CLM8_HUMAN
ID CLM8_HUMAN Reviewed; 299 AA.
AC Q9UGN4; A8MW96; O95100; Q9HD97; Q9P0F3; Q9UBK4; Q9UMS9; Q9UMT0;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=CMRF35-like molecule 8;
DE Short=CLM-8;
DE AltName: Full=CD300 antigen-like family member A;
DE AltName: Full=CMRF-35-H9;
DE Short=CMRF35-H9;
DE AltName: Full=CMRF35-H;
DE AltName: Full=IRC1/IRC2;
DE AltName: Full=Immunoglobulin superfamily member 12;
DE Short=IgSF12;
DE AltName: Full=Inhibitory receptor protein 60;
DE Short=IRp60;
DE AltName: Full=NK inhibitory receptor;
DE AltName: CD_antigen=CD300a;
DE Flags: Precursor;
GN Name=CD300A; Synonyms=CMRF35H, IGSF12; ORFNames=HSPC083;
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), TISSUE SPECIFICITY, AND
RP PHOSPHORYLATION.
RC TISSUE=Lymphoid tissue;
RX PubMed=10540326;
RX DOI=10.1002/(sici)1521-4141(199910)29:10<3148::aid-immu3148>3.0.co;2-l;
RA Cantoni C., Bottino C., Augugliaro R., Morelli L., Marcenaro E.,
RA Castriconi R., Vitale M., Pende D., Sivori S., Millo R., Biassoni R.,
RA Moretta L., Moretta A.;
RT "Molecular and functional characterization of IRp60, a member of the
RT immunoglobulin superfamily that functions as an inhibitory receptor in
RT human NK cells.";
RL Eur. J. Immunol. 29:3148-3159(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT GLN-111.
RC TISSUE=Lymphoid tissue;
RA Cantoni C., Biassoni R.;
RT "IRC1 isoforms.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9701027; DOI=10.1093/intimm/10.7.891;
RA Green B.J., Clark G.J., Hart D.N.J.;
RT "The CMRF-35 mAb recognizes a second leukocyte membrane molecule with a
RT domain similar to the poly Ig receptor.";
RL Int. Immunol. 10:891-899(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=10746781; DOI=10.1034/j.1399-0039.2000.550201.x;
RA Clark G.J., Green B.J., Hart D.N.J.;
RT "The CMRF-35H gene structure predicts for an independently expressed member
RT of an ITIM/ITAM pair of molecules localized to human chromosome 17.";
RL Tissue Antigens 55:101-109(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Umbilical cord blood;
RA Zhang Q.H., Ye M., Zhou J., Shen Y., Wu X.Y., Guan Z.Q., Wang L., Fan H.Y.,
RA Mao Y.F., Dai M., Huang Q.H., Chen S.J., Chen Z.;
RT "Human partial CDS cloned from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Blood;
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 [8]
RP FUNCTION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=16339535; DOI=10.4049/jimmunol.175.12.7989;
RA Bachelet I., Munitz A., Moretta A., Moretta L., Levi-Schaffer F.;
RT "The inhibitory receptor IRp60 (CD300a) is expressed and functional on
RT human mast cells.";
RL J. Immunol. 175:7989-7995(2005).
RN [9]
RP FUNCTION.
RX PubMed=22043923; DOI=10.1111/j.1365-2567.2011.03528.x;
RA Kim E.J., Lee S.M., Suk K., Lee W.H.;
RT "CD300a and CD300f differentially regulate the MyD88 and TRIF-mediated TLR
RT signalling pathways through activation of SHP-1 and/or SHP-2 in human
RT monocytic cell lines.";
RL Immunology 135:226-235(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-128.
RA Dimasi N., Marquez J.A.;
RT "The crystal structure of IRp60 ectodomain.";
RL Submitted (JUN-2007) to the PDB data bank.
RN [11]
RP VARIANT GLN-111.
RX PubMed=12483297; DOI=10.1007/s00439-002-0851-y;
RA Speckman R.A., Wright Daw J.A., Helms C., Duan S., Cao L.,
RA Taillon-Miller P., Kwok P.Y., Menter A., Bowcock A.M.;
RT "Novel immunoglobulin superfamily gene cluster, mapping to a region of
RT human chromosome 17q25, linked to psoriasis susceptibility.";
RL Hum. Genet. 112:34-41(2003).
CC -!- FUNCTION: Inhibitory receptor which may contribute to the down-
CC regulation of cytolytic activity in natural killer (NK) cells, and to
CC the down-regulation of mast cell degranulation (PubMed:10746781,
CC PubMed:16339535, PubMed:9701027). Negatively regulates the Toll-like
CC receptor (TLR) signaling mediated by MYD88 but not TRIF through
CC activation of PTPN6 (PubMed:22043923). {ECO:0000269|PubMed:10746781,
CC ECO:0000269|PubMed:16339535, ECO:0000269|PubMed:22043923,
CC ECO:0000269|PubMed:9701027}.
CC -!- SUBUNIT: Upon tyrosine-phosphorylation, interacts with PTN6/SHP-1 and
CC PTPN11/SHP-2 and INPP5D. {ECO:0000250|UniProtKB:Q6SJQ0}.
