MUC18_HUMAN
ID MUC18_HUMAN Reviewed; 646 AA.
AC P43121; O95812; Q59E86; Q6PHR3; Q6ZTR2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Cell surface glycoprotein MUC18;
DE AltName: Full=Cell surface glycoprotein P1H12;
DE AltName: Full=Melanoma cell adhesion molecule;
DE AltName: Full=Melanoma-associated antigen A32;
DE AltName: Full=Melanoma-associated antigen MUC18;
DE AltName: Full=S-endo 1 endothelial-associated antigen;
DE AltName: CD_antigen=CD146;
DE Flags: Precursor;
GN Name=MCAM; Synonyms=MUC18;
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).
RC TISSUE=Melanoma;
RX PubMed=2602381; DOI=10.1073/pnas.86.24.9891;
RA Lehmann J.M., Riethmueller G., Johnson J.P.;
RT "MUC18, a marker of tumor progression in human melanoma, shows sequence
RT similarity to the neural cell adhesion molecules of the immunoglobulin
RT superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9891-9895(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND SEQUENCE
RP REVISION.
RC TISSUE=Melanoma;
RX PubMed=8378324; DOI=10.1073/pnas.90.18.8514;
RA Sers C., Kirsch K., Rothbaecher U., Riethmueller G., Johnson J.P.;
RT "Genomic organization of the melanoma-associated glycoprotein MUC18:
RT implications for the evolution of the immunoglobulin domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8514-8518(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11709656; DOI=10.1067/mlc.2001.118519;
RA Solovey A.N., Gui L., Chang L., Enenstein J., Browne P.V., Hebbel R.P.;
RT "Identification and functional assessment of endothelial P1H12.";
RL J. Lab. Clin. Med. 138:322-331(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-89.
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=PNS;
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 24-44; 98-112; 135-153; 240-260; 379-389 AND 460-478.
RX PubMed=8162602;
RA Shih I.-M., Eleder D.E., Speicher D., Johnson J.P., Herlyn M.;
RT "Isolation and functional characterization of the A32 melanoma-associated
RT antigen.";
RL Cancer Res. 54:2514-2520(1994).
RN [8]
RP PROTEIN SEQUENCE OF 27-40; 98-112 AND 236-260.
RX PubMed=8573133; DOI=10.1006/bbrc.1996.0037;
RA Bardin N., Frances V., Lesaule G., Horschowski N., George F., Sampol J.;
RT "Identification of the S-endo 1 endothelial-associated antigen.";
RL Biochem. Biophys. Res. Commun. 218:210-216(1996).
RN [9]
RP FUNCTION.
RX PubMed=8292890; DOI=10.1097/00008390-199310000-00006;
RA Johnson J.P., Rothbacher U., Sers C.;
RT "The progression associated antigen MUC18: a unique member of the
RT immunoglobulin supergene family.";
RL Melanoma Res. 3:337-340(1993).
RN [10]
RP FUNCTION.
RX PubMed=11036077; DOI=10.1074/jbc.m007065200;
RA Anfosso F., Bardin N., Vivier E., Sabatier F., Sampol J., Dignat-George F.;
RT "Outside-in signaling pathway linked to CD146 engagement in human
RT endothelial cells.";
RL J. Biol. Chem. 276:1564-1569(2001).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-467.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614 AND SER-628, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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).
CC -!- FUNCTION: Plays a role in cell adhesion, and in cohesion of the
CC endothelial monolayer at intercellular junctions in vascular tissue.
CC Its expression may allow melanoma cells to interact with cellular
CC elements of the vascular system, thereby enhancing hematogeneous tumor
CC spread. Could be an adhesion molecule active in neural crest cells
CC during embryonic development. Acts as surface receptor that triggers
CC tyrosine phosphorylation of FYN and PTK2/FAK1, and a transient increase
CC in the intracellular calcium concentration.
CC {ECO:0000269|PubMed:11036077, ECO:0000269|PubMed:8292890}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43121-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43121-2; Sequence=VSP_016938, VSP_016939;
CC -!- TISSUE SPECIFICITY: Detected in endothelial cells in vascular tissue
CC throughout the body. May appear at the surface of neural crest cells
CC during their embryonic migration. Appears to be limited to vascular
CC smooth muscle in normal adult tissues. Associated with tumor
CC progression and the development of metastasis in human malignant
CC melanoma. Expressed most strongly on metastatic lesions and advanced
CC primary tumors and is only rarely detected in benign melanocytic nevi
CC and thin primary melanomas with a low probability of metastasis.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93162.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MCAMID41314ch11q23.html";
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DR EMBL; M29277; AAA20824.1; -; mRNA.
DR EMBL; M28882; AAA20922.1; -; mRNA.
DR EMBL; X68264; CAA48332.1; -; Genomic_DNA.
