SN_MOUSE
ID SN_MOUSE Reviewed; 1695 AA.
AC Q62230; D3YVZ3; D3YVZ4; O55216; Q62228; Q62229;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Sialoadhesin;
DE AltName: Full=Sheep erythrocyte receptor;
DE Short=SER;
DE AltName: Full=Sialic acid-binding Ig-like lectin 1;
DE Short=Siglec-1;
DE AltName: CD_antigen=CD169;
DE Flags: Precursor;
GN Name=Siglec1; Synonyms=Sa, Sn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND PARTIAL PROTEIN
RP SEQUENCE.
RC STRAIN=C57BL/6J; TISSUE=Macrophage;
RX PubMed=7925291; DOI=10.1002/j.1460-2075.1994.tb06771.x;
RA Crocker P.R., Mucklow S., Boukson V., McWilliam A., Willis A.C., Gordon S.,
RA Milon G., Kelm S., Bradfield P.;
RT "Sialoadhesin, a macrophage sialic acid binding receptor for haemopoietic
RT cells with 17 immunoglobulin-like domains.";
RL EMBO J. 13:4490-4503(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9383289; DOI=10.1007/s003359900615;
RA Mucklow S., Gordon S., Crocker P.R.;
RT "Characterization of the mouse sialoadhesin gene, Sn.";
RL Mamm. Genome 8:934-937(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP CHARACTERIZATION.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=2050106; DOI=10.1002/j.1460-2075.1991.tb07689.x;
RA Crocker P.R.;
RT "Purification and properties of sialoadhesin, a sialic acid-binding
RT receptor of murine tissue macrophages.";
RL EMBO J. 10:1661-1669(1991).
RN [5]
RP SIALIC ACID-BINDING.
RX PubMed=7533044; DOI=10.1016/s0960-9822(00)00220-7;
RA Kelm S., Pelz A., Schauer R., Filbin M.T., Tang S., de Bellard M.E.,
RA Schnaar R.L., Mahoney J.A., Hartnell A., Bradfield P., Crocker P.R.;
RT "Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family
RT of sialic acid-dependent adhesion molecules of the immunoglobulin
RT superfamily.";
RL Curr. Biol. 4:965-972(1994).
RN [6]
RP INTERACTION WITH SPN.
RX PubMed=11238599; DOI=10.4049/jimmunol.166.6.3637;
RA van den Berg T.K., Nath D., Ziltener H.J., Vestweber D., Fukuda M.,
RA van Die I., Crocker P.R.;
RT "CD43 functions as a T cell counterreceptor for the macrophage adhesion
RT receptor sialoadhesin (Siglec-1).";
RL J. Immunol. 166:3637-3640(2001).
RN [7]
RP FUNCTION, INTERACTION WITH CLEC10A, AND TISSUE SPECIFICITY.
RX PubMed=15364954; DOI=10.1074/jbc.m409300200;
RA Kumamoto Y., Higashi N., Denda-Nagai K., Tsuiji M., Sato K., Crocker P.R.,
RA Irimura T.;
RT "Identification of sialoadhesin as a dominant lymph node counter-receptor
RT for mouse macrophage galactose-type C-type lectin 1.";
RL J. Biol. Chem. 279:49274-49280(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 20-138 IN COMPLEX WITH
RP 3'SIALYLLACTOSE, AND DISULFIDE BOND.
RX PubMed=9660955; DOI=10.1016/s1097-2765(00)80071-4;
RA May A.P., Robinson R.C., Vinson M., Crocker P.R., Jones E.Y.;
RT "Crystal structure of the N-terminal domain of sialoadhesin in complex with
RT 3' sialyllactose at 1.85 A resolution.";
RL Mol. Cell 1:719-728(1998).
RN [10]
RP STRUCTURE BY NMR OF 20-138, AND MUTAGENESIS OF TRP-21 AND ARG-116.
