ID   NALDL_HUMAN             Reviewed;         740 AA.
AC   Q9UQQ1; C9J8A1; C9J964; C9JL35; C9JSN0; O43176;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   24-JAN-2024, entry version 180.
DE   RecName: Full=Aminopeptidase NAALADL1 {ECO:0000305};
DE            EC=3.4.11.- {ECO:0000269|PubMed:25752612};
DE   AltName: Full=100 kDa ileum brush border membrane protein {ECO:0000303|PubMed:9388249};
DE            Short=I100 {ECO:0000303|PubMed:9388249};
DE   AltName: Full=Ileal dipeptidylpeptidase;
DE   AltName: Full=N-acetylated-alpha-linked acidic dipeptidase-like protein;
DE            Short=NAALADase L {ECO:0000303|PubMed:10085079};
GN   Name=NAALADL1;
GN   Synonyms=NAALADASEL, NAALADL {ECO:0000303|PubMed:10085079};
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] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8).
RC   TISSUE=Small intestine;
RX   PubMed=10085079; DOI=10.1074/jbc.274.13.8470;
RA   Pangalos M.N., Neefs J.-M., Somers M., Verhasselt P., Bekkers M.,
RA   van der Helm L., Fraiponts E., Ashton D., Gordon R.D.;
RT   "Isolation and expression of novel human glutamate carboxypeptidases with
RT   N-acetylated alpha-linked acidic dipeptidase and dipeptidyl peptidase IV
RT   activity.";
RL   J. Biol. Chem. 274:8470-8483(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 419-740, AND TISSUE SPECIFICITY.
RC   TISSUE=Ileum;
RX   PubMed=9388249; DOI=10.1074/jbc.272.49.31006;
RA   Shneider B.L., Thevananther S., Moyer M.S., Walters H.C., Rinaldo P.,
RA   Devarajan P., Sun A.Q., Dawson P.A., Ananthanarayanan M.;
RT   "Cloning and characterization of a novel peptidase from rat and human
RT   ileum.";
RL   J. Biol. Chem. 272:31006-31015(1997).
RN   [4] {ECO:0007744|PDB:4TWE}
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 28-740 IN COMPLEX WITH CALCIUM
RP   AND ZINC, CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, COFACTOR,
RP   SUBUNIT, GLYCOSYLATION AT ASN-136; ASN-299; ASN-334; ASN-345; ASN-451 AND
RP   ASN-492, DISULFIDE BOND, MUTAGENESIS OF GLU-416, ACTIVE SITE, TISSUE
RP   SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=25752612; DOI=10.1074/jbc.m114.628149;
RA   Tykvart J., Barinka C., Svoboda M., Navratil V., Soucek R., Hubalek M.,
RA   Hradilek M., Sacha P., Lubkowski J., Konvalinka J.;
RT   "Structural and biochemical characterization of a novel aminopeptidase from
RT   human intestine.";
RL   J. Biol. Chem. 290:11321-11336(2015).
CC   -!- FUNCTION: Aminopeptidase with broad substrate specificity. Has lower
CC       activity with substrates that have Asp or Glu in the P2' position, or
CC       Pro in the P3' position. Lacks activity with substrates that have both
CC       Pro in the P3' position and Asp or Glu in the P2' position
CC       (PubMed:25752612). Lacks carboxypeptidase activity. Lacks dipeptidyl-
CC       peptidase IV type activity (PubMed:25752612).
CC       {ECO:0000269|PubMed:25752612}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:25752612};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:25752612};
CC   -!- ACTIVITY REGULATION: Inhibited by bestatin.
CC       {ECO:0000269|PubMed:25752612}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25752612}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:O54697}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:O54697}. Note=Ileal brush border membrane.
