ID   ICAM3_HUMAN             Reviewed;         547 AA.
AC   P32942; Q6PD68;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 2.
DT   04-NOV-2026, entry version 229.
DE   RecName: Full=Intercellular adhesion molecule 3 {ECO:0000303|PubMed:8459213};
DE            Short=ICAM-3 {ECO:0000303|PubMed:1448173};
DE   AltName: Full=CDw50 {ECO:0000303|PubMed:8325327};
DE   AltName: Full=ICAM-R {ECO:0000303|PubMed:1448174};
DE   AltName: CD_antigen=CD50;
DE   Flags: Precursor;
GN   Name=ICAM3 {ECO:0000312|HGNC:HGNC:5346};
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], FUNCTION, TISSUE SPECIFICITY, AND VARIANTS
RP   GLY-115 AND GLY-143.
RX   PubMed=1448173; DOI=10.1038/360481a0;
RA   Fawcett J., Holness C.L., Needham L.A., Turley H., Gatter K.C., Mason D.Y.,
RA   Simmons D.L.;
RT   "Molecular cloning of ICAM-3, a third ligand for LFA-1, constitutively
RT   expressed on resting leukocytes.";
RL   Nature 360:481-484(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANTS
RP   GLY-115 AND GLY-143.
RX   PubMed=1448174; DOI=10.1038/360485a0;
RA   Vazeux R., Hoffman P.A., Tomita J.K., Dickinson E.S., Jasman R.L.,
RA   St John T., Gallatin W.M.;
RT   "Cloning and characterization of a new intercellular adhesion molecule
RT   ICAM-R.";
RL   Nature 360:485-488(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND VARIANTS
RP   GLY-115 AND GLY-143.
RX   PubMed=8459213; DOI=10.1084/jem.177.4.1187;
RA   de Fougerolles A.R., Kilckstein L.B., Springer T.A.;
RT   "Cloning and expression of intercellular adhesion molecule 3 reveals strong
RT   homology to other immunoglobulin family counter-receptors for lymphocyte
RT   function-associated antigen 1.";
RL   J. Exp. Med. 177:1187-1192(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Tan J., Ong R., Hibberd M.L., Seielstad M.;
RT   "Genetic variation in immune response genes.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 197-217; 269-293 AND 338-365, FUNCTION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=8325327; DOI=10.1002/eji.1830230717;
RA   Juan M., Vilella R., Mila J., Yague J., Miralles A., Campbell K.S.,
RA   Friedrich R.J., Cambier J., Vives J., de Fougerolles A.R., Springer T.A.;
RT   "CDw50 and ICAM-3: two names for the same molecule.";
RL   Eur. J. Immunol. 23:1508-1512(1993).
RN   [8]
RP   FUNCTION.
RX   PubMed=8777714; DOI=10.1016/1074-7613(95)90058-6;
RA   Van der Vieren M., Le Trong H., Wood C.L., Moore P.F., St John T.,
RA   Staunton D.E., Gallatin W.M.;
RT   "A novel leukointegrin, alpha d beta 2, binds preferentially to ICAM-3.";
RL   Immunity 3:683-690(1995).
RN   [9]
RP   INTERACTION WITH MSN.
RX   PubMed=9298994; DOI=10.1083/jcb.138.6.1409;
RA   Serrador J.M., Alonso-Lebrero J.L., del Pozo M.A., Furthmayr H.,
RA   Schwartz-Albiez R., Calvo J., Lozano F., Sanchez-Madrid F.;
RT   "Moesin interacts with the cytoplasmic region of intercellular adhesion
RT   molecule-3 and is redistributed to the uropod of T lymphocytes during cell
RT   polarization.";
RL   J. Cell Biol. 138:1409-1423(1997).
RN   [10]
RP   FUNCTION.
RX   PubMed=10721994; DOI=10.1016/s0092-8674(00)80693-5;
RA   Geijtenbeek T.B., Torensma R., van Vliet S.J., van Duijnhoven G.C.,
RA   Adema G.J., van Kooyk Y., Figdor C.G.;
RT   "Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor
RT   that supports primary immune responses.";
RL   Cell 100:575-585(2000).
RN   [11]
RP   STRUCTURE OF N-LINKED CARBOHYDRATES.
