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Macrophage mannose receptor 1 (MMR) (C-type lectin domain family 13 member D) (C-type lectin domain family 13 member D-like) (Human mannose receptor) (hMR) (Macrophage mannose receptor 1-like protein 1) (CD antigen CD206)

 MRC1_HUMAN              Reviewed;        1456 AA.
P22897; A5PKW3; Q5VSJ2; Q5VSK2;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
22-NOV-2017, entry version 199.
RecName: Full=Macrophage mannose receptor 1;
Short=MMR;
AltName: Full=C-type lectin domain family 13 member D;
AltName: Full=C-type lectin domain family 13 member D-like;
AltName: Full=Human mannose receptor;
Short=hMR;
AltName: Full=Macrophage mannose receptor 1-like protein 1;
AltName: CD_antigen=CD206;
Flags: Precursor;
Name=MRC1; Synonyms=CLEC13D, CLEC13DL, MRC1L1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Placenta;
PubMed=2373685;
Taylor M.E., Conary J.T., Lennartz M.R., Stahl P.D., Drickamer K.;
"Primary structure of the mannose receptor contains multiple motifs
resembling carbohydrate-recognition domains.";
J. Biol. Chem. 265:12156-12162(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2258707; DOI=10.1084/jem.172.6.1785;
Ezekowitz R.A., Sastry K., Bailly P., Warner A.;
"Molecular characterization of the human macrophage mannose receptor:
demonstration of multiple carbohydrate recognition-like domains and
phagocytosis of yeasts in Cos-1 cells.";
J. Exp. Med. 172:1785-1794(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1294118; DOI=10.1016/S0888-7543(05)80174-0;
Kim S.J., Ruiz N., Bezouska K., Drickamer K.;
"Organization of the gene encoding the human macrophage mannose
receptor (MRC1).";
Genomics 14:721-727(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
SER-396; ALA-399 AND PHE-407.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
STUDIES ON THE BINDING OF INDIVIDUAL LECTIN DOMAINS.
PubMed=1730714;
Taylor M.E., Bezouska K., Drickamer K.;
"Contribution to ligand binding by multiple carbohydrate-recognition
domains in the macrophage mannose receptor.";
J. Biol. Chem. 267:1719-1726(1992).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1205.
TISSUE=Milk;
PubMed=18780401; DOI=10.1002/pmic.200701057;
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic
interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
[9]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH DENGUE VIRUS
ENVELOPE PROTEIN E.
PubMed=18266465; DOI=10.1371/journal.ppat.0040017;
Miller J.L., de Wet B.J., deWet B.J., Martinez-Pomares L.,
Radcliffe C.M., Dwek R.A., Rudd P.M., Gordon S.;
"The mannose receptor mediates dengue virus infection of
macrophages.";
PLoS Pathog. 4:E17-E17(2008).
[10]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HEPATITIS B VIRUS
ENVELOPE PROTEIN.
PubMed=19683778; DOI=10.1016/j.virol.2009.07.015;
Op den Brouw M.L., Binda R.S., Geijtenbeek T.B., Janssen H.L.,
Woltman A.M.;
"The mannose receptor acts as hepatitis B virus surface antigen
receptor mediating interaction with intrahepatic dendritic cells.";
Virology 393:84-90(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 642-788.
PubMed=10779515; DOI=10.1074/jbc.M002366200;
Feinberg H., Park-Snyder S., Kolatkar A.R., Heise C.T., Taylor M.E.,
Weis W.I.;
"Structure of a C-type carbohydrate recognition domain from the
macrophage mannose receptor.";
J. Biol. Chem. 275:21539-21548(2000).
[13]
POLYMORPHISM, POSSIBLE ASSOCIATION OF VARIANT SER-396 WITH RESISTANCE
TO LEPROSY, VARIANTS ILE-167; ALA-399 AND PHE-407, AND SUBCELLULAR
LOCATION.
PubMed=20035344; DOI=10.1007/s00439-009-0775-x;
Alter A., de Leseleuc L., Van Thuc N., Thai V.H., Huong N.T., Ba N.N.,
Cardoso C.C., Grant A.V., Abel L., Moraes M.O., Alcais A., Schurr E.;
"Genetic and functional analysis of common MRC1 exon 7 polymorphisms
in leprosy susceptibility.";
Hum. Genet. 127:337-348(2010).
-!- FUNCTION: Mediates the endocytosis of glycoproteins by
macrophages. Binds both sulfated and non-sulfated polysaccharide
chains.
-!- FUNCTION: (Microbial infection) Acts as phagocytic receptor for
bacteria, fungi and other pathogens. Acts as a receptor for Dengue
virus envelope protein E (PubMed:18266465). Interacts with
hepatitis B virus envelope protein (PubMed:19683778).
