ID   AMPN_CANLF              Reviewed;         975 AA.
AC   P79143; F1PCB5;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   02-SEP-2026, entry version 145.
DE   RecName: Full=Aminopeptidase N {ECO:0000305};
DE            Short=AP-N;
DE            Short=cAPN;
DE            EC=3.4.11.2 {ECO:0000250|UniProtKB:P15144};
DE   AltName: Full=Alanyl aminopeptidase;
DE   AltName: Full=Aminopeptidase M;
DE            Short=AP-M;
DE   AltName: Full=Microsomal aminopeptidase;
DE   AltName: CD_antigen=CD13;
GN   Name=ANPEP;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer;
RX   PubMed=16341006; DOI=10.1038/nature04338;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA   Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA   Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA   Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA   Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA   Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA   Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA   Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA   Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA   Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA   Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA   Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA   Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA   Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA   Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA   Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA   Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA   Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA   Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA   LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA   Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA   Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA   Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA   Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA   Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA   Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA   Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA   Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA   Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA   Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA   Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA   Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA   Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 657-847, FUNCTION (MICROBIAL INFECTION),
RP   INTERACTION WITH CCOV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), AND
RP   IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR CCOV INFECTION (MICROBIAL
RP   INFECTION).
RC   TISSUE=Small intestine;
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).
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. 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   -!- FUNCTION: (Microbial infection) Probable receptor for canine
CC       coronavirus (CCoV). {ECO:0000269|PubMed:8985407}.
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:0000250|UniProtKB:P15144};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P15144};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15144};
CC   -!- SUBUNIT: (Microbial infection) Interacts with CCoV spike glycoprotein.
CC       {ECO:0000269|PubMed:8985407}.
CC   -!- SUBUNIT: Homodimer. Interacts with SLC6A19 (By similarity).
CC       {ECO:0000250|UniProtKB:P15144, ECO:0000250|UniProtKB:P97449}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15144};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:P15144}.
CC       Note=Also found as a soluble form. {ECO:0000250|UniProtKB:P15144}.
CC   -!- DOMAIN: Amino acids 1-191 are essential to mediate susceptibility to
CC       infection with CCV (in canine/human chimeric studies).
CC       {ECO:0000269|PubMed:8985407}.
CC   -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.
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; AAEX03002325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X98239; CAA66895.1; -; mRNA.
DR   RefSeq; NP_001139506.1; NM_001146034.1.
DR   PDB; 7U0L; X-ray; 3.30 A; A=72-975.
DR   PDB; 8YZI; EM; 3.05 A; B/D=36-975.
DR   PDB; 8Z27; EM; 2.86 A; b=36-975.
DR   AlphaFoldDB; P79143; -.
DR   EMDB; EMD-39694; -.
DR   EMDB; EMD-39743; -.
DR   SMR; P79143; -.
DR   FunCoup; P79143; 99.
DR   STRING; 9615.ENSCAFP00000017681; -.
DR   MEROPS; M01.001; -.
DR   GlyCosmos; P79143; 9 sites, No reported glycans.
DR   PaxDb; 9615-ENSCAFP00000017681; -.
DR   Ensembl; ENSCAFT00000019074; ENSCAFP00000017681; ENSCAFG00000012013.
DR   Ensembl; ENSCAFT00805048776; ENSCAFP00805038162; ENSCAFG00805026851.
DR   GeneID; 403913; -.
DR   KEGG; cfa:403913; -.
DR   CTD; 290; -.
DR   VGNC; VGNC:53146; ANPEP.
DR   eggNOG; KOG1046; Eukaryota.
DR   InParanoid; P79143; -.
DR   OMA; EETEYMP; -.
DR   OrthoDB; 510539at2759; -.
DR   Reactome; R-CFA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000805418; Unplaced.
DR   Bgee; ENSCAFG00000012013; Expressed in jejunum and 46 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016285; F:alanyl aminopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0002003; P:angiotensin maturation; IBA:GO_Central.
DR   GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR   CDD; cd09601; M1_APN-Q_like; 1.
DR   FunFam; 2.60.40.1910:FF:000005; Aminopeptidase; 1.
DR   FunFam; 1.25.50.20:FF:000012; Aminopeptidase N; 1.
DR   FunFam; 2.60.40.1730:FF:000012; Aminopeptidase N; 1.
DR   FunFam; 1.10.390.10:FF:000016; Glutamyl aminopeptidase; 1.
DR   Gene3D; 1.25.50.20; -; 1.
DR   Gene3D; 2.60.40.1910; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 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; IPR050344; Peptidase_M1_aminopeptidases.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF172; AMINOPEPTIDASE N; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   PDBsum; 7U0L; -.
DR   PDBsum; 8YZI; -.
DR   PDBsum; 8Z27; -.