RX   PubMed=11179968; DOI=10.1046/j.1432-1327.2001.01960.x;
RA   Funatsu O., Sato T., Kotovuori P., Gahmberg C.G., Ikekita M., Furukawa K.;
RT   "Structural study of N-linked oligosaccharides of human intercellular
RT   adhesion molecule-3 (CD50).";
RL   Eur. J. Biochem. 268:1020-1029(2001).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-363.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [13]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-363.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [14]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-87; ASN-134; ASN-206;
RP   ASN-295 AND ASN-363.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [17]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=23775590; DOI=10.1007/s10495-013-0873-z;
RA   Kristof E., Zahuczky G., Katona K., Doro Z., Nagy E., Fesues L.;
RT   "Novel role of ICAM3 and LFA-1 in the clearance of apoptotic neutrophils by
RT   human macrophages.";
RL   Apoptosis 18:1235-1251(2013).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [19] {ECO:0007744|PDB:1T0P}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ITGAL AND MG(2+), DISULFIDE BOND, AND
RP   GLYCOSYLATION AT ASN-52 AND ASN-110.
RX   PubMed=15728350; DOI=10.1073/pnas.0500200102;
RA   Song G., Yang Y., Liu J.-H., Casasnovas J.M., Shimaoka M., Springer T.A.,
RA   Wang J.-H.;
RT   "An atomic resolution view of ICAM recognition in a complex between the
RT   binding domains of ICAM-3 and integrin alphaLbeta2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3366-3371(2005).
CC   -!- FUNCTION: Cell adhesion molecule that functions as a receptor ligand of
CC       the signaling receptor ITGAL:ITGB2/LFA-1 (lymphocyte-function
CC       associated (LFA) molecule 1) ensuring apoptotic neutrophil phagocytosis
CC       by macrophages (PubMed:1448173, PubMed:1448174, PubMed:23775590,
CC       PubMed:8325327, PubMed:8459213). Is also a ligand for integrin
CC       ITGAD/ITGB2 (PubMed:8777714). Ligand of CD209 on dendritic cells (DC)
CC       through an integrin-independent mechanism that requires Ca(2+) and that
CC       forms a first contact between DC and resting T cell, facilitating the
CC       downstream DC-T cell clustering process and DC-induced proliferation of
CC       resting T Cells (PubMed:10721994). {ECO:0000269|PubMed:10721994,
CC       ECO:0000269|PubMed:1448173, ECO:0000269|PubMed:1448174,
CC       ECO:0000269|PubMed:23775590, ECO:0000269|PubMed:8325327,
CC       ECO:0000269|PubMed:8459213, ECO:0000269|PubMed:8777714}.
CC   -!- SUBUNIT: Interacts (via cytoplasmic tail) with MSN/moesin.
CC       {ECO:0000269|PubMed:9298994}.
CC   -!- INTERACTION:
CC       P32942; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-725421, EBI-12244618;
CC       P32942; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-725421, EBI-12256978;
CC       P32942; O14493: CLDN4; NbExp=3; IntAct=EBI-725421, EBI-9316372;
CC       P32942; P56851: EDDM3B; NbExp=3; IntAct=EBI-725421, EBI-10215665;
CC       P32942; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-725421, EBI-10317425;
CC       P32942; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-725421, EBI-8652744;
CC       P32942; P11686: SFTPC; NbExp=3; IntAct=EBI-725421, EBI-10197617;
CC       P32942; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-725421, EBI-8640191;
CC       P32942; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-725421, EBI-12188413;
CC       P32942; P30536: TSPO; NbExp=3; IntAct=EBI-725421, EBI-6623146;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23775590,
CC       ECO:0000269|PubMed:8459213}; Single-pass type I membrane protein.
CC       Note=Localization at uropodium is mediated through interaction with
CC       MSN. {ECO:0000269|PubMed:9298994}.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed only on resting leukocytes
CC       (PubMed:8325327). No expressed on resting or cytokine-activated
CC       endothelial cells (PubMed:1448174). {ECO:0000269|PubMed:1448173,
CC       ECO:0000269|PubMed:1448174, ECO:0000269|PubMed:23775590,
CC       ECO:0000269|PubMed:8325327}.
CC   -!- PTM: N-glycosylated; glycans consist of a mixture of tri- and tetra-
CC       antennary complex-type chains and high-mannose chains.
CC       {ECO:0000269|PubMed:15728350, ECO:0000269|PubMed:16335952,
CC       ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=ICAM-3;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_263";
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DR   EMBL; S50015; AAB24331.2; -; mRNA.
DR   EMBL; X69711; CAA49369.1; -; mRNA.
DR   EMBL; X69819; CAA49473.1; -; mRNA.
DR   EMBL; DQ217937; ABB01007.1; -; Genomic_DNA.
DR   EMBL; CH471106; EAW84092.1; -; Genomic_DNA.
DR   EMBL; BC058903; AAH58903.1; -; mRNA.
DR   CCDS; CCDS12235.1; -.
DR   PIR; S28904; S28904.