{ECO:0000269|PubMed:18266465, ECO:0000269|PubMed:19683778}.
-!- SUBUNIT: (Microbial infection) Interacts with Dengue virus.
{ECO:0000269|PubMed:18266465}.
-!- SUBUNIT: (Microbial infection) May act as a receptor for hepatitis
B virus, enabling uptake of the virus in hepatic dendritic cells.
{ECO:0000269|PubMed:19683778}.
-!- SUBCELLULAR LOCATION: Endosome membrane
{ECO:0000269|PubMed:20035344}; Single-pass type I membrane protein
{ECO:0000269|PubMed:20035344}. Cell membrane
{ECO:0000269|PubMed:20035344}; Single-pass type I membrane protein
{ECO:0000269|PubMed:20035344}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P22897-1; Sequence=Displayed;
Name=2;
IsoId=P22897-2; Sequence=VSP_041340, VSP_041341;
Note=No experimental confirmation available.;
-!- POLYMORPHISM: Genetic variations in MRC1 may influence
susceptibility or resistance to leprosy in some populations.
Particularly, Gly-396 seems to be a risk factor for leprosy when
associated with Ala-399 and Phe-407.
-!- MISCELLANEOUS: CRDs 1-3 have at most very weak affinity for
carbohydrate. CRD 4 shows the highest affinity binding and has
multispecificity for a variety of monosaccharides. At least 3 CRDs
(4, 5, and 7) are required for high affinity binding and
endocytosis of multivalent glycoconjugates.
-!- SEQUENCE CAUTION:
Sequence=CAH70733.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH70872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH71176.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI15339.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Macrophage mannose receptor;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_00127";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MRC1ID44561ch10p12.html";
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EMBL; J05550; AAA59868.1; -; mRNA.
EMBL; X55635; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M93221; AAA60389.1; -; Genomic_DNA.
EMBL; M93192; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93193; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93194; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93195; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93196; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93197; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93198; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93199; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93200; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93201; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93202; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93203; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93204; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93205; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93206; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93207; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93208; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93209; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93210; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93211; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93212; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93213; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93214; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93215; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93216; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93217; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93218; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93219; AAA60389.1; JOINED; Genomic_DNA.
EMBL; M93220; AAA60389.1; JOINED; Genomic_DNA.
EMBL; EF444997; ACA06020.1; -; Genomic_DNA.
EMBL; AL928729; CAH70733.1; ALT_SEQ; Genomic_DNA.
EMBL; AC069023; CAH70733.1; JOINED; Genomic_DNA.
EMBL; AL139238; CAH70872.1; ALT_SEQ; Genomic_DNA.
EMBL; AL928580; CAH70872.1; JOINED; Genomic_DNA.
EMBL; BX255924; CAH70872.1; JOINED; Genomic_DNA.
EMBL; AL928580; CAH71176.1; ALT_SEQ; Genomic_DNA.
EMBL; AL139238; CAH71176.1; JOINED; Genomic_DNA.
EMBL; BX255924; CAH71176.1; JOINED; Genomic_DNA.
EMBL; BX255924; CAI15339.1; ALT_SEQ; Genomic_DNA.
EMBL; AL139238; CAI15339.1; JOINED; Genomic_DNA.
EMBL; AL928580; CAI15339.1; JOINED; Genomic_DNA.
EMBL; BC142642; AAI42643.1; -; mRNA.
CCDS; CCDS7123.2; -. [P22897-1]
PIR; A36563; A36563.
RefSeq; NP_002429.1; NM_002438.3. [P22897-1]
UniGene; Hs.743903; -.
UniGene; Hs.75182; -.
PDB; 1EGG; X-ray; 2.30 A; A/B=644-787.
PDB; 1EGI; X-ray; 2.30 A; A/B=644-787.
PDBsum; 1EGG; -.
PDBsum; 1EGI; -.
ProteinModelPortal; P22897; -.
SMR; P22897; -.
BioGrid; 110500; 1.
DIP; DIP-101N; -.
IntAct; P22897; 2.
MINT; MINT-2801902; -.
STRING; 9606.ENSP00000239761; -.
BindingDB; P22897; -.
ChEMBL; CHEMBL2176854; -.
iPTMnet; P22897; -.
PhosphoSitePlus; P22897; -.
DMDM; 126730; -.
EPD; P22897; -.
PaxDb; P22897; -.
PeptideAtlas; P22897; -.
PRIDE; P22897; -.
Ensembl; ENST00000569591; ENSP00000455897; ENSG00000260314. [P22897-1]
GeneID; 4360; -.
