ICAM3_HUMAN
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 03-AUG-2022, entry version 209.
DE RecName: Full=Intercellular adhesion molecule 3;
DE Short=ICAM-3;
DE AltName: Full=CDw50;
DE AltName: Full=ICAM-R;
DE AltName: CD_antigen=CD50;
DE Flags: Precursor;
GN Name=ICAM3;
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], AND VARIANTS 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], AND VARIANTS 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.
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 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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
RP FUNCTION, 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 [16]
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 [17]
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 30-115 IN COMPLEX WITH INTEGRIN
RP ALPHALBETA2, DISULFIDE BOND, AND 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: ICAM proteins are ligands for the leukocyte adhesion protein
CC LFA-1 (integrin alpha-L/beta-2) (PubMed:1448173). ICAM3 is also a
CC ligand for integrin alpha-D/beta-2. In association with integrin alpha-
CC L/beta-2, contributes to apoptotic neutrophil phagocytosis by
CC macrophages (PubMed:23775590). {ECO:0000269|PubMed:1448173,
CC ECO:0000269|PubMed:23775590}.
CC -!- SUBUNIT: Interacts with moesin/MSN. {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: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Leukocytes. {ECO:0000269|PubMed:1448173,
CC ECO:0000269|PubMed:23775590}.
CC -!- PTM: Upon stimulation by a physiologic stimuli becomes rapidly and
CC transiently phosphorylated on serine residues.
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; ALT_SEQ; 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_002162.4.
DR PDB; 1T0P; X-ray; 1.66 A; B=30-114.
DR PDBsum; 1T0P; -.
DR AlphaFoldDB; P32942; -.
DR SMR; P32942; -.
DR BioGRID; 109612; 28.
DR IntAct; P32942; 17.
DR MINT; P32942; -.
DR STRING; 9606.ENSP00000160262; -.
DR ChEMBL; CHEMBL3712862; -.
DR GlyConnect; 286; 17 N-Linked glycans.
DR GlyGen; P32942; 16 sites, 26 N-linked glycans (1 site).
DR iPTMnet; P32942; -.
DR PhosphoSitePlus; P32942; -.
DR BioMuta; ICAM3; -.
DR DMDM; 206729872; -.
DR EPD; P32942; -.
DR jPOST; P32942; -.
DR MassIVE; P32942; -.
DR MaxQB; P32942; -.
DR PaxDb; P32942; -.
DR PeptideAtlas; P32942; -.
DR PRIDE; P32942; -.
DR ProteomicsDB; 54892; -.
DR Antibodypedia; 3738; 1563 antibodies from 45 providers.
DR DNASU; 3385; -.
DR Ensembl; ENST00000160262.10; ENSP00000160262.3; ENSG00000076662.10.
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 GeneCards; ICAM3; -.
DR HGNC; HGNC:5346; ICAM3.
DR HPA; ENSG00000076662; Group enriched (bone marrow, liver, lymphoid tissue).
DR MIM; 146631; gene.
DR neXtProt; NX_P32942; -.
DR OpenTargets; ENSG00000076662; -.
DR PharmGKB; PA29594; -.
DR VEuPathDB; HostDB:ENSG00000076662; -.
DR eggNOG; ENOG502RZRA; Eukaryota.
DR GeneTree; ENSGT00940000159005; -.
DR InParanoid; P32942; -.
DR OMA; IDRAKCP; -.
DR OrthoDB; 1011028at2759; -.
DR PhylomeDB; P32942; -.
DR TreeFam; TF333745; -.
DR PathwayCommons; 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 BioGRID-ORCS; 3385; 15 hits in 1078 CRISPR screens.
DR ChiTaRS; ICAM3; human.
DR EvolutionaryTrace; P32942; -.
DR GeneWiki; ICAM3; -.
DR GenomeRNAi; 3385; -.
DR Pharos; P32942; Tbio.
DR PRO; PR:P32942; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P32942; protein.
DR Bgee; ENSG00000076662; Expressed in blood and 161 other tissues.
DR ExpressionAtlas; P32942; baseline and differential.
DR Genevisible; P32942; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005178; F:integrin binding; IPI:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR003988; ICAM.
DR InterPro; IPR013768; ICAM_N.
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 Pfam; PF03921; ICAM_N; 1.
DR PRINTS; PR01473; ICAM.
DR PRINTS; PR01472; ICAMVCAM1.
DR SMART; SM00409; IG; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Phagocytosis;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW 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 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