CC       {ECO:0000250|UniProtKB:O54697}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=1;
CC         IsoId=Q9UQQ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UQQ1-2; Sequence=VSP_005343;
CC       Name=3;
CC         IsoId=Q9UQQ1-3; Sequence=VSP_005344;
CC       Name=4;
CC         IsoId=Q9UQQ1-4; Sequence=VSP_005345;
CC       Name=5;
CC         IsoId=Q9UQQ1-5; Sequence=VSP_005346, VSP_005347;
CC       Name=6;
CC         IsoId=Q9UQQ1-6; Sequence=VSP_005348, VSP_005349;
CC       Name=7;
CC         IsoId=Q9UQQ1-7; Sequence=VSP_005350, VSP_005351;
CC       Name=8;
CC         IsoId=Q9UQQ1-8; Sequence=VSP_005352, VSP_005353;
CC   -!- TISSUE SPECIFICITY: Detected in small intestine (at protein level)
CC       (PubMed:25752612). Detected in ileum (PubMed:9388249). Detected in
CC       small intestine, spleen and testis. Isoform 2 and isoform 3 are found
CC       in the small intestine and colon (PubMed:10085079).
CC       {ECO:0000269|PubMed:10085079, ECO:0000269|PubMed:25752612,
CC       ECO:0000269|PubMed:9388249}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O54697}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally shown to have aminopeptidase IV activity
CC       (PubMed:10085079). Later characterization was unable to detect any
CC       significant aminopeptidase IV activity (PubMed:25752612).
CC       {ECO:0000269|PubMed:10085079, ECO:0000269|PubMed:25752612}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB87645.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ012371; CAB39968.1; -; mRNA.
DR   EMBL; AP003068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF010141; AAB87645.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS31604.1; -. [Q9UQQ1-1]
DR   RefSeq; NP_005459.2; NM_005468.2. [Q9UQQ1-1]
DR   RefSeq; XP_011543012.1; XM_011544710.2.
DR   PDB; 4TWE; X-ray; 1.75 A; A/B=28-740.
DR   PDBsum; 4TWE; -.
DR   AlphaFoldDB; Q9UQQ1; -.
DR   SMR; Q9UQQ1; -.
DR   BioGRID; 115322; 241.
DR   IntAct; Q9UQQ1; 2.
DR   STRING; 9606.ENSP00000351484; -.
DR   MEROPS; M28.011; -.
DR   GlyCosmos; Q9UQQ1; 7 sites, No reported glycans.
DR   GlyGen; Q9UQQ1; 7 sites.
DR   iPTMnet; Q9UQQ1; -.
DR   PhosphoSitePlus; Q9UQQ1; -.
DR   BioMuta; NAALADL1; -.
DR   DMDM; 313104139; -.
DR   MassIVE; Q9UQQ1; -.
DR   PaxDb; 9606-ENSP00000351484; -.
DR   PeptideAtlas; Q9UQQ1; -.
DR   ProteomicsDB; 85563; -. [Q9UQQ1-1]
DR   ProteomicsDB; 85564; -. [Q9UQQ1-2]
DR   ProteomicsDB; 85565; -. [Q9UQQ1-3]
DR   ProteomicsDB; 85566; -. [Q9UQQ1-4]
DR   ProteomicsDB; 85567; -. [Q9UQQ1-5]
DR   ProteomicsDB; 85568; -. [Q9UQQ1-6]
DR   ProteomicsDB; 85569; -. [Q9UQQ1-7]
DR   ProteomicsDB; 85570; -. [Q9UQQ1-8]
DR   Antibodypedia; 58724; 164 antibodies from 16 providers.
DR   DNASU; 10004; -.
DR   Ensembl; ENST00000340252.8; ENSP00000344244.4; ENSG00000168060.16. [Q9UQQ1-4]
DR   Ensembl; ENST00000355721.7; ENSP00000347955.3; ENSG00000168060.16. [Q9UQQ1-2]
DR   Ensembl; ENST00000358658.8; ENSP00000351484.3; ENSG00000168060.16. [Q9UQQ1-1]
DR   GeneID; 10004; -.
DR   KEGG; hsa:10004; -.
DR   MANE-Select; ENST00000358658.8; ENSP00000351484.3; NM_005468.3; NP_005459.2.
DR   UCSC; uc001ocn.4; human. [Q9UQQ1-1]
DR   AGR; HGNC:23536; -.
DR   CTD; 10004; -.
DR   DisGeNET; 10004; -.
DR   GeneCards; NAALADL1; -.