DR   RefSeq; NP_002153.2; NM_002162.5.
DR   PDB; 1T0P; X-ray; 1.66 A; B=30-114.
DR   SMR; P32942; -.
DR   BioGRID; 109612; 30.
DR   IntAct; P32942; 20.
DR   STRING; 9606.ENSP00000160262; -.
DR   NDEx; IQUERY-CP-ICAM3; 2 NDEx IQuery Curated Pathways.
DR   ChEMBL; CHEMBL3712862; -.
DR   GlyConnect; P32942; 17 N-Linked glycans.
DR   GlyCosmos; P32942; 17 sites, 51 glycans.
DR   GlyGen; P32942; 20 sites, 50 N-linked glycans (5 sites), 1 O-linked glycan (4 sites).
DR   iPTMnet; P32942; -.
DR   PhosphoSitePlus; P32942; -.
DR   BioMuta; ICAM3; -.
DR   DMDM; 206729872; -.
DR   PaxDb; 9606-ENSP00000160262; -.
DR   PeptideAtlas; P32942; -.
DR   ProteomicsDB; 54892; -.
DR   jPOST; P32942; -.
DR   MassIVE; P32942; -.
DR   DNASU; 3385; -.
DR   Ensembl; ENST00000160262.10; ENSP00000160262.3; ENSG00000076662.12.
DR   GeneID; 3385; -.
DR   KEGG; hsa:3385; -.
DR   MANE-Select; ENST00000160262.10; ENSP00000160262.3; NM_002162.5; NP_002153.2.
DR   UCSC; uc002mob.3; human.
DR   CTD; 3385; -.
DR   DisGeNET; 3385; -.
DR   VEuPathDB; HostDB:ENSG00000076662; -.
DR   GeneCards; ICAM3; -.
DR   HGNC; HGNC:5346; ICAM3.
DR   AGR; HGNC:5346; -.
DR   HPA; ENSG00000076662; Tissue enhanced (bone marrow, lymphoid tissue).
DR   MIM; 146631; gene.
DR   OpenTargets; ENSG00000076662; -.
DR   ClinPGx; PA29594; -.
DR   eggNOG; ENOG502RZRA; Eukaryota.
DR   GeneTree; ENSGT00940000159005; -.
DR   InParanoid; P32942; -.
DR   OMA; ACCQLPT; -.
DR   OrthoDB; 6250964at2759; -.
DR   PhylomeDB; P32942; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
DR   SignaLink; P32942; -.
DR   SIGNOR; P32942; -.
DR   ChiTaRS; ICAM3; human.
DR   EvolutionaryTrace; P32942; -.
DR   Agora; ENSG00000076662; -.
DR   GeneWiki; ICAM3; -.
DR   GenomeRNAi; 3385; -.
DR   PRO; PR:P32942; -.
DR   Bgee; ENSG00000076662; Expressed in blood and 163 other cell types or tissues.
DR   ExpressionAtlas; P32942; baseline and differential.
DR   CDD; cd00096; Ig; 1.
DR   CDD; cd20997; IgI_N_ICAM-3; 1.
DR   FunFam; 2.60.40.10:FF:000194; Intercellular adhesion molecule 1; 1.
DR   FunFam; 2.60.40.10:FF:000459; Intercellular adhesion molecule 1; 1.
DR   FunFam; 2.60.40.10:FF:000648; Intercellular adhesion molecule 1; 1.
DR   FunFam; 2.60.40.10:FF:002232; Intercellular adhesion molecule 3; 1.
DR   FunFam; 2.60.40.10:FF:000338; intercellular adhesion molecule 5; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   InterPro; IPR003988; ICAM.
DR   InterPro; IPR048679; ICAM1_3_5_D2.
DR   InterPro; IPR013768; ICAM_N.
DR   InterPro; IPR047012; ICAM_VCAM.
DR   InterPro; IPR003987; ICAM_VCAM_N.
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   PANTHER; PTHR13771; INTERCELLULAR ADHESION MOLECULE; 1.
DR   PANTHER; PTHR13771:SF17; INTERCELLULAR ADHESION MOLECULE 3; 1.
DR   Pfam; PF21146; ICAM1_3_5_D2; 1.
DR   Pfam; PF03921; ICAM_N; 1.
DR   PRINTS; PR01473; ICAM.
DR   PRINTS; PR01472; ICAMVCAM1.
DR   SMART; SM00409; IG; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 5.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR   GO; GO:0048018; F:receptor ligand activity; IDA:UniProt.
DR   GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR   GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IDA:UniProt.
DR   GO; GO:0033079; P:immature T cell proliferation; IDA:UniProt.