KEGG; hsa:4360; -.
UCSC; uc031ptj.2; human. [P22897-1]
CTD; 4360; -.
DisGeNET; 4360; -.
EuPathDB; HostDB:ENSG00000260314.2; -.
GeneCards; MRC1; -.
H-InvDB; HIX0035369; -.
HGNC; HGNC:7228; MRC1.
HPA; CAB068203; -.
HPA; HPA004114; -.
HPA; HPA045134; -.
MIM; 153618; gene.
neXtProt; NX_P22897; -.
OpenTargets; ENSG00000260314; -.
PharmGKB; PA134941260; -.
PharmGKB; PA30933; -.
eggNOG; ENOG410IS47; Eukaryota.
eggNOG; ENOG410XRS3; LUCA.
GeneTree; ENSGT00720000108514; -.
HOGENOM; HOG000113647; -.
HOVERGEN; HBG107130; -.
InParanoid; P22897; -.
KO; K06560; -.
OMA; ANEDENC; -.
OrthoDB; EOG091G0EGC; -.
PhylomeDB; P22897; -.
TreeFam; TF316663; -.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
SIGNOR; P22897; -.
EvolutionaryTrace; P22897; -.
GenomeRNAi; 4360; -.
PRO; PR:P22897; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000260314; -.
CleanEx; HS_MRC1; -.
Genevisible; P22897; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005537; F:mannose binding; TAS:ProtInc.
GO; GO:0004872; F:receptor activity; IDA:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
CDD; cd00062; FN2; 1.
CDD; cd00161; RICIN; 1.
Gene3D; 2.10.10.10; -; 1.
Gene3D; 3.10.100.10; -; 8.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR000562; FN_type2_dom.
InterPro; IPR036943; FN_type2_sf.
InterPro; IPR013806; Kringle-like.
InterPro; IPR035992; Ricin_B-like_lectins.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00040; fn2; 1.
Pfam; PF00059; Lectin_C; 8.
Pfam; PF00652; Ricin_B_lectin; 1.
SMART; SM00034; CLECT; 8.
SMART; SM00059; FN2; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF56436; SSF56436; 8.
SUPFAM; SSF57440; SSF57440; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 6.
PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
PROSITE; PS00023; FN2_1; 1.
PROSITE; PS51092; FN2_2; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Endocytosis; Endosome; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction; Lectin;
Membrane; Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 1456 Macrophage mannose receptor 1.
/FTId=PRO_0000017548.
TOPO_DOM 19 1389 Extracellular. {ECO:0000255}.
TRANSMEM 1390 1410 Helical. {ECO:0000255}.
TOPO_DOM 1411 1456 Cytoplasmic. {ECO:0000255}.
DOMAIN 22 142 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
DOMAIN 163 211 Fibronectin type-II.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 225 341 C-type lectin 1. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 369 487 C-type lectin 2. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 511 626 C-type lectin 3. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 655 778 C-type lectin 4. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 807 923 C-type lectin 5. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 952 1080 C-type lectin 6. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 1102 1213 C-type lectin 7. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 1241 1356 C-type lectin 8. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 344 344 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 529 529 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 926 926 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 930 930 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1160 1160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1205 1205 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401}.
CARBOHYD 1311 1311 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 49 {ECO:0000250}.
DISULFID 74 91 {ECO:0000250}.
DISULFID 168 194 {ECO:0000250}.
DISULFID 182 209 {ECO:0000250}.
DISULFID 247 340 {ECO:0000250}.
DISULFID 316 332 {ECO:0000250}.
DISULFID 391 486 {ECO:0000250}.
DISULFID 463 478 {ECO:0000250}.
DISULFID 532 625 {ECO:0000250}.
DISULFID 600 617 {ECO:0000250}.
DISULFID 646 659
DISULFID 680 777
DISULFID 753 769
DISULFID 828 922 {ECO:0000250}.
DISULFID 899 914 {ECO:0000250}.
DISULFID 977 1079 {ECO:0000250}.
DISULFID 1052 1071 {ECO:0000250}.
DISULFID 1123 1212 {ECO:0000250}.
DISULFID 1190 1204 {ECO:0000250}.
DISULFID 1263 1355 {ECO:0000250}.
DISULFID 1332 1347 {ECO:0000250}.
VAR_SEQ 470 498 DGYWADRGCEWPLGYICKMKSRSQGPEIV -> AGVQWHNL
GSMQPLPREFKRFSCLSLPSS (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041340.
VAR_SEQ 499 1456 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041341.
VARIANT 167 167 T -> I (in dbSNP:rs2296414).