DR   HGNC; HGNC:23536; NAALADL1.
DR   HPA; ENSG00000168060; Tissue enriched (intestine).
DR   MIM; 602640; gene.
DR   neXtProt; NX_Q9UQQ1; -.
DR   OpenTargets; ENSG00000168060; -.
DR   PharmGKB; PA134867982; -.
DR   VEuPathDB; HostDB:ENSG00000168060; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   GeneTree; ENSGT01030000234598; -.
DR   InParanoid; Q9UQQ1; -.
DR   OMA; TEWMEEY; -.
DR   OrthoDB; 2428249at2759; -.
DR   PhylomeDB; Q9UQQ1; -.
DR   TreeFam; TF312981; -.
DR   PathwayCommons; Q9UQQ1; -.
DR   SignaLink; Q9UQQ1; -.
DR   BioGRID-ORCS; 10004; 24 hits in 1151 CRISPR screens.
DR   ChiTaRS; NAALADL1; human.
DR   GenomeRNAi; 10004; -.
DR   Pharos; Q9UQQ1; Tbio.
DR   PRO; PR:Q9UQQ1; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9UQQ1; Protein.
DR   Bgee; ENSG00000168060; Expressed in ileal mucosa and 139 other cell types or tissues.
DR   ExpressionAtlas; Q9UQQ1; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; NAS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0043171; P:peptide catabolic process; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd08022; M28_PSMA_like; 1.
DR   CDD; cd02121; PA_GCPII_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   InterPro; IPR039373; Peptidase_M28B.
DR   InterPro; IPR007365; TFR-like_dimer_dom.
DR   InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR   PANTHER; PTHR10404:SF50; AMINOPEPTIDASE NAALADL1; 1.
DR   PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   Pfam; PF04253; TFR_dimer; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   Genevisible; Q9UQQ1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Aminopeptidase; Calcium; Cell membrane;
KW   Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..740
FT                   /note="Aminopeptidase NAALADL1"
FT                   /id="PRO_0000174123"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..740
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        416
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000305|PubMed:25752612"
FT   BINDING         258
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   BINDING         261
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   BINDING         368
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   BINDING         378
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   BINDING         378
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   BINDING         417
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   BINDING         425
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   BINDING         428
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   BINDING         445
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   BINDING         545
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   CARBOHYD        451
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   DISULFID        296..313
FT                   /evidence="ECO:0000269|PubMed:25752612,
FT                   ECO:0007744|PDB:4TWE"
FT   VAR_SEQ         161..201
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10085079"
FT                   /id="VSP_005343"
FT   VAR_SEQ         296..330
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10085079"
FT                   /id="VSP_005344"
FT   VAR_SEQ         359
FT                   /note="P -> PGEPSSCCLHPRPLLCSGCRCPHPALPLPPPSPAPPAHLSLSSGSLP
FT                   LFLWP (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10085079"
FT                   /id="VSP_005345"
FT   VAR_SEQ         502..543
FT                   /note="PSLGSLGAGSDYAPFVHFLGISSMDIAYTYDRSKTSARIYPT -> PRARLQ
FT                   PGSPPTTQPLTPLTMWTSFWTRASAAIRLWPGQRGV (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:10085079"
FT                   /id="VSP_005348"
FT   VAR_SEQ         502..522
FT                   /note="PSLGSLGAGSDYAPFVHFLGI -> PRLQQPSGCGPDSGECDSPAQ (in
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10085079"
FT                   /id="VSP_005346"
FT   VAR_SEQ         523..740
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10085079"
FT                   /id="VSP_005347"
FT   VAR_SEQ         544..740
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:10085079"
FT                   /id="VSP_005349"
FT   VAR_SEQ         562..579
FT                   /note="FSSHQAVARTAGSVILRL -> FEEGDKGHPETRTGEAED (in isoform
FT                   7)"
FT                   /evidence="ECO:0000303|PubMed:10085079"
FT                   /id="VSP_005350"
FT   VAR_SEQ         580..740
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:10085079"
FT                   /id="VSP_005351"
FT   VAR_SEQ         619..635
FT                   /note="GPLVTAVEKFEAEAAAL -> GMHSPDPEVWGALHPHD (in isoform
FT                   8)"
FT                   /evidence="ECO:0000303|PubMed:10085079"
FT                   /id="VSP_005352"
FT   VAR_SEQ         636..740
FT                   /note="Missing (in isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:10085079"
FT                   /id="VSP_005353"
FT   VARIANT         2
FT                   /note="Q -> H (in dbSNP:rs35422506)"
FT                   /id="VAR_057155"
FT   VARIANT         398
FT                   /note="K -> T (in dbSNP:rs12223986)"
FT                   /id="VAR_057156"
FT   VARIANT         611
FT                   /note="L -> V (in dbSNP:rs36053340)"
FT                   /id="VAR_057157"
FT   MUTAGEN         416
FT                   /note="E->A: Loss of enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:25752612"
FT   CONFLICT        420..424
FT                   /note="LIGST -> SPGLQ (in Ref. 3; AAB87645)"