DR EMBL; X68265; CAA48332.1; JOINED; Genomic_DNA.
DR EMBL; X68266; CAA48332.1; JOINED; Genomic_DNA.
DR EMBL; X68267; CAA48332.1; JOINED; Genomic_DNA.
DR EMBL; X68268; CAA48332.1; JOINED; Genomic_DNA.
DR EMBL; X68270; CAA48332.1; JOINED; Genomic_DNA.
DR EMBL; X68271; CAA48332.1; JOINED; Genomic_DNA.
DR EMBL; AF089868; AAD17799.1; -; mRNA.
DR EMBL; AK126303; BAC86520.1; -; mRNA.
DR EMBL; AB209925; BAD93162.1; ALT_INIT; mRNA.
DR EMBL; BC056418; AAH56418.1; -; mRNA.
DR CCDS; CCDS31690.1; -. [P43121-1]
DR PIR; I38049; I38049.
DR RefSeq; NP_006491.2; NM_006500.2. [P43121-1]
DR PDB; 6LYN; X-ray; 2.78 A; C/D=336-519.
DR PDBsum; 6LYN; -.
DR AlphaFoldDB; P43121; -.
DR SMR; P43121; -.
DR BioGRID; 110332; 84.
DR DIP; DIP-52791N; -.
DR IntAct; P43121; 27.
DR MINT; P43121; -.
DR STRING; 9606.ENSP00000264036; -.
DR ChEMBL; CHEMBL3712863; -.
DR GuidetoPHARMACOLOGY; 2988; -.
DR GlyConnect; 1104; 2 N-Linked glycans (2 sites).
DR GlyGen; P43121; 9 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P43121; -.
DR PhosphoSitePlus; P43121; -.
DR SwissPalm; P43121; -.
DR BioMuta; MCAM; -.
DR DMDM; 85681878; -.
DR EPD; P43121; -.
DR jPOST; P43121; -.
DR MassIVE; P43121; -.
DR MaxQB; P43121; -.
DR PaxDb; P43121; -.
DR PeptideAtlas; P43121; -.
DR PRIDE; P43121; -.
DR ProteomicsDB; 55589; -. [P43121-1]
DR ProteomicsDB; 55590; -. [P43121-2]
DR ABCD; P43121; 2 sequenced antibodies.
DR Antibodypedia; 2244; 1987 antibodies from 47 providers.
DR DNASU; 4162; -.
DR Ensembl; ENST00000264036.6; ENSP00000264036.4; ENSG00000076706.17. [P43121-1]
DR GeneID; 4162; -.
DR KEGG; hsa:4162; -.
DR MANE-Select; ENST00000264036.6; ENSP00000264036.4; NM_006500.3; NP_006491.2.
DR UCSC; uc001pwf.4; human. [P43121-1]
DR CTD; 4162; -.
DR DisGeNET; 4162; -.
DR GeneCards; MCAM; -.
DR HGNC; HGNC:6934; MCAM.
DR HPA; ENSG00000076706; Low tissue specificity.
DR MIM; 155735; gene.
DR neXtProt; NX_P43121; -.
DR OpenTargets; ENSG00000076706; -.
DR PharmGKB; PA30678; -.
DR VEuPathDB; HostDB:ENSG00000076706; -.
DR eggNOG; ENOG502QV1U; Eukaryota.
DR GeneTree; ENSGT00940000155838; -.
DR HOGENOM; CLU_028888_3_0_1; -.
DR InParanoid; P43121; -.
DR OMA; RCMASVP; -.
DR PhylomeDB; P43121; -.
DR TreeFam; TF330534; -.
DR PathwayCommons; P43121; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; P43121; -.
DR BioGRID-ORCS; 4162; 10 hits in 1082 CRISPR screens.
DR ChiTaRS; MCAM; human.
DR GeneWiki; CD146; -.
DR GenomeRNAi; 4162; -.
DR Pharos; P43121; Tbio.
DR PRO; PR:P43121; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P43121; protein.
DR Bgee; ENSG00000076706; Expressed in blood vessel layer and 207 other tissues.
DR ExpressionAtlas; P43121; baseline and differential.
DR Genevisible; P43121; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0001525; P:angiogenesis; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0003094; P:glomerular filtration; IEP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0061042; P:vascular wound healing; IEP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 5.
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; 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; PF00047; ig; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:8162602"
FT CHAIN 24..646
FT /note="Cell surface glycoprotein MUC18"
FT /id="PRO_0000014891"
FT TOPO_DOM 24..559
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 584..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..129
FT /note="Ig-like V-type 1"
FT DOMAIN 139..242
FT /note="Ig-like V-type 2"
FT DOMAIN 244..330
FT /note="Ig-like C2-type 1"
FT DOMAIN 335..424
FT /note="Ig-like C2-type 2"
FT DOMAIN 430..510
FT /note="Ig-like C2-type 3"
FT REGION 278..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R2Y2"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..116
FT /evidence="ECO:0000305"
FT DISULFID 161..223
FT /evidence="ECO:0000305"
FT DISULFID 272..320
FT /evidence="ECO:0000305"
FT DISULFID 365..407
FT /evidence="ECO:0000305"
FT DISULFID 452..499
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..187
FT /note="MGLPRLVCAFLLAACCCCPRVAGVPGEAEQPAPELVEVEVGSTALLKCGLSQ
FT SQGNLSHVDWFSVHKEKRTLIFRVRQGQGQSEPGEYEQRLSLQDRGATLALTQVTPQDE
FT RIFLCQGKRPRSQEYRIQLRVYKAPEEPNIQVNPLGIPVNSKEPEEVATCVGRNGYPIP
FT QVIWYKNGRPLKEEKNR -> MVYIVRQFLLYNVSGSVYLDQLIVLLTAKFSILRIAGS
FT RVHHSPFSGHLDGCSFLSLQHSLHTSLDMSRHENVFLGLTLSSKSAGLKGFQLAFVPGL
FT LQGTGGYLDGPLPTPVDNPRVGLEVGLRLSLPPLPPCPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016938"
FT VAR_SEQ 549..646
FT /note="ERKLPEPESRGVVIVAVIVCILVLAVLGAVLYFLYKKGKLPCRRSGKQEITL
FT PPSRKSELVVEVKSDKLPEEMGLLQGSSGDKRAPGDQGEKYIDLRH -> GKPGLAREQ
FT GCARASFLPCPSPESPVQKGE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016939"
FT VARIANT 89
FT /note="E -> G (in dbSNP:rs34587557)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_049915"
FT CONFLICT 322..324
FT /note="GLD -> AWN (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="G -> D (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 424..425
FT /note="NV -> KL (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="S -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 343..352
FT /evidence="ECO:0007829|PDB:6LYN"
FT STRAND 361..371
FT /evidence="ECO:0007829|PDB:6LYN"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:6LYN"
FT STRAND 382..394
FT /evidence="ECO:0007829|PDB:6LYN"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6LYN"
FT STRAND 403..410
FT /evidence="ECO:0007829|PDB:6LYN"
FT STRAND 418..427
FT /evidence="ECO:0007829|PDB:6LYN"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:6LYN"
FT STRAND 436..441
FT /evidence="ECO:0007829|PDB:6LYN"
FT STRAND 447..458
FT /evidence="ECO:0007829|PDB:6LYN"
FT STRAND 461..468
FT /evidence="ECO:0007829|PDB:6LYN"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:6LYN"
FT STRAND 479..487
FT /evidence="ECO:0007829|PDB:6LYN"
FT HELIX 490..495
FT /evidence="ECO:0007829|PDB:6LYN"
FT STRAND 497..503
FT /evidence="ECO:0007829|PDB:6LYN"
FT STRAND 506..515
FT /evidence="ECO:0007829|PDB:6LYN"
SQ SEQUENCE 646 AA; 71607 MW; E46CB8AC7BA0738E CRC64;
MGLPRLVCAF LLAACCCCPR VAGVPGEAEQ PAPELVEVEV GSTALLKCGL SQSQGNLSHV
DWFSVHKEKR TLIFRVRQGQ GQSEPGEYEQ RLSLQDRGAT LALTQVTPQD ERIFLCQGKR
PRSQEYRIQL RVYKAPEEPN IQVNPLGIPV NSKEPEEVAT CVGRNGYPIP QVIWYKNGRP
LKEEKNRVHI QSSQTVESSG LYTLQSILKA QLVKEDKDAQ FYCELNYRLP SGNHMKESRE
VTVPVFYPTE KVWLEVEPVG MLKEGDRVEI RCLADGNPPP HFSISKQNPS TREAEEETTN
DNGVLVLEPA RKEHSGRYEC QGLDLDTMIS LLSEPQELLV NYVSDVRVSP AAPERQEGSS
LTLTCEAESS QDLEFQWLRE ETGQVLERGP VLQLHDLKRE AGGGYRCVAS VPSIPGLNRT
QLVNVAIFGP PWMAFKERKV WVKENMVLNL SCEASGHPRP TISWNVNGTA SEQDQDPQRV
LSTLNVLVTP ELLETGVECT ASNDLGKNTS ILFLELVNLT TLTPDSNTTT GLSTSTASPH
TRANSTSTER KLPEPESRGV VIVAVIVCIL VLAVLGAVLY FLYKKGKLPC RRSGKQEITL
PPSRKSELVV EVKSDKLPEE MGLLQGSSGD KRAPGDQGEK YIDLRH