PE   1: Evidence at protein level;
KW   3D-structure; Aminopeptidase; Angiogenesis; Cell membrane;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Host cell receptor for virus entry; Host-virus interaction; Hydrolase;
KW   Membrane; Metal-binding; Metalloprotease; Protease; Receptor;
KW   Reference proteome; Signal-anchor; Sulfation; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..975
FT                   /note="Aminopeptidase N"
FT                   /id="PRO_0000095079"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   TRANSMEM        12..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..975
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   REGION          33..74
FT                   /note="Cytosolic Ser/Thr-rich junction"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   REGION          41..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..975
FT                   /note="Metalloprotease"
FT   COMPBIAS        43..59
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        395
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         358..362
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   BINDING         394
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         398
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         417
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   SITE            483
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   MOD_RES         182
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         425
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         430
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   CARBOHYD        533
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   CARBOHYD        580
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   CARBOHYD        633
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   CARBOHYD        689
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   CARBOHYD        747
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        826
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   DISULFID        769..776
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   DISULFID        806..842
FT                   /evidence="ECO:0000250|UniProtKB:P15144"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:7U0L"
FT   TURN            76..78
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          86..97
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          108..121
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          124..129
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:7U0L"
FT   STRAND          141..146
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           154..156
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          158..161
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            163..165
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          168..171
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           175..177
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          181..191
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          194..206
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          209..216
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           221..226
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          237..255
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          257..259
FT                   /evidence="ECO:0007829|PDB:8YZI"
FT   STRAND          265..267
FT                   /evidence="ECO:0007829|PDB:7U0L"
FT   STRAND          268..274
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           276..279
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            283..285
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          288..291
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          294..299
FT                   /evidence="ECO:0007829|PDB:8YZI"
FT   STRAND          308..310
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           312..317
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            318..320
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           321..338
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          348..354
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          356..359
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          363..369
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           370..373
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            377..379
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           382..400
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            402..404
FT                   /evidence="ECO:0007829|PDB:8YZI"
FT   STRAND          405..408
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           410..412
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           413..431
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          433..435
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           437..441
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           442..446
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           447..454
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           458..460
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            465..467
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           471..477
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           480..496
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            497..499
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           500..512
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            513..515
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          516..518
FT                   /evidence="ECO:0007829|PDB:8YZI"
FT   HELIX           520..533
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           543..552
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          557..561
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            563..565
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          567..572
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          575..578
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            586..589
FT                   /evidence="ECO:0007829|PDB:7U0L"
FT   STRAND          593..595
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          597..599
FT                   /evidence="ECO:0007829|PDB:8YZI"
FT   STRAND          607..609
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          611..616
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            618..620
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          628..631
FT                   /evidence="ECO:0007829|PDB:8YZI"
FT   HELIX           632..634
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          639..642
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           644..656
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          658..661
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           663..678
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           684..692
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           693..695
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           700..717
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          718..720
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           723..744
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            745..749
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           755..770
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           774..788
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   STRAND          789..793
FT                   /evidence="ECO:0007829|PDB:7U0L"
FT   TURN            798..800
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           801..811
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           814..826
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           830..840
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           846..857
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            859..861
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           864..876
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           878..890
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           892..895
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           896..900
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            901..903
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           906..912
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            914..916
FT                   /evidence="ECO:0007829|PDB:8YZI"
FT   HELIX           920..932
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   TURN            933..936
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           941..958
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           959..963
FT                   /evidence="ECO:0007829|PDB:8Z27"
FT   HELIX           964..975
FT                   /evidence="ECO:0007829|PDB:8Z27"
SQ   SEQUENCE   975 AA;  110257 MW;  921D2446A2F84725 CRC64;
     MAKGFYISKA LGILAIVLGI AAVSTIIALS VVYAQEKNKN AESSPVSSPV SSPVSSPVSP
     TNPSTTAATT LAQSKPWNHY RLPKTLIPSS YNVTLRPYLT PNSNGLYTFK GSSTVRFTCK
     ESTSMIIIHS KKLNYTNIQG QRVALRGVGG SQAPAIDRTE LVEVTEYLVV HLREPLQVNS
     QYEMDSKFEG ELADDLAGFY RSEYTENGVK KVLATTQMQA ADARKSFPCF DEPAMKATFN
     ITLIHPSNLV ALSNMLPRGP SVPFTEEPNW NVTEFETTPI MSTYLLAYIV SEFKNVQENT
     PSNVLIRIWA RPSAMDQGHG NYALRVTGPI LDFFSRHYDT PYPLNKSDQI ALPDFNAGAM
     ENWGLVTYRE SALLYDPQSS SIGNKERVVT VIAHELAHQW FGNLVTLEWW NDLWLNEGFA
     SYVEYLGADY AEPTWNLKDL IVLNEVYRVM AVDALASSHP LSSPASEVNT PAQISEVFDS
     ISYSKGASVL RMLSSFLTED LFKKGVASYL HTFAYQNTIY LDLWNHLQWA LGNQTAINLP
     YTVNAIMDRW ILQMGFPVVT VDTTTGTLSQ KHFLLDPQSN VTRPSKFNYL WIIPISSVKS
     GTQQAHYWMP DNAKVQNDLF KTTGDEWVLL NLNVTGYYLV NYDQNNWKKI HTQLQTDLSV
     IPVINRAQVI HDTFDLASAQ IVPVTLALNS TLFLNQETEY MPWEAALSSL SYFKLMFDRS
     EVYGPMKNYL RKQVTPLFNH FEKITQNWTD HPQTLTEQYN EINAVSTACT YGVPKCKDLV
     STLFAEWRKN PQNNPIYPNL RSTVYCNAIA QGGEEEWNFV WEQFRNTSLV NEADKLRSAL
     ACSTQVWILN RYLSYTLNPE FIRKQDVIST LSSIASNVIG QSLAWDFIQS NWKKLFEDYG
     TGSFSFSNLI QAVTRRFSTE FELQQLEQFK ANNMDTGFGS GTRALEQALE KTKANIKWVK
     ENKEAVLQWF RENSQ
//