RX PubMed=10393093; DOI=10.1042/bj3410355;
RA Crocker P.R., Vinson M., Kelm S., Drickamer K.;
RT "Molecular analysis of sialoside binding to sialoadhesin by NMR and site-
RT directed mutagenesis.";
RL Biochem. J. 341:355-361(1999).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 20-138 IN COMPLEX WITH SIALIC
RP ACID-BASED INHIBITORS, AND DISULFIDE BOND.
RX PubMed=12737821; DOI=10.1016/s0969-2126(03)00073-x;
RA Zaccai N.R., Maenaka K., Maenaka T., Crocker P.R., Brossmer R., Kelm S.,
RA Jones E.Y.;
RT "Structure-guided design of sialic acid-based Siglec inhibitors and
RT crystallographic analysis in complex with sialoadhesin.";
RL Structure 11:557-567(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-137 IN COMPLEX WITH SIALIC
RP ACID-CONTAINING PEPTIDE, AND DISULFIDE BOND.
RX PubMed=15488769; DOI=10.1016/j.bbapap.2004.08.015;
RA Bukrinsky J.T., St Hilaire P.M., Meldal M., Crocker P.R., Henriksen A.;
RT "Complex of sialoadhesin with a glycopeptide ligand.";
RL Biochim. Biophys. Acta 1702:173-179(2004).
CC -!- FUNCTION: Acts as an endocytic receptor mediating clathrin dependent
CC endocytosis. Macrophage-restricted adhesion molecule that mediates
CC sialic-acid dependent binding to lymphocytes, including granulocytes,
CC monocytes, natural killer cells, B-cells and CD8 T-cells (By
CC similarity). Preferentially binds to alpha-2,3-linked sialic acid.
CC Binds to SPN/CD43 on T-cells. May play a role in hematopoiesis. May act
CC as a counter-receptor for CLEC10A in lymph node. {ECO:0000250,
CC ECO:0000269|PubMed:15364954}.
CC -!- SUBUNIT: Interacts with CLEC10A. {ECO:0000269|PubMed:11238599,
CC ECO:0000269|PubMed:12737821, ECO:0000269|PubMed:15364954,
CC ECO:0000269|PubMed:15488769, ECO:0000269|PubMed:9660955}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q62230-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62230-2; Sequence=VSP_002573, VSP_002574;
CC Name=3;
CC IsoId=Q62230-3; Sequence=VSP_002575, VSP_002576;
CC -!- TISSUE SPECIFICITY: Detected in lymph node in the subcapsular sinus,
CC interfollicular regions, and T and B-cell boundary (at protein level).
CC Expressed by macrophages in various tissues. Highest expression in
CC spleen and lymph node with lower amounts in lung, liver, bone marrow,
CC heart and skin. No expression in thymus, kidney, brain or small
CC intestine. {ECO:0000269|PubMed:15364954}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA85268.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA85290.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Siglec-1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_193";
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DR EMBL; Z36293; CAA85290.1; ALT_FRAME; mRNA.
DR EMBL; Z36233; CAA85268.1; ALT_FRAME; mRNA.
DR EMBL; Z36234; CAA85269.1; -; mRNA.
DR EMBL; U92842; AAB95641.1; -; Genomic_DNA.
DR EMBL; U92833; AAB95641.1; JOINED; Genomic_DNA.
DR EMBL; U92834; AAB95641.1; JOINED; Genomic_DNA.
DR EMBL; U92836; AAB95641.1; JOINED; Genomic_DNA.
DR EMBL; U92837; AAB95641.1; JOINED; Genomic_DNA.
DR EMBL; U92838; AAB95641.1; JOINED; Genomic_DNA.
DR EMBL; U92839; AAB95641.1; JOINED; Genomic_DNA.
DR EMBL; U92840; AAB95641.1; JOINED; Genomic_DNA.
DR EMBL; U92841; AAB95641.1; JOINED; Genomic_DNA.
DR EMBL; AL831736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL833771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S50065; S50065.
DR RefSeq; NP_035556.3; NM_011426.3.
DR PDB; 1OD7; X-ray; 3.00 A; A=20-138.
DR PDB; 1OD9; X-ray; 2.10 A; A=20-138.
DR PDB; 1ODA; X-ray; 3.31 A; A=20-138.
DR PDB; 1QFO; X-ray; 1.85 A; A/B/C=20-138.
DR PDB; 1QFP; X-ray; 2.80 A; A=20-138.
DR PDB; 1URL; X-ray; 2.40 A; A=20-137.
DR PDB; 2BVE; X-ray; 2.20 A; A/B=20-138.
DR PDBsum; 1OD7; -.
DR PDBsum; 1OD9; -.
DR PDBsum; 1ODA; -.
DR PDBsum; 1QFO; -.
DR PDBsum; 1QFP; -.
DR PDBsum; 1URL; -.
DR PDBsum; 2BVE; -.
DR AlphaFoldDB; Q62230; -.
DR SMR; Q62230; -.
DR BioGRID; 203360; 2.
DR IntAct; Q62230; 2.
DR STRING; 10090.ENSMUSP00000028794; -.
DR UniLectin; Q62230; -.
DR GlyGen; Q62230; 15 sites.
DR iPTMnet; Q62230; -.
DR PhosphoSitePlus; Q62230; -.
DR MaxQB; Q62230; -.
DR PaxDb; Q62230; -.
DR PRIDE; Q62230; -.
DR ProteomicsDB; 261097; -. [Q62230-1]
DR ProteomicsDB; 261098; -. [Q62230-2]
DR ProteomicsDB; 261099; -. [Q62230-3]
DR DNASU; 20612; -.
DR GeneID; 20612; -.
DR KEGG; mmu:20612; -.
DR UCSC; uc008mkp.1; mouse. [Q62230-3]
DR UCSC; uc008mkq.1; mouse. [Q62230-2]
DR CTD; 6614; -.
DR MGI; MGI:99668; Siglec1.
DR eggNOG; KOG4475; Eukaryota.
DR InParanoid; Q62230; -.
DR OrthoDB; 54136at2759; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 20612; 2 hits in 72 CRISPR screens.
DR EvolutionaryTrace; Q62230; -.
DR PRO; PR:Q62230; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q62230; protein.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046790; F:virion binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IBA:GO_Central.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0070234; P:positive regulation of T cell apoptotic process; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 17.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13895; Ig_2; 6.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 16.
DR SMART; SM00408; IGc2; 15.
DR SUPFAM; SSF48726; SSF48726; 12.
DR PROSITE; PS50835; IG_LIKE; 14.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Endocytosis; Glycoprotein;
KW Immunoglobulin domain; Lectin; Membrane; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT CHAIN 20..1695
FT /note="Sialoadhesin"
FT /id="PRO_0000014969"
FT TOPO_DOM 20..1639
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1640..1660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1661..1695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..136
FT /note="Ig-like V-type"
FT DOMAIN 153..235
FT /note="Ig-like C2-type 1"
FT DOMAIN 239..321
FT /note="Ig-like C2-type 2"
FT DOMAIN 326..406
FT /note="Ig-like C2-type 3"
FT DOMAIN 416..508
FT /note="Ig-like C2-type 4"
FT DOMAIN 509..594
FT /note="Ig-like C2-type 5"
FT DOMAIN 602..701
FT /note="Ig-like C2-type 6"
FT DOMAIN 704..781
FT /note="Ig-like C2-type 7"
FT DOMAIN 795..890
FT /note="Ig-like C2-type 8"
FT DOMAIN 894..973
FT /note="Ig-like C2-type 9"
FT DOMAIN 980..1079
FT /note="Ig-like C2-type 10"
FT DOMAIN 1081..1161
FT /note="Ig-like C2-type 11"
FT DOMAIN 1172..1264
FT /note="Ig-like C2-type 12"
FT DOMAIN 1245..1337
FT /note="Ig-like C2-type 13"
FT DOMAIN 1342..1439
FT /note="Ig-like C2-type 14"
FT DOMAIN 1442..1520
FT /note="Ig-like C2-type 15"
FT DOMAIN 1534..1627
FT /note="Ig-like C2-type 16"
FT MOTIF 827..829
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT BINDING 63
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000305|PubMed:9660955"
FT BINDING 116
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000305|PubMed:10393093,
FT ECO:0000305|PubMed:12737821, ECO:0000305|PubMed:15488769,
FT ECO:0000305|PubMed:9660955"
FT BINDING 122..126
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1090
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 41..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:15488769"
FT DISULFID 160..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 263..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 347..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 434..492
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 532..576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 625..685
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 725..770
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 813..872
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 912..956
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1001..1063
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1103..1145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1189..1237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1277..1320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1363..1422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1463..1509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1552..1611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 326..340
FT /note="MAEVKMNPAGPVLEN -> SESWMRLRGPVSGKH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7925291"
FT /id="VSP_002573"
FT VAR_SEQ 341..1695
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7925291"
FT /id="VSP_002574"
FT VAR_SEQ 1529..1599
FT /note="YPPKTPTLIVFVEPQGGHQGILDCRVDSEPLAILTLHRGSQLVASNQLHDAP
FT TKPHIRVTAPPNALRVDIE -> CEYEPISALCLSLHLTGPYQAFSSAQSKGFIGKGLR
FT TLASSLAGCMWFVSMLGYPALKWRILLPFWDEYRR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7925291"
FT /id="VSP_002575"
FT VAR_SEQ 1600..1695
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7925291"
FT /id="VSP_002576"
FT MUTAGEN 21
FT /note="W->Q: Loss of sialic acid binding."
FT /evidence="ECO:0000269|PubMed:10393093"
FT MUTAGEN 116
FT /note="R->A: Loss of sialic acid binding."
FT /evidence="ECO:0000269|PubMed:10393093"
FT MUTAGEN 116
FT /note="R->L: 10-fold loss in affinity to sialic acid."
FT /evidence="ECO:0000269|PubMed:10393093"
FT CONFLICT 159
FT /note="N -> F (in Ref. 2; AAB95641)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="V -> S (in Ref. 1; CAA85268/CAA85290 and 2;
FT AAB95641)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="P -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="V -> G (in Ref. 1; CAA85268/CAA85290 and 2;
FT AAB95641)"
FT /evidence="ECO:0000305"
FT CONFLICT 759..760
FT /note="PV -> LL (in Ref. 1; CAA85268/CAA85290 and 2;
FT AAB95641)"
FT /evidence="ECO:0000305"
FT CONFLICT 1050..1052
FT /note="IHF -> FLV (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1055..1056
FT /note="LE -> VQ (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1062