FT                   /evidence="ECO:0000305"
FT   HELIX           42..51
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           54..64
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           74..88
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          95..108
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          116..120
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          137..143
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          163..165
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           171..179
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          188..196
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           198..206
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   TURN            207..209
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          212..216
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           219..222
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           229..231
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          235..238
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          251..254
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           272..274
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          283..285
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           288..295
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          300..302
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           305..307
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          310..313
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          319..321
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          325..327
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          332..337
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          340..353
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          356..368
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          372..374
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   TURN            376..379
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           380..398
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          405..414
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   TURN            417..419
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           421..429
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           431..437
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          438..443
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          447..449
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          451..458
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           460..462
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           463..471
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          476..480
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           483..487
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   TURN            488..490
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          491..495
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   TURN            496..498
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          499..502
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          509..511
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           513..518
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          524..530
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   TURN            533..535
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   TURN            542..545
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           551..556
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           563..581
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           589..591
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           592..613
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           619..643
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           649..661
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           662..666
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          675..677
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   TURN            681..683
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   STRAND          688..690
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           694..703
FT                   /evidence="ECO:0007829|PDB:4TWE"
FT   HELIX           711..734
FT                   /evidence="ECO:0007829|PDB:4TWE"
SQ   SEQUENCE   740 AA;  80558 MW;  018D59835F2C48AC CRC64;
     MQWTKVLGLG LGAAALLGLG IILGHFAIPK KANSLAPQDL DLEILETVMG QLDAHRIREN
     LRELSREPHL ASSPRDEDLV QLLLQRWKDP ESGLDSAEAS TYEVLLSFPS QEQPNVVDIV
     GPTGGIIHSC HRTEENVTGE QGGPDVVQPY AAYAPSGTPQ GLLVYANRGA EEDFKELQTQ
     GIKLEGTIAL TRYGGVGRGA KAVNAAKHGV AGVLVYTDPA DINDGLSSPD ETFPNSWYLP
     PSGVERGSYY EYFGDPLTPY LPAVPSSFRV DLANVSGFPP IPTQPIGFQD ARDLLCNLNG
     TLAPATWQGA LGCHYRLGPG FRPDGDFPAD SQVNVSVYNR LELRNSSNVL GIIRGAVEPD
     RYVLYGNHRD SWVHGAVDPS SGTAVLLELS RVLGTLLKKG TWRPRRSIVF ASWGAEEFGL
     IGSTEFTEEF FNKLQERTVA YINVDISVFA NATLRVQGTP PVQSVVFSAT KEIRSPGPGD
     LSIYDNWIRY FNRSSPVYGL VPSLGSLGAG SDYAPFVHFL GISSMDIAYT YDRSKTSARI
     YPTYHTAFDT FDYVDKFLDP GFSSHQAVAR TAGSVILRLS DSFFLPLKVS DYSETLRSFL
     QAAQQDLGAL LEQHSISLGP LVTAVEKFEA EAAALGQRIS TLQKGSPDPL QVRMLNDQLM
     LLERTFLNPR AFPEERYYSH VLWAPRTGSV VTFPGLSNAC SRARDTASGS EAWAEVQRQL
     SIVVTALEGA AATLRPVADL
//