SIGL7_HUMAN
ID SIGL7_HUMAN Reviewed; 467 AA.
AC Q9Y286; Q9NZQ1; Q9UJ86; Q9UJ87; Q9Y502;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Sialic acid-binding Ig-like lectin 7;
DE Short=Siglec-7;
DE AltName: Full=Adhesion inhibitory receptor molecule 1;
DE Short=AIRM-1;
DE AltName: Full=CDw328;
DE AltName: Full=D-siglec;
DE AltName: Full=QA79 membrane protein;
DE AltName: Full=p75;
DE AltName: CD_antigen=CD328;
DE Flags: Precursor;
GN Name=SIGLEC7; Synonyms=AIRM1;
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] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RX PubMed=10567377; DOI=10.1074/jbc.274.48.34089;
RA Nicoll G., Ni J., Liu D., Klenerman P., Munday J., Dubock S., Mattei M.-G.,
RA Crocker P.R.;
RT "Identification and characterization of a novel siglec, siglec-7, expressed
RT by human natural killer cells and monocytes.";
RL J. Biol. Chem. 274:34089-34095(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), PHOSPHORYLATION, AND
RP INTERACTION WITH PTPN6.
RC TISSUE=Lymphoid tissue;
RX PubMed=10499918; DOI=10.1084/jem.190.6.793;
RA Falco M., Biassoni R., Bottino C., Vitale M., Sivori S., Augugliaro R.,
RA Moretta L., Moretta A.;
RT "Identification and molecular cloning of p75/AIRM1, a novel member of the
RT sialoadhesin family that functions as an inhibitory receptor in human
RT natural killer cells.";
RL J. Exp. Med. 190:793-802(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Dendritic cell;
RA Zhang W., Wan T., Cao X.;
RT "Characterization of a novel siglec from dendritic cells.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10764831; DOI=10.1093/glycob/10.4.431;
RA Angata T., Varki A.;
RT "Siglec-7: a sialic acid-binding lectin of the immunoglobulin
RT superfamily.";
RL Glycobiology 10:431-438(2000).
RN [5]
RP FUNCTION.
RX PubMed=10611343; DOI=10.1073/pnas.96.26.15091;
RA Vitale C., Romagnani C., Falco M., Ponte M., Vitale M., Moretta A.,
RA Bacigalupo A., Moretta L., Mingari M.C.;
RT "Engagement of p75/AIRM1 or CD33 inhibits the proliferation of normal or
RT leukemic myeloid cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15091-15096(1999).
RN [6]
RP DISIALOGANGLIOSIDE-BINDING.
RX PubMed=11389909; DOI=10.1016/s0014-5793(01)02476-0;
RA Ito A., Handa K., Withers D.A., Satoh M., Hakomori S.;
RT "Binding specificity of siglec7 to disialogangliosides of renal cell
RT carcinoma: possible role of disialogangliosides in tumor progression.";
RL FEBS Lett. 498:116-120(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 18-144, DISULFIDE BOND, AND
RP GLYCOSYLATION AT ASN-105.
RX PubMed=12438315; DOI=10.1074/jbc.m210602200;
RA Alphey M.S., Attrill H., Crocker P.R., van Aalten D.M.;
RT "High resolution crystal structures of Siglec-7. Insights into ligand
RT specificity in the Siglec family.";
RL J. Biol. Chem. 278:3372-3377(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 19-150, AND DISULFIDE BOND.
RX PubMed=14747738; DOI=10.1107/s0907444903028439;
RA Dimasi N., Moretta A., Moretta L., Biassoni R., Mariuzza R.A.;
RT "Structure of the saccharide-binding domain of the human natural killer
RT cell inhibitory receptor p75/AIRM1.";
RL Acta Crystallogr. D 60:401-403(2004).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 18-144 IN COMPLEX WITH SIALYLATED
RP LIGAND, GLYCOSYLATION AT ASN-105, AND DISULFIDE BOND.
RX PubMed=16623661; DOI=10.1042/bj20060103;
RA Attrill H., Takazawa H., Witt S., Kelm S., Isecke R., Brossmer R., Ando T.,
RA Ishida H., Kiso M., Crocker P.R., van Aalten D.M.;
RT "The structure of siglec-7 in complex with sialosides: leads for rational
RT structure-based inhibitor design.";
RL Biochem. J. 397:271-278(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 18-144 IN COMPLEX WITH
RP ALPHA(2,8)-DISIALYLATED LIGAND GT1B, GLYCOSYLATION AT ASN-105, AND
RP DISULFIDE BOND.
RX PubMed=16895906; DOI=10.1074/jbc.m601714200;
RA Attrill H., Imamura A., Sharma R.S., Kiso M., Crocker P.R.,
RA van Aalten D.M.;
RT "Siglec-7 undergoes a major conformational change when complexed with the
RT alpha(2,8)-disialylganglioside GT1b.";
RL J. Biol. Chem. 281:32774-32783(2006).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] PRO-215.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Putative adhesion molecule that mediates sialic-acid
CC dependent binding to cells. Preferentially binds to alpha-2,3- and
CC alpha-2,6-linked sialic acid. Also binds disialogangliosides
CC (disialogalactosyl globoside, disialyl lactotetraosylceramide and
CC disialyl GalNAc lactotetraoslylceramide). The sialic acid recognition
CC site may be masked by cis interactions with sialic acids on the same
CC cell surface. In the immune response, may act as an inhibitory receptor
CC upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic
CC phosphatase(s) via their SH2 domain(s) that block signal transduction
CC through dephosphorylation of signaling molecules. Mediates inhibition
CC of natural killer cells cytotoxicity. May play a role in hemopoiesis.
CC Inhibits differentiation of CD34+ cell precursors towards
CC myelomonocytic cell lineage and proliferation of leukemic myeloid cells
CC (in vitro). {ECO:0000269|PubMed:10611343}.
CC -!- SUBUNIT: Interacts with PTPN6/SHP-1 upon phosphorylation.
CC {ECO:0000269|PubMed:10499918, ECO:0000269|PubMed:16623661,
CC ECO:0000269|PubMed:16895906}.
CC -!- INTERACTION:
CC Q9Y286; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-2801178, EBI-12188413;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=AIRM-1b;
CC IsoId=Q9Y286-1; Sequence=Displayed;
CC Name=2; Synonyms=AIRM-2;
CC IsoId=Q9Y286-2; Sequence=VSP_002555;
CC Name=3; Synonyms=AIRM-3;
CC IsoId=Q9Y286-3; Sequence=VSP_002556, VSP_002558;
CC Name=4;
CC IsoId=Q9Y286-4; Sequence=VSP_002557, VSP_002558;
CC -!- TISSUE SPECIFICITY: Predominantly expressed by resting and activated
CC natural killer cells and at lower levels by granulocytes and monocytes.
CC High expression found in placenta, liver, lung, spleen, and peripheral
CC blood leukocytes.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000269|PubMed:10499918}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF44346.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Siglec-7;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_274";
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DR EMBL; AF170485; AAF12759.1; -; mRNA.
DR EMBL; AJ007395; CAB46011.1; -; mRNA.
DR EMBL; AJ130710; CAB51126.1; -; mRNA.
DR EMBL; AJ130711; CAB51127.1; -; mRNA.
DR EMBL; AJ130712; CAB51128.1; -; mRNA.
DR EMBL; AJ130713; CAB51129.1; -; mRNA.
DR EMBL; AF178981; AAF44346.1; ALT_FRAME; mRNA.
DR EMBL; AF193441; AAF06790.1; -; mRNA.
DR CCDS; CCDS12826.1; -. [Q9Y286-1]
DR CCDS; CCDS42601.1; -. [Q9Y286-2]
DR CCDS; CCDS62771.1; -. [Q9Y286-4]
DR RefSeq; NP_001264130.1; NM_001277201.1. [Q9Y286-4]
DR RefSeq; NP_055200.1; NM_014385.3. [Q9Y286-1]
DR RefSeq; NP_057627.2; NM_016543.3. [Q9Y286-2]
DR PDB; 1NKO; X-ray; 1.45 A; A=19-150.
DR PDB; 1O7S; X-ray; 1.75 A; A=18-144.
DR PDB; 1O7V; X-ray; 1.90 A; A=18-144.
DR PDB; 2DF3; X-ray; 1.90 A; A=18-144.
DR PDB; 2G5R; X-ray; 1.60 A; A=18-144.
DR PDB; 2HRL; X-ray; 1.85 A; A=18-144.
DR PDBsum; 1NKO; -.
DR PDBsum; 1O7S; -.
DR PDBsum; 1O7V; -.
DR PDBsum; 2DF3; -.
DR PDBsum; 2G5R; -.
DR PDBsum; 2HRL; -.
DR AlphaFoldDB; Q9Y286; -.
DR SMR; Q9Y286; -.
DR BioGRID; 117967; 14.
DR IntAct; Q9Y286; 8.
DR STRING; 9606.ENSP00000323328; -.
DR BindingDB; Q9Y286; -.
DR ChEMBL; CHEMBL3603730; -.
DR DrugBank; DB03740; N-acetyl-alpha-D-glucosamine.
DR UniLectin; Q9Y286; -.
DR GlyConnect; 569; 16 N-Linked glycans.
DR GlyGen; Q9Y286; 9 sites, 31 N-linked glycans (1 site).
DR iPTMnet; Q9Y286; -.
DR PhosphoSitePlus; Q9Y286; -.
DR BioMuta; SIGLEC7; -.
DR DMDM; 25009269; -.
DR jPOST; Q9Y286; -.
DR MassIVE; Q9Y286; -.
DR PaxDb; Q9Y286; -.
DR PeptideAtlas; Q9Y286; -.
DR PRIDE; Q9Y286; -.
DR ProteomicsDB; 85695; -. [Q9Y286-1]
DR ProteomicsDB; 85696; -. [Q9Y286-2]
DR ProteomicsDB; 85697; -. [Q9Y286-3]
DR ProteomicsDB; 85698; -. [Q9Y286-4]
DR Antibodypedia; 18998; 830 antibodies from 35 providers.
DR CPTC; Q9Y286; 1 antibody.
DR DNASU; 27036; -.
DR Ensembl; ENST00000305628.7; ENSP00000306757.6; ENSG00000168995.13. [Q9Y286-2]
DR Ensembl; ENST00000317643.10; ENSP00000323328.6; ENSG00000168995.13. [Q9Y286-1]
DR Ensembl; ENST00000536156.5; ENSP00000437609.1; ENSG00000168995.13. [Q9Y286-3]
DR Ensembl; ENST00000600577.1; ENSP00000472529.1; ENSG00000168995.13. [Q9Y286-4]
DR GeneID; 27036; -.
DR KEGG; hsa:27036; -.
DR MANE-Select; ENST00000317643.10; ENSP00000323328.6; NM_014385.4; NP_055200.1.
DR UCSC; uc002pvv.1; human. [Q9Y286-1]
DR CTD; 27036; -.
DR DisGeNET; 27036; -.
DR GeneCards; SIGLEC7; -.
DR HGNC; HGNC:10876; SIGLEC7.
DR HPA; ENSG00000168995; Tissue enhanced (lymphoid).
DR MIM; 604410; gene.
DR neXtProt; NX_Q9Y286; -.
DR OpenTargets; ENSG00000168995; -.
DR PharmGKB; PA35777; -.
DR VEuPathDB; HostDB:ENSG00000168995; -.
DR eggNOG; ENOG502S41V; Eukaryota.
DR GeneTree; ENSGT01040000240469; -.
DR HOGENOM; CLU_024444_6_1_1; -.
DR InParanoid; Q9Y286; -.
DR OMA; CFQNLTC; -.
DR OrthoDB; 324083at2759; -.
DR PhylomeDB; Q9Y286; -.
DR TreeFam; TF332441; -.
DR PathwayCommons; Q9Y286; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q9Y286; -.
DR BioGRID-ORCS; 27036; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; SIGLEC7; human.