CC -!- INTERACTION:
CC Q9UGN4; A8K4G0: CD300LB; NbExp=2; IntAct=EBI-10320732, EBI-26499879;
CC Q9UGN4; O76015: KRT38; NbExp=3; IntAct=EBI-10320732, EBI-1047263;
CC Q9UGN4; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-10320732, EBI-8652744;
CC Q9UGN4; Q8N511: TMEM199; NbExp=3; IntAct=EBI-10320732, EBI-10265825;
CC Q9UGN4; A2RU14: TMEM218; NbExp=3; IntAct=EBI-10320732, EBI-10173151;
CC Q9UGN4; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-10320732, EBI-2852148;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=IRC1a;
CC IsoId=Q9UGN4-1; Sequence=Displayed;
CC Name=2; Synonyms=IRC1c;
CC IsoId=Q9UGN4-2; Sequence=VSP_010559;
CC Name=3; Synonyms=IRC1b;
CC IsoId=Q9UGN4-3; Sequence=VSP_010558;
CC Name=4;
CC IsoId=Q9UGN4-4; Sequence=VSP_010559, VSP_041246;
CC -!- TISSUE SPECIFICITY: Expressed not only by natural killer (NK) cells but
CC also by T-cell subsets, B-cells, dendritic cells, mast cells,
CC granulocytes and monocytes. {ECO:0000269|PubMed:10540326,
CC ECO:0000269|PubMed:16339535, ECO:0000269|PubMed:9701027}.
CC -!- PTM: Phosphorylated on tyrosine. {ECO:0000269|PubMed:10540326,
CC ECO:0000269|PubMed:16339535}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6SJQ0}.
CC -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28906.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF28906.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ238323; CAB66145.1; -; mRNA.
DR EMBL; AJ010101; CAB52291.1; -; mRNA.
DR EMBL; AJ010102; CAB52292.1; -; mRNA.
DR EMBL; AJ010103; CAB52293.1; -; mRNA.
DR EMBL; AJ224864; CAB55347.1; -; mRNA.
DR EMBL; AF020314; AAD01646.1; -; mRNA.
DR EMBL; AF176991; AAF89957.1; -; Genomic_DNA.
DR EMBL; AF176985; AAF89957.1; JOINED; Genomic_DNA.
DR EMBL; AF176986; AAF89957.1; JOINED; Genomic_DNA.
DR EMBL; AF176987; AAF89957.1; JOINED; Genomic_DNA.
DR EMBL; AF176988; AAF89957.1; JOINED; Genomic_DNA.
DR EMBL; AF176989; AAF89957.1; JOINED; Genomic_DNA.
DR EMBL; AF176990; AAF89957.1; JOINED; Genomic_DNA.
DR EMBL; AF161346; AAF28906.1; ALT_SEQ; mRNA.
DR EMBL; AC079325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032352; AAH32352.1; -; mRNA.
DR CCDS; CCDS32720.1; -. [Q9UGN4-1]
DR CCDS; CCDS58590.1; -. [Q9UGN4-2]
DR CCDS; CCDS82196.1; -. [Q9UGN4-4]
DR RefSeq; NP_001243770.1; NM_001256841.1. [Q9UGN4-2]
DR RefSeq; NP_001317386.1; NM_001330457.1. [Q9UGN4-4]
DR RefSeq; NP_009192.2; NM_007261.3. [Q9UGN4-1]
DR PDB; 2Q87; X-ray; 1.70 A; A/B/C=19-125.
DR PDBsum; 2Q87; -.
DR AlphaFoldDB; Q9UGN4; -.
DR SASBDB; Q9UGN4; -.
DR SMR; Q9UGN4; -.
DR BioGRID; 116445; 7.
DR IntAct; Q9UGN4; 12.
DR STRING; 9606.ENSP00000353259; -.
DR GlyGen; Q9UGN4; 2 sites.
DR iPTMnet; Q9UGN4; -.
DR PhosphoSitePlus; Q9UGN4; -.
DR BioMuta; CD300A; -.
DR DMDM; 126302534; -.
DR jPOST; Q9UGN4; -.
DR MassIVE; Q9UGN4; -.
DR PaxDb; Q9UGN4; -.
DR PeptideAtlas; Q9UGN4; -.
DR PRIDE; Q9UGN4; -.
DR ProteomicsDB; 84246; -. [Q9UGN4-1]
DR ProteomicsDB; 84247; -. [Q9UGN4-2]
DR ProteomicsDB; 84248; -. [Q9UGN4-3]
DR ProteomicsDB; 84249; -. [Q9UGN4-4]
DR TopDownProteomics; Q9UGN4-1; -. [Q9UGN4-1]
DR Antibodypedia; 2610; 352 antibodies from 30 providers.
DR DNASU; 11314; -.
DR Ensembl; ENST00000310828.9; ENSP00000308188.5; ENSG00000167851.15. [Q9UGN4-2]
DR Ensembl; ENST00000360141.8; ENSP00000353259.3; ENSG00000167851.15. [Q9UGN4-1]
DR Ensembl; ENST00000361933.7; ENSP00000354564.3; ENSG00000167851.15. [Q9UGN4-3]
DR Ensembl; ENST00000392625.7; ENSP00000376401.3; ENSG00000167851.15. [Q9UGN4-4]
DR GeneID; 11314; -.
DR KEGG; hsa:11314; -.
DR MANE-Select; ENST00000360141.8; ENSP00000353259.3; NM_007261.4; NP_009192.2.
DR UCSC; uc002jkv.5; human. [Q9UGN4-1]
DR CTD; 11314; -.
DR DisGeNET; 11314; -.
DR GeneCards; CD300A; -.
DR HGNC; HGNC:19319; CD300A.
DR HPA; ENSG00000167851; Tissue enhanced (lymphoid).
DR MIM; 606790; gene.
DR neXtProt; NX_Q9UGN4; -.
DR OpenTargets; ENSG00000167851; -.
DR PharmGKB; PA142672149; -.
DR VEuPathDB; HostDB:ENSG00000167851; -.
DR eggNOG; ENOG502S7MA; Eukaryota.
DR GeneTree; ENSGT00940000163943; -.
DR HOGENOM; CLU_051023_0_0_1; -.
DR InParanoid; Q9UGN4; -.
DR OMA; WRMIRRH; -.
DR OrthoDB; 1494510at2759; -.
DR PhylomeDB; Q9UGN4; -.
DR TreeFam; TF334441; -.
DR PathwayCommons; Q9UGN4; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9UGN4; -.
DR BioGRID-ORCS; 11314; 9 hits in 1066 CRISPR screens.
DR ChiTaRS; CD300A; human.
DR EvolutionaryTrace; Q9UGN4; -.
DR GeneWiki; CD300A; -.
DR GenomeRNAi; 11314; -.
DR Pharos; Q9UGN4; Tbio.
DR PRO; PR:Q9UGN4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UGN4; protein.
DR Bgee; ENSG00000167851; Expressed in granulocyte and 145 other tissues.
DR ExpressionAtlas; Q9UGN4; baseline and differential.
DR Genevisible; Q9UGN4; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IDA:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:1902569; P:negative regulation of activation of Janus kinase activity; IDA:UniProtKB.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:UniProtKB.
DR GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:1902567; P:negative regulation of eosinophil activation; IDA:UniProtKB.
DR GO; GO:2000417; P:negative regulation of eosinophil migration; IDA:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; IDA:UniProtKB.
DR GO; GO:0043305; P:negative regulation of mast cell degranulation; IDA:UniProtKB.
DR GO; GO:0034125; P:negative regulation of MyD88-dependent toll-like receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:1902564; P:negative regulation of neutrophil activation; IDA:UniProtKB.
DR GO; GO:0051134; P:negative regulation of NK T cell activation; IDA:UniProtKB.
DR GO; GO:0060101; P:negative regulation of phagocytosis, engulfment; IMP:UniProtKB.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
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; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..299
FT /note="CMRF35-like molecule 8"
FT /id="PRO_0000014682"
FT TOPO_DOM 18..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..123
FT /note="Ig-like V-type"
FT REGION 278..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 293
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6SJQ0"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 14..209
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010558"
FT VAR_SEQ 14..126
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.5"
FT /id="VSP_010559"
FT VAR_SEQ 223..258
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_041246"
FT VARIANT 111
FT /note="R -> Q (in dbSNP:rs2272111)"
FT /evidence="ECO:0000269|PubMed:12483297, ECO:0000269|Ref.2"
FT /id="VAR_030797"
FT CONFLICT 28..29
FT /note="VG -> W (in Ref. 3; AAD01646 and 4; AAF89957)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="E -> Q (in Ref. 4; AAF89957)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="L -> M (in Ref. 5; AAF28906)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="L -> M (in Ref. 5; AAF28906)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="K -> KWIK (in Ref. 3; AAD01646)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="S -> F (in Ref. 5; AAF28906)"
FT /evidence="ECO:0000305"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:2Q87"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2Q87"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2Q87"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:2Q87"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2Q87"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2Q87"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2Q87"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2Q87"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2Q87"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:2Q87"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2Q87"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:2Q87"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:2Q87"
SQ SEQUENCE 299 AA; 33201 MW; 978461DA87E86269 CRC64;
MWLPWALLLL WVPGCFALSK CRTVAGPVGG SLSVQCPYEK EHRTLNKYWC RPPQIFLCDK
IVETKGSAGK RNGRVSIRDS PANLSFTVTL ENLTEEDAGT YWCGVDTPWL RDFHDPVVEV
EVSVFPASTS MTPASITAAK TSTITTAFPP VSSTTLFAVG ATHSASIQEE TEEVVNSQLP
LLLSLLALLL LLLVGASLLA WRMFQKWIKA GDHSELSQNP KQAATQSELH YANLELLMWP
LQEKPAPPRE VEVEYSTVAS PREELHYASV VFDSNTNRIA AQRPREEEPD SDYSVIRKT
