CLM9_HUMAN
ID CLM9_HUMAN Reviewed; 332 AA.
AC Q6UXG3; B4DNY5; F5H7P9; F8W9M3; Q8IX38; Q8IX39; Q8TA95;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=CMRF35-like molecule 9;
DE Short=CLM-9;
DE AltName: Full=CD300 antigen-like family member G;
DE AltName: Full=Triggering receptor expressed on myeloid cells 4;
DE Short=TREM-4;
DE AltName: CD_antigen=CD300g;
DE Flags: Precursor;
GN Name=CD300LG; Synonyms=CLM9, TREM4; ORFNames=UNQ422/PRO846;
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] (ISOFORMS 2 AND 3).
RA Colonna M.;
RT "Triggering receptor expressed on myeloid cells 4.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND VARIANT
RP ALA-228.
RC TISSUE=Lung, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-221.
RC TISSUE=Testis;
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 [6]
RP PROTEIN SEQUENCE OF 19-33.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3).
RX PubMed=16876123; DOI=10.1016/j.bbrc.2006.07.047;
RA Takatsu H., Hase K., Ohmae M., Ohshima S., Hashimoto K., Taniura N.,
RA Yamamoto A., Ohno H.;
RT "CD300 antigen like family member G: a novel Ig receptor like protein
RT exclusively expressed on capillary endothelium.";
RL Biochem. Biophys. Res. Commun. 348:183-191(2006).
CC -!- FUNCTION: Receptor which may mediate L-selectin-dependent lymphocyte
CC rollings. Binds SELL in a calcium dependent manner. Binds lymphocyte
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q6UXG3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10254587, EBI-3867333;
CC Q6UXG3; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-10254587, EBI-11959885;
CC Q6UXG3; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-10254587, EBI-10172052;
CC Q6UXG3; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-10254587, EBI-11987425;
CC Q6UXG3; P21145: MAL; NbExp=3; IntAct=EBI-10254587, EBI-3932027;
CC Q6UXG3; P55061: TMBIM6; NbExp=3; IntAct=EBI-10254587, EBI-1045825;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q1ERP8}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q1ERP8}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q1ERP8}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q1ERP8}. Endosome, multivesicular body membrane
CC {ECO:0000250|UniProtKB:Q1ERP8}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q1ERP8}. Note=Transcytoses across the cytoplasm.
CC {ECO:0000250|UniProtKB:Q1ERP8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=CD300LG-gamma;
CC IsoId=Q6UXG3-1; Sequence=Displayed;
CC Name=2; Synonyms=TREM4-alpha, CD300LG-alpha 1;
CC IsoId=Q6UXG3-2; Sequence=VSP_028410, VSP_028411;
CC Name=3; Synonyms=TREM4-beta, CD300LG-alpha 2;
CC IsoId=Q6UXG3-3; Sequence=VSP_028410, VSP_028412;
CC Name=4;
CC IsoId=Q6UXG3-4; Sequence=VSP_028412;
CC Name=5;
CC IsoId=Q6UXG3-5; Sequence=VSP_045362, VSP_028412;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and
CC placenta. {ECO:0000269|PubMed:16876123}.
CC -!- DOMAIN: Ig-like V-type domain mediates binding to lymphocyte.
CC {ECO:0000250}.
CC -!- PTM: O-glycosylated with sialylated oligosaccharides. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
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DR EMBL; AF427619; AAN86134.1; -; mRNA.
DR EMBL; AF427620; AAN86135.1; -; mRNA.
DR EMBL; AY358364; AAQ88730.1; -; mRNA.
DR EMBL; AK298112; BAG60397.1; -; mRNA.
DR EMBL; AK309938; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC007993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025395; AAH25395.1; -; mRNA.
DR CCDS; CCDS11470.1; -. [Q6UXG3-1]
DR CCDS; CCDS54131.1; -. [Q6UXG3-4]
DR CCDS; CCDS54132.1; -. [Q6UXG3-5]
DR CCDS; CCDS54133.1; -. [Q6UXG3-2]
DR RefSeq; NP_001161794.1; NM_001168322.1. [Q6UXG3-4]
DR RefSeq; NP_001161795.1; NM_001168323.1. [Q6UXG3-5]
DR RefSeq; NP_001161796.1; NM_001168324.1. [Q6UXG3-2]
DR RefSeq; NP_660316.2; NM_145273.3. [Q6UXG3-1]
DR AlphaFoldDB; Q6UXG3; -.
DR SMR; Q6UXG3; -.
DR BioGRID; 127023; 7.
DR IntAct; Q6UXG3; 6.
DR STRING; 9606.ENSP00000321005; -.
DR GlyGen; Q6UXG3; 26 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q6UXG3; -.
DR PhosphoSitePlus; Q6UXG3; -.
DR BioMuta; CD300LG; -.
DR DMDM; 296434455; -.
DR jPOST; Q6UXG3; -.
DR MassIVE; Q6UXG3; -.
DR PaxDb; Q6UXG3; -.
DR PeptideAtlas; Q6UXG3; -.
DR PRIDE; Q6UXG3; -.
DR ProteomicsDB; 27553; -.
DR ProteomicsDB; 30350; -.
DR ProteomicsDB; 67609; -. [Q6UXG3-1]
DR ProteomicsDB; 67610; -. [Q6UXG3-2]
DR ProteomicsDB; 67611; -. [Q6UXG3-3]
DR Antibodypedia; 1022; 119 antibodies from 21 providers.
DR DNASU; 146894; -.
DR Ensembl; ENST00000293396.12; ENSP00000293396.7; ENSG00000161649.13. [Q6UXG3-2]
DR Ensembl; ENST00000317310.5; ENSP00000321005.3; ENSG00000161649.13. [Q6UXG3-1]
DR Ensembl; ENST00000377203.8; ENSP00000366408.3; ENSG00000161649.13. [Q6UXG3-5]
DR Ensembl; ENST00000539718.5; ENSP00000442368.1; ENSG00000161649.13. [Q6UXG3-4]
DR Ensembl; ENST00000586233.5; ENSP00000468800.1; ENSG00000161649.13. [Q6UXG3-3]
DR GeneID; 146894; -.
DR KEGG; hsa:146894; -.
DR MANE-Select; ENST00000317310.5; ENSP00000321005.3; NM_145273.4; NP_660316.2.
DR UCSC; uc002iel.3; human. [Q6UXG3-1]
DR CTD; 146894; -.
DR DisGeNET; 146894; -.
DR GeneCards; CD300LG; -.
DR HGNC; HGNC:30455; CD300LG.
DR HPA; ENSG00000161649; Tissue enhanced (adipose tissue, breast, placenta).
DR MIM; 610520; gene.
DR neXtProt; NX_Q6UXG3; -.
DR OpenTargets; ENSG00000161649; -.
DR PharmGKB; PA142672154; -.
DR VEuPathDB; HostDB:ENSG00000161649; -.
DR eggNOG; ENOG502SURU; Eukaryota.
DR GeneTree; ENSGT00940000162429; -.
DR HOGENOM; CLU_051023_1_0_1; -.
DR InParanoid; Q6UXG3; -.
DR OMA; YAGEEGQ; -.
DR OrthoDB; 1494510at2759; -.
DR PhylomeDB; Q6UXG3; -.
DR TreeFam; TF334441; -.
DR PathwayCommons; Q6UXG3; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q6UXG3; -.
DR BioGRID-ORCS; 146894; 12 hits in 1065 CRISPR screens.
DR GenomeRNAi; 146894; -.
DR Pharos; Q6UXG3; Tbio.
DR PRO; PR:Q6UXG3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6UXG3; protein.
DR Bgee; ENSG00000161649; Expressed in adipose tissue of abdominal region and 149 other tissues.
DR ExpressionAtlas; Q6UXG3; baseline and differential.
DR Genevisible; Q6UXG3; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
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 Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Endosome; Glycoprotein; Immunity; Immunoglobulin domain;
KW Membrane; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 19..332
FT /note="CMRF35-like molecule 9"
FT /id="PRO_0000306112"
FT TOPO_DOM 19..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..121
FT /note="Ig-like V-type"
FT REGION 146..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT DISULFID 37..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 127..211
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028410"
FT VAR_SEQ 127..161
FT /note="GPCCPPSPSPTFQPLATTRLQPKAKAQQTQPPGLT -> A (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045362"
FT VAR_SEQ 296..332
FT /note="TAEEKEAPSQAPEGDVISMPPLHTSEEELGFSKFVSA -> NHRTSELDPDE
FT AFEISSLTFLSV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028411"
FT VAR_SEQ 296..332
FT /note="TAEEKEAPSQAPEGDVISMPPLHTSEEELGFSKFVSA -> NSLMFSLSLPW
FT L (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_028412"
FT VARIANT 221
FT /note="D -> N (in dbSNP:rs17852267)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035261"
FT VARIANT 228
FT /note="T -> A (in dbSNP:rs12453522)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_035262"
FT CONFLICT 10
FT /note="C -> W (in Ref. 1; AAN86134/AAN86135)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="D -> G (in Ref. 1; AAN86134/AAN86135)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="T -> H (in Ref. 1; AAN86134/AAN86135)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="V -> L (in Ref. 1; AAN86134/AAN86135)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="G -> A (in Ref. 1; AAN86134/AAN86135)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="C -> W (in Ref. 2; AAQ88730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 36060 MW; 2347FF0FA55515FB CRC64;
MRLLVLLWGC LLLPGYEALE GPEEISGFEG DTVSLQCTYR EELRDHRKYW CRKGGILFSR
CSGTIYAEEE GQETMKGRVS IRDSRQELSL IVTLWNLTLQ DAGEYWCGVE KRGPDESLLI
SLFVFPGPCC PPSPSPTFQP LATTRLQPKA KAQQTQPPGL TSPGLYPAAT TAKQGKTGAE
APPLPGTSQY GHERTSQYTG TSPHPATSPP AGSSRPPMQL DSTSAEDTSP ALSSGSSKPR
VSIPMVRILA PVLVLLSLLS AAGLIAFCSH LLLWRKEAQQ ATETQRNEKF CLSRLTAEEK
EAPSQAPEGD VISMPPLHTS EEELGFSKFV SA