{ECO:0000269|PubMed:20035344}.
/FTId=VAR_019700.
VARIANT 396 396 G -> S (probably protective against
leprosy when associated with A-399 and F-
407; dbSNP:rs1926736).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_065250.
VARIANT 399 399 T -> A (in dbSNP:rs35950447).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:20035344}.
/FTId=VAR_065251.
VARIANT 407 407 L -> F (in dbSNP:rs2437257).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:20035344}.
/FTId=VAR_065252.
CONFLICT 1334 1334 A -> T (in Ref. 2; X55635).
{ECO:0000305}.
STRAND 654 657 {ECO:0000244|PDB:1EGG}.
STRAND 659 663 {ECO:0000244|PDB:1EGG}.
HELIX 667 669 {ECO:0000244|PDB:1EGG}.
HELIX 673 681 {ECO:0000244|PDB:1EGG}.
TURN 682 684 {ECO:0000244|PDB:1EGG}.
STRAND 685 687 {ECO:0000244|PDB:1EGI}.
HELIX 693 706 {ECO:0000244|PDB:1EGG}.
STRAND 712 718 {ECO:0000244|PDB:1EGG}.
HELIX 746 748 {ECO:0000244|PDB:1EGG}.
STRAND 752 757 {ECO:0000244|PDB:1EGG}.
STRAND 764 768 {ECO:0000244|PDB:1EGG}.
STRAND 773 778 {ECO:0000244|PDB:1EGG}.
SEQUENCE 1456 AA; 166012 MW; 264E5AF3C576A5E3 CRC64;
MRLPLLLVFA SVIPGAVLLL DTRQFLIYNE DHKRCVDAVS PSAVQTAACN QDAESQKFRW
VSESQIMSVA FKLCLGVPSK TDWVAITLYA CDSKSEFQKW ECKNDTLLGI KGEDLFFNYG
NRQEKNIMLY KGSGLWSRWK IYGTTDNLCS RGYEAMYTLL GNANGATCAF PFKFENKWYA
DCTSAGRSDG WLWCGTTTDY DTDKLFGYCP LKFEGSESLW NKDPLTSVSY QINSKSALTW
HQARKSCQQQ NAELLSITEI HEQTYLTGLT SSLTSGLWIG LNSLSFNSGW QWSDRSPFRY
LNWLPGSPSA EPGKSCVSLN PGKNAKWENL ECVQKLGYIC KKGNTTLNSF VIPSESDVPT
HCPSQWWPYA GHCYKIHRDE KKIQRDALTT CRKEGGDLTS IHTIEELDFI ISQLGYEPND
ELWIGLNDIK IQMYFEWSDG TPVTFTKWLR GEPSHENNRQ EDCVVMKGKD GYWADRGCEW
PLGYICKMKS RSQGPEIVEV EKGCRKGWKK HHFYCYMIGH TLSTFAEANQ TCNNENAYLT
TIEDRYEQAF LTSFVGLRPE KYFWTGLSDI QTKGTFQWTI EEEVRFTHWN SDMPGRKPGC
VAMRTGIAGG LWDVLKCDEK AKFVCKHWAE GVTHPPKPTT TPEPKCPEDW GASSRTSLCF
KLYAKGKHEK KTWFESRDFC RALGGDLASI NNKEEQQTIW RLITASGSYH KLFWLGLTYG
SPSEGFTWSD GSPVSYENWA YGEPNNYQNV EYCGELKGDP TMSWNDINCE HLNNWICQIQ
KGQTPKPEPT PAPQDNPPVT EDGWVIYKDY QYYFSKEKET MDNARAFCKR NFGDLVSIQS
ESEKKFLWKY VNRNDAQSAY FIGLLISLDK KFAWMDGSKV DYVSWATGEP NFANEDENCV
TMYSNSGFWN DINCGYPNAF ICQRHNSSIN ATTVMPTMPS VPSGCKEGWN FYSNKCFKIF
GFMEEERKNW QEARKACIGF GGNLVSIQNE KEQAFLTYHM KDSTFSAWTG LNDVNSEHTF
LWTDGRGVHY TNWGKGYPGG RRSSLSYEDA DCVVIIGGAS NEAGKWMDDT CDSKRGYICQ
TRSDPSLTNP PATIQTDGFV KYGKSSYSLM RQKFQWHEAE TYCKLHNSLI ASILDPYSNA
FAWLQMETSN ERVWIALNSN LTDNQYTWTD KWRVRYTNWA ADEPKLKSAC VYLDLDGYWK
TAHCNESFYF LCKRSDEIPA TEPPQLPGRC PESDHTAWIP FHGHCYYIES SYTