV RECEPTOR FUNCTION.
PubMed=1350661; DOI=10.1038/357417a0;
Delmas B., Gelfi J., L'Haridon R., Vogel L.K., Sjostrom H., Noren O.,
Laude H.;
"Aminopeptidase N is a major receptor for the entero-pathogenic
coronavirus TGEV.";
Nature 357:417-420(1992).
[6]
CHARACTERIZATION OF PRCOV RECEPTOR FUNCTION.
PubMed=7911642;
Delmas B., Gelfi J., Sjostrom H., Noren O., Laude H.;
"Further characterization of aminopeptidase-N as a receptor for
coronaviruses.";
Adv. Exp. Med. Biol. 342:293-298(1993).
[7]
CATALYTIC ACTIVITY.
PubMed=8963385; DOI=10.1007/BF02349634;
Terashima H., Bunnett N.W.;
"Purification and characterization of aminopeptidase M from muscle and
mucosa of the pig intestine.";
J. Gastroenterol. 30:696-704(1995).
[8]
FUNCTION (MICROBIAL INFECTION), AND IDENTIFICATION OF RECEPTOR
FUNCTIONAL DOMAINS FOR TGEV INFECTION.
PubMed=8985407;
Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B.;
"Interspecies aminopeptidase-N chimeras reveal species-specific
receptor recognition by canine coronavirus, feline infectious
peritonitis virus, and transmissible gastroenteritis virus.";
J. Virol. 71:734-737(1997).
[9]
FUNCTION (MICROBIAL INFECTION), AND IDENTIFICATION OF RECEPTOR
FUNCTIONAL DOMAINS FOR TGEV INFECTION.
PubMed=9634079; DOI=10.1099/0022-1317-79-6-1387;
Hegyi A., Kolb A.F.;
"Characterization of determinants involved in the feline infectious
peritonitis virus receptor function of feline aminopeptidase N.";
J. Gen. Virol. 79:1387-1391(1998).
[10]
SUBUNIT.
PubMed=6119979; DOI=10.1042/bj1970573;
Benajiba A., Maroux S.;
"Subunit structured of pig small-intestinal brush-border
aminopeptidase N.";
Biochem. J. 197:573-580(1981).
[11]
SULFATION.
PubMed=3121301;
Danielsen E.M.;
"Tyrosine sulfation, a post-translational modification of microvillar
enzymes in the small intestinal enterocyte.";
EMBO J. 6:2891-2896(1987).
[12]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 36-963 IN COMPLEX WITH
PORCINE RESPIRATORY CORONAVIRUS S PROTEIN, SUBUNIT, COFACTOR,
ZINC-BINDING SITES, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-82;
ASN-124; ASN-229; ASN-237; ASN-314; ASN-328; ASN-506; ASN-622; ASN-646
AND ASN-736.
PubMed=22876187; DOI=10.1371/journal.ppat.1002859;
Reguera J., Santiago C., Mudgal G., Ordono D., Enjuanes L.,
Casasnovas J.M.;
"Structural bases of coronavirus attachment to host aminopeptidase N
and its inhibition by neutralizing antibodies.";
PLoS Pathog. 8:E1002859-E1002859(2012).
-!- FUNCTION: Broad specificity aminopeptidase which plays a role in
the final digestion of peptides generated from hydrolysis of
proteins by gastric and pancreatic proteases. Also involved in the
processing of various peptides including peptide hormones, such as
angiotensin III and IV, neuropeptides, and chemokines. May also be
involved the cleavage of peptides bound to major
histocompatibility complex class II molecules of antigen
presenting cells. May have a role in angiogenesis and promote
cholesterol crystallization (By similarity). It is able to degrade
Leu-enkephalin and Met-enkephalin but not cholecystokinin CCK8,
neuromedin C (GRP-10), somatostatin-14, substance P and vasoactive
intestinal peptide (PubMed:8963385).
{ECO:0000250|UniProtKB:P15144, ECO:0000269|PubMed:8963385}.
-!- FUNCTION: (Microbial infection) In case of porcine transmissible
gastroenteritis coronavirus (TGEV) and porcine respiratory
coronavirus (PRCoV) infections, serves as a receptor for TGEV and
PRCoV spike glycoprotein in a species-specific manner.
{ECO:0000269|PubMed:1350661, ECO:0000269|PubMed:7911642,
ECO:0000269|PubMed:7913510, ECO:0000269|PubMed:8985407,
ECO:0000269|PubMed:9634079}.
-!- CATALYTIC ACTIVITY:
Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
peptide, amide or arylamide. Xaa is preferably Ala, but may be
most amino acids including Pro (slow action). When a terminal
hydrophobic residue is followed by a prolyl residue, the two may
be released as an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
Evidence={ECO:0000269|PubMed:8963385};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:22876187};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22876187};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22876187,
ECO:0000269|PubMed:6119979}.
-!- SUBUNIT: (Microbial infection) Interacts with TGEV and PRCoV spike
glycoprotein. {ECO:0000269|PubMed:22876187,
ECO:0000269|PubMed:7913510, ECO:0000269|PubMed:8985407,
ECO:0000269|PubMed:9634079}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7913510};
Single-pass type II membrane protein {ECO:0000305|PubMed:7913510}.
Note=Also found as a soluble form. {ECO:0000250|UniProtKB:P15144}.
-!- PTM: Sulfated. {ECO:0000269|PubMed:3121301}.
-!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P15144}.
-!- PTM: May undergo proteolysis and give rise to a soluble form.
{ECO:0000250|UniProtKB:P15144}.
-!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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EMBL; Z29522; CAA82641.1; -; mRNA.
EMBL; X16088; CAA34216.1; ALT_TERM; Genomic_DNA.
EMBL; F14846; CAA23291.1; -; mRNA.
PIR; A53984; A53984.
RefSeq; NP_999442.1; NM_214277.1.
UniGene; Ssc.820; -.
PDB; 4F5C; X-ray; 3.20 A; A/B=36-963.
PDB; 4FKE; X-ray; 1.85 A; A=62-963.
PDB; 4FKH; X-ray; 2.05 A; A=62-963.
PDB; 4FKK; X-ray; 2.60 A; A=62-963.
PDB; 4HOM; X-ray; 1.90 A; A=63-963.
PDB; 4NAQ; X-ray; 2.10 A; A=64-963.
PDB; 4NZ8; X-ray; 2.00 A; A=64-963.
PDB; 4OU3; X-ray; 1.95 A; A=63-963.
PDB; 5LDS; X-ray; 2.00 A; A/B/C/D=36-963.
PDB; 5LG6; X-ray; 2.50 A; A/B=36-963.
PDB; 6BUY; X-ray; 2.10 A; A=63-963.
PDB; 6BV0; X-ray; 1.86 A; A=63-963.
PDB; 6BV1; X-ray; 2.00 A; A=63-963.
PDB; 6BV2; X-ray; 2.14 A; A=63-963.
PDB; 6BV3; X-ray; 2.20 A; A=63-963.
PDB; 6BV4; X-ray; 2.02 A; A=63-963.
PDBsum; 4F5C; -.
PDBsum; 4FKE; -.
PDBsum; 4FKH; -.
PDBsum; 4FKK; -.
PDBsum; 4HOM; -.
PDBsum; 4NAQ; -.
PDBsum; 4NZ8; -.
PDBsum; 4OU3; -.
PDBsum; 5LDS; -.
PDBsum; 5LG6; -.
PDBsum; 6BUY; -.
PDBsum; 6BV0; -.
PDBsum; 6BV1; -.
PDBsum; 6BV2; -.
PDBsum; 6BV3; -.
PDBsum; 6BV4; -.
SMR; P15145; -.
STRING; 9823.ENSSSCP00000029051; -.
BindingDB; P15145; -.
ChEMBL; CHEMBL2590; -.
MEROPS; M01.001; -.
iPTMnet; P15145; -.
PaxDb; P15145; -.
PeptideAtlas; P15145; -.
PRIDE; P15145; -.
GeneID; 397520; -.
KEGG; ssc:397520; -.
CTD; 290; -.
eggNOG; KOG1046; Eukaryota.
eggNOG; COG0308; LUCA.
HOGENOM; HOG000106482; -.
HOVERGEN; HBG006616; -.
InParanoid; P15145; -.
KO; K11140; -.
PMAP-CutDB; P15145; -.
PRO; PR:P15145; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
GO; GO:0042277; F:peptide binding; IBA:GO_Central.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
GO; GO:0006508; P:proteolysis; IBA:GO_Central.
CDD; cd09601; M1_APN_2; 1.
InterPro; IPR024571; ERAP1-like_C_dom.
InterPro; IPR034016; M1_APN-typ.
InterPro; IPR001930; Peptidase_M1.
InterPro; IPR014782; Peptidase_M1_N.
PANTHER; PTHR11533; PTHR11533; 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; Aminopeptidase; Angiogenesis; Cell membrane;
Complete proteome; Developmental protein; Differentiation;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction; Hydrolase;
Membrane; Metal-binding; Metalloprotease; Protease; Receptor;
Reference proteome; Signal-anchor; Sulfation; Transmembrane;
Transmembrane helix; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1977382}.
CHAIN 2 963 Aminopeptidase N.
/FTId=PRO_0000095083.
TOPO_DOM 2 8 Cytoplasmic.
{ECO:0000305|PubMed:7913510}.
TRANSMEM 9 32 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 33 963 Extracellular.
{ECO:0000269|PubMed:7913510}.
REGION 33 64 Cytosolic Ser/Thr-rich junction.
REGION 65 963 Metalloprotease.
REGION 347 351 Substrate binding.
{ECO:0000250|UniProtKB:P15144}.
REGION 717 813 Interaction with TGEV spike glycoprotein.
{ECO:0000269|PubMed:7913510,
ECO:0000269|PubMed:8985407,
ECO:0000269|PubMed:9634079}.
ACT_SITE 384 384 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 383 383 Zinc; catalytic. {ECO:0000244|PDB:4F5C,
ECO:0000269|PubMed:22876187}.
METAL 387 387 Zinc; catalytic. {ECO:0000244|PDB:4F5C,
ECO:0000269|PubMed:22876187}.
METAL 406 406 Zinc; catalytic. {ECO:0000244|PDB:4F5C,
ECO:0000269|PubMed:22876187}.
SITE 472 472 Transition state stabilizer.
{ECO:0000250|UniProtKB:P15144}.
MOD_RES 171 171 Sulfotyrosine. {ECO:0000255}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4F5C,
ECO:0000269|PubMed:22876187}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4F5C,
ECO:0000269|PubMed:22876187}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4F5C,
ECO:0000269|PubMed:22876187}.
CARBOHYD 237 237 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4F5C,
ECO:0000269|PubMed:22876187}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 286 286 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 314 314 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4F5C,
ECO:0000269|PubMed:22876187}.
CARBOHYD 328 328 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4F5C,
ECO:0000269|PubMed:22876187}.
CARBOHYD 506 506 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4F5C,
ECO:0000269|PubMed:22876187}.
CARBOHYD 556 556 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 569 569 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 622 622 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4F5C,
ECO:0000269|PubMed:22876187}.
CARBOHYD 646 646 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4F5C,
ECO:0000269|PubMed:22876187}.
CARBOHYD 736 736 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4F5C,
ECO:0000269|PubMed:22876187}.
DISULFID 758 765 {ECO:0000269|PubMed:22876187}.
DISULFID 795 831 {ECO:0000269|PubMed:22876187}.
CONFLICT 82 82 N -> F (in Ref. 1; CAA82641 and 2;
CAA34216). {ECO:0000305}.
CONFLICT 107 108 LL -> FI (in Ref. 4; CAA23291).
{ECO:0000305}.
CONFLICT 111 111 E -> G (in Ref. 4; CAA23291).
{ECO:0000305}.
CONFLICT 126 126 T -> N (in Ref. 4; CAA23291).
{ECO:0000305}.
CONFLICT 140 140 S -> F (in Ref. 4; CAA23291).
{ECO:0000305}.
HELIX 66 68 {ECO:0000244|PDB:4FKE}.
STRAND 69 71 {ECO:0000244|PDB:4FKE}.
STRAND 74 87 {ECO:0000244|PDB:4FKE}.
STRAND 93 95 {ECO:0000244|PDB:4FKE}.
STRAND 98 111 {ECO:0000244|PDB:4FKE}.
STRAND 113 119 {ECO:0000244|PDB:4FKE}.
STRAND 122 125 {ECO:0000244|PDB:4FKK}.
STRAND 128 131 {ECO:0000244|PDB:4FKE}.
STRAND 133 137 {ECO:0000244|PDB:4FKE}.
STRAND 145 151 {ECO:0000244|PDB:4FKE}.
TURN 152 155 {ECO:0000244|PDB:4FKE}.
STRAND 156 165 {ECO:0000244|PDB:4FKE}.
STRAND 170 180 {ECO:0000244|PDB:4FKE}.
STRAND 183 195 {ECO:0000244|PDB:4FKE}.
STRAND 198 206 {ECO:0000244|PDB:4FKE}.
TURN 208 211 {ECO:0000244|PDB:4FKE}.
HELIX 212 214 {ECO:0000244|PDB:4FKE}.
STRAND 221 224 {ECO:0000244|PDB:4F5C}.
STRAND 226 235 {ECO:0000244|PDB:4FKE}.
STRAND 238 244 {ECO:0000244|PDB:4FKE}.
STRAND 246 249 {ECO:0000244|PDB:4FKE}.
STRAND 251 253 {ECO:0000244|PDB:5LDS}.
STRAND 254 256 {ECO:0000244|PDB:4F5C}.
STRAND 259 264 {ECO:0000244|PDB:4FKE}.
HELIX 272 274 {ECO:0000244|PDB:4FKE}.
STRAND 277 281 {ECO:0000244|PDB:4FKE}.
STRAND 283 288 {ECO:0000244|PDB:4FKE}.
STRAND 294 299 {ECO:0000244|PDB:4FKE}.
HELIX 301 305 {ECO:0000244|PDB:4FKE}.
TURN 306 309 {ECO:0000244|PDB:4FKE}.
HELIX 310 326 {ECO:0000244|PDB:4FKE}.
STRAND 332 341 {ECO:0000244|PDB:4FKE}.
STRAND 345 349 {ECO:0000244|PDB:5LDS}.
STRAND 354 358 {ECO:0000244|PDB:4FKE}.
HELIX 359 362 {ECO:0000244|PDB:4FKE}.
TURN 366 368 {ECO:0000244|PDB:4FKE}.
HELIX 371 386 {ECO:0000244|PDB:4FKE}.
TURN 387 389 {ECO:0000244|PDB:4FKE}.
TURN 391 393 {ECO:0000244|PDB:4FKE}.
STRAND 394 398 {ECO:0000244|PDB:4FKE}.
HELIX 399 401 {ECO:0000244|PDB:4FKE}.
HELIX 402 420 {ECO:0000244|PDB:4FKE}.
HELIX 422 424 {ECO:0000244|PDB:5LDS}.
HELIX 426 429 {ECO:0000244|PDB:4FKE}.
HELIX 430 433 {ECO:0000244|PDB:4FKE}.
HELIX 435 442 {ECO:0000244|PDB:4FKE}.
HELIX 454 456 {ECO:0000244|PDB:4FKE}.
HELIX 460 464 {ECO:0000244|PDB:4FKE}.
HELIX 469 486 {ECO:0000244|PDB:4FKE}.
HELIX 488 502 {ECO:0000244|PDB:4FKE}.
STRAND 505 507 {ECO:0000244|PDB:4FKE}.
HELIX 509 521 {ECO:0000244|PDB:4FKE}.
STRAND 524 526 {ECO:0000244|PDB:5LDS}.
HELIX 532 540 {ECO:0000244|PDB:4FKE}.
STRAND 546 550 {ECO:0000244|PDB:4FKE}.
TURN 552 554 {ECO:0000244|PDB:4FKE}.
STRAND 556 561 {ECO:0000244|PDB:4FKE}.
STRAND 564 567 {ECO:0000244|PDB:4F5C}.
TURN 575 578 {ECO:0000244|PDB:4FKE}.
STRAND 582 584 {ECO:0000244|PDB:4FKE}.
STRAND 586 588 {ECO:0000244|PDB:4FKE}.
STRAND 596 598 {ECO:0000244|PDB:4FKE}.
STRAND 602 605 {ECO:0000244|PDB:4FKE}.
HELIX 607 609 {ECO:0000244|PDB:4FKE}.
STRAND 617 620 {ECO:0000244|PDB:4FKE}.
HELIX 621 623 {ECO:0000244|PDB:4FKE}.
STRAND 628 631 {ECO:0000244|PDB:4FKE}.
HELIX 633 645 {ECO:0000244|PDB:4FKE}.
HELIX 647 649 {ECO:0000244|PDB:4FKE}.
HELIX 652 667 {ECO:0000244|PDB:4FKE}.
HELIX 673 678 {ECO:0000244|PDB:4FKE}.
HELIX 679 685 {ECO:0000244|PDB:4FKE}.
HELIX 689 706 {ECO:0000244|PDB:4FKE}.
HELIX 712 733 {ECO:0000244|PDB:4FKE}.
TURN 734 738 {ECO:0000244|PDB:4FKE}.
HELIX 744 759 {ECO:0000244|PDB:4FKE}.
HELIX 763 777 {ECO:0000244|PDB:4FKE}.
TURN 787 789 {ECO:0000244|PDB:4FKE}.
HELIX 790 800 {ECO:0000244|PDB:4FKE}.
HELIX 803 815 {ECO:0000244|PDB:4FKE}.
HELIX 819 829 {ECO:0000244|PDB:4FKE}.
HELIX 835 844 {ECO:0000244|PDB:4FKE}.
TURN 848 850 {ECO:0000244|PDB:4FKE}.
HELIX 853 855 {ECO:0000244|PDB:4FKE}.
HELIX 856 865 {ECO:0000244|PDB:4FKE}.
HELIX 869 880 {ECO:0000244|PDB:4FKE}.
TURN 882 886 {ECO:0000244|PDB:4FKE}.
STRAND 887 890 {ECO:0000244|PDB:4FKE}.
HELIX 895 903 {ECO:0000244|PDB:4FKE}.
HELIX 909 919 {ECO:0000244|PDB:4FKE}.
HELIX 920 922 {ECO:0000244|PDB:4FKK}.
STRAND 923 925 {ECO:0000244|PDB:4FKE}.
HELIX 928 930 {ECO:0000244|PDB:4FKE}.
HELIX 933 962 {ECO:0000244|PDB:4FKE}.
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


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