FT /note="T -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1066
FT /note="S -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1426
FT /note="N -> H (in Ref. 1; CAA85268/CAA85290 and 2;
FT AAB95641)"
FT /evidence="ECO:0000305"
FT CONFLICT 1453
FT /note="V -> W (in Ref. 1; CAA85268/CAA85290 and 2;
FT AAB95641)"
FT /evidence="ECO:0000305"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1QFO"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1QFO"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1QFO"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1QFO"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1QFO"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:1QFO"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1QFO"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1QFO"
FT TURN 81..86
FT /evidence="ECO:0007829|PDB:1QFO"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1QFO"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1QFO"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1QFO"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1QFO"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:1QFO"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1QFO"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:1QFO"
SQ SEQUENCE 1695 AA; 182979 MW; AF704F68C40E113A CRC64;
MCVLFSLLLL ASVFSLGQTT WGVSSPKNVQ GLSGSCLLIP CIFSYPADVP VSNGITAIWY
YDYSGKRQVV IHSGDPKLVD KRFRGRAELM GNMDHKVCNL LLKDLKPEDS GTYNFRFEIS
DSNRWLDVKG TTVTVTTDPS PPTITIPEEL REGMERNFNC STPYLCLQEK QVSLQWRGQD
PTHSVTSSFQ SLEPTGVYHQ TTLHMALSWQ DHGRTLLCQF SLGAHSSRKE VYLQVPHAPK
GVEILLSSSG RNILPGDPVT LTCRVNSSYP AVSAVQWARD GVNLGVTGHV LRLFSAAWND
SGAYTCQATN DMGSLVSSPL SLHVFMAEVK MNPAGPVLEN ETVTLLCSTP KEAPQELRYS
WYKNHILLED AHASTLHLPA VTRADTGFYF CEVQNAQGSE RSSPLSVVVR YPPLTPDLTT
FLETQAGLVG ILHCSVVSEP LATVVLSHGG LTLASNSGEN DFNPRFRISS APNSLRLEIR
DLQPADSGEY TCLAVNSLGN STSSLDFYAN VARLLINPSA EVVEGQAVTL SCRSGLSPAP
DTRFSWYLNG ALLLEGSSSS LLLPAASSTD AGSYYCRTQA GPNTSGPSLP TVLTVFYPPR
KPTFTARLDL DTSGVGDGRR GILLCHVDSD PPAQLRLLHK GHVVATSLPS RCGSCSQRTK
VSRTSNSLHV EIQKPVLEDE GVYLCEASNT LGNSSAAASF NAKATVLVIT PSNTLREGTE
ANLTCNVNQE VAVSPANFSW FRNGVLWTQG SLETVRLQPV ARTDAAVYAC RLLTEDGAQL
SAPVVLSVLY APDPPKLSAL LDVGQGHMAV FICTVDSYPL AHLSLFRGDH LLATNLEPQR
PSHGRIQAKA TANSLQLEVR ELGLVDSGNY HCEATNILGS ANSSLFFQVR GAWVQVSPSP
ELREGQAVVL SCQVPTGVSE GTSYSWYQDG RPLQESTSST LRIAAISLRQ AGAYHCQAQA
PDTAIASLAA PVSLHVSYTP RHVTLSALLS TDPERLGHLV CSVQSDPPAQ LQLFHRNRLV
ASTLQGADEL AGSNPRLHVT VLPNELRLQI HFPELEDDGT YTCEASNTLG QASAAADFDA
QAVRVTVWPN ATVQEGQQVN LTCLVWSTHQ DSLSYTWYKG GQQLLGARSI TLPSVKVLDA
TSYRCGVGLP GHAPHLSRPV TLDVLHAPRN LRLTYLLETQ GRQLALVLCT VDSRPPAQLT
LSHGDQLVAS STEASVPNTL RLELQDPRPS NEGLYSCSAH SPLGKANTSL ELLLEGVRVK
MNPSGSVPEG EPVTVTCEDP AALSSALYAW FHNGHWLQEG PASSLQFLVT TRAHAGAYFC
QVHDTQGTRS SRPASLQILY APRDAVLSSF RDSRTRLMVV IQCTVDSEPP AEMVLSHNGK
VLAASHERHS SASGIGHIQV ARNALRLQVQ DVTLGDGNTY VCTAQNTLGS ISTTQRLLTE
TDIRVTAEPG LDVPEGTALN LSCLLPGGSG PTGNSSFTWF WNRHRLHSAP VPTLSFTPVV
RAQAGLYHCR ADLPTGATTS APVMLRVLYP PKTPTLIVFV EPQGGHQGIL DCRVDSEPLA
ILTLHRGSQL VASNQLHDAP TKPHIRVTAP PNALRVDIEE LGPSNQGEYV CTASNTLGSA
SASAYFGTRA LHQLQLFQRL LWVLGFLAGF LCLLLGLVAY HTWRKKSSTK LNEDENSAEM
ATKKNTIQEE VVAAL