DR   GO; GO:0006955; P:immune response; IDA:UniProtKB.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:UniProtKB.
DR   Proteomes; UP000005640; Chromosome 19.
DR   PathwayCommons; P32942; -.
DR   Pharos; P32942; Tbio.
DR   Antibodypedia; 3738; 1765 antibodies from 49 providers.
DR   RNAct; P32942; protein.
DR   BioGRID-ORCS; 3385; 16 hits in 1163 CRISPR screens.
DR   AlphaFoldDB; P32942; -.
DR   FunCoup; P32942; 240.
DR   PAN-GO; P32942; 3 GO annotations based on evolutionary models.
PE   1: Evidence at protein level;
KW   3D-structure; Cell adhesion; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Phagocytosis; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..547
FT                   /note="Intercellular adhesion molecule 3"
FT                   /id="PRO_0000014794"
FT   TOPO_DOM        30..485
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        486..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        511..547
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          46..103
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          132..197
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          234..301
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          329..382
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          416..469
FT                   /note="Ig-like C2-type 5"
FT   BINDING         66
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with ITGAL"
FT                   /evidence="ECO:0000269|PubMed:15728350,
FT                   ECO:0007744|PDB:1T0P"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15728350"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15728350"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973"
FT   CARBOHYD        389
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        453
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:15728350, ECO:0007744|PDB:1T0P"
FT   DISULFID        57..100
FT                   /evidence="ECO:0000269|PubMed:15728350,
FT                   ECO:0007744|PDB:1T0P"
FT   DISULFID        139..190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        241..294
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        336..375
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        423..462
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VARIANT         63
FT                   /note="I -> V (in dbSNP:rs17697947)"
FT                   /id="VAR_046547"
FT   VARIANT         115
FT                   /note="R -> G (in dbSNP:rs7258015)"
FT                   /evidence="ECO:0000269|PubMed:1448174,
FT                   ECO:0000269|PubMed:8459213"
FT                   /id="VAR_059394"
FT   VARIANT         143
FT                   /note="D -> G (in dbSNP:rs2304237)"
FT                   /evidence="ECO:0000269|PubMed:1448173,
FT                   ECO:0000269|PubMed:1448174, ECO:0000269|PubMed:8459213"
FT                   /id="VAR_046548"
FT   VARIANT         525
FT                   /note="S -> T (in dbSNP:rs2230399)"
FT                   /id="VAR_024498"
FT   CONFLICT        60
FT                   /note="S -> F (in Ref. 1; AAB24331)"
FT                   /evidence="ECO:0000305"
FT   STRAND          34..38
FT                   /evidence="ECO:0007829|PDB:1T0P"
FT   STRAND          48..55
FT                   /evidence="ECO:0007829|PDB:1T0P"
FT   STRAND          61..66
FT                   /evidence="ECO:0007829|PDB:1T0P"
FT   STRAND          68..77
FT                   /evidence="ECO:0007829|PDB:1T0P"
FT   STRAND          80..86
FT                   /evidence="ECO:0007829|PDB:1T0P"
FT   STRAND          92..100
FT                   /evidence="ECO:0007829|PDB:1T0P"
FT   STRAND          103..113
FT                   /evidence="ECO:0007829|PDB:1T0P"
SQ   SEQUENCE   547 AA;  59541 MW;  4B7BDC02F24F3031 CRC64;
     MATMVPSVLW PRACWTLLVC CLLTPGVQGQ EFLLRVEPQN PVLSAGGSLF VNCSTDCPSS
     EKIALETSLS KELVASGMGW AAFNLSNVTG NSRILCSVYC NGSQITGSSN ITVYRLPERV
     ELAPLPPWQP VGQNFTLRCQ VEDGSPRTSL TVVLLRWEEE LSRQPAVEEP AEVTATVLAS
     RDDHGAPFSC RTELDMQPQG LGLFVNTSAP RQLRTFVLPV TPPRLVAPRF LEVETSWPVD
     CTLDGLFPAS EAQVYLALGD QMLNATVMNH GDTLTATATA TARADQEGAR EIVCNVTLGG
     ERREARENLT VFSFLGPIVN LSEPTAHEGS TVTVSCMAGA RVQVTLDGVP AAAPGQPAQL
     QLNATESDDG RSFFCSATLE VDGEFLHRNS SVQLRVLYGP KIDRATCPQH LKWKDKTRHV
     LQCQARGNPY PELRCLKEGS SREVPVGIPF FVNVTHNGTY QCQASSSRGK YTLVVVMDIE
     AGSSHFVPVF VAVLLTLGVV TIVLALMYVF REHQRSGSYH VREESTYLPL TSMQPTEAMG
     EEPSRAE
//