DR EvolutionaryTrace; Q9Y286; -.
DR GeneWiki; SIGLEC7; -.
DR GenomeRNAi; 27036; -.
DR Pharos; Q9Y286; Tchem.
DR PRO; PR:Q9Y286; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y286; protein.
DR Bgee; ENSG00000168995; Expressed in granulocyte and 129 other tissues.
DR ExpressionAtlas; Q9Y286; baseline and differential.
DR Genevisible; Q9Y286; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
DR GO; GO:0033691; F:sialic acid binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Lectin; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..467
FT /note="Sialic acid-binding Ig-like lectin 7"
FT /id="PRO_0000014947"
FT TOPO_DOM 19..353
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..122
FT /note="Ig-like V-type"
FT DOMAIN 150..233
FT /note="Ig-like C2-type 1"
FT DOMAIN 240..336
FT /note="Ig-like C2-type 2"
FT REGION 401..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 435..440
FT /note="ITIM motif"
FT COMPBIAS 415..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000269|PubMed:16623661,
FT ECO:0000269|PubMed:16895906"
FT BINDING 131..135
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000269|PubMed:12438315,
FT ECO:0000269|PubMed:16623661, ECO:0000269|PubMed:16895906"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16623661,
FT ECO:0000269|PubMed:16895906"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:12438315, ECO:0000269|PubMed:14747738,
FT ECO:0000269|PubMed:16623661, ECO:0000269|PubMed:16895906"
FT DISULFID 168..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 276..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 145..238
FT /note="ALTHRPNILIPGTLESGCFQNLTCSVPWACEQGTPPMISWMGTSVSPLHPST
FT TRSSVLTLIPQPQHHGTSLTCQVTLPGAGVTTNRTIQLNVSY -> D (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:10499918,
FT ECO:0000303|PubMed:10764831, ECO:0000303|Ref.3"
FT /id="VSP_002555"
FT VAR_SEQ 145
FT /note="A -> E (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10499918"
FT /id="VSP_002556"
FT VAR_SEQ 145
FT /note="A -> G (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10499918"
FT /id="VSP_002557"
FT VAR_SEQ 146..467
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10499918"
FT /id="VSP_002558"
FT VARIANT 215
FT /note="L -> P (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035523"
FT CONFLICT 42
FT /note="V -> A (in Ref. 4; AAF44346)"
FT /evidence="ECO:0000305"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1NKO"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:1NKO"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1NKO"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1NKO"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1NKO"
FT TURN 54..58
FT /evidence="ECO:0007829|PDB:1NKO"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:1NKO"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2HRL"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1O7V"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1NKO"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:2HRL"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1NKO"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1NKO"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1NKO"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1NKO"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1NKO"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1NKO"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:1NKO"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:1NKO"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1NKO"
SQ SEQUENCE 467 AA; 51143 MW; 8AFE44462B001F52 CRC64;
MLLLLLLPLL WGRERVEGQK SNRKDYSLTM QSSVTVQEGM CVHVRCSFSY PVDSQTDSDP
VHGYWFRAGN DISWKAPVAT NNPAWAVQEE TRDRFHLLGD PQTKNCTLSI RDARMSDAGR
YFFRMEKGNI KWNYKYDQLS VNVTALTHRP NILIPGTLES GCFQNLTCSV PWACEQGTPP
MISWMGTSVS PLHPSTTRSS VLTLIPQPQH HGTSLTCQVT LPGAGVTTNR TIQLNVSYPP
QNLTVTVFQG EGTASTALGN SSSLSVLEGQ SLRLVCAVDS NPPARLSWTW RSLTLYPSQP
SNPLVLELQV HLGDEGEFTC RAQNSLGSQH VSLNLSLQQE YTGKMRPVSG VLLGAVGGAG
ATALVFLSFC VIFIVVRSCR KKSARPAADV GDIGMKDANT IRGSASQGNL TESWADDNPR
HHGLAAHSSG EEREIQYAPL SFHKGEPQDL SGQEATNNEY SEIKIPK
