NALDL_HUMAN
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 03-AUG-2022, entry version 172.
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; 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 GlyGen; Q9UQQ1; 7 sites.
DR iPTMnet; Q9UQQ1; -.
DR PhosphoSitePlus; Q9UQQ1; -.
DR BioMuta; NAALADL1; -.
DR DMDM; 313104139; -.
DR MassIVE; Q9UQQ1; -.
DR PaxDb; Q9UQQ1; -.
DR PeptideAtlas; Q9UQQ1; -.
DR PRIDE; 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; 151 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 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; IEFVSWD; -.
DR OrthoDB; 804230at2759; -.
DR PhylomeDB; Q9UQQ1; -.
DR TreeFam; TF312981; -.
DR PathwayCommons; Q9UQQ1; -.
DR SignaLink; Q9UQQ1; -.
DR BioGRID-ORCS; 10004; 21 hits in 1071 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 137 other tissues.
DR ExpressionAtlas; Q9UQQ1; baseline and differential.
DR Genevisible; Q9UQQ1; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of 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 Gene3D; 1.20.930.40; -; 1.
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; PTHR10404; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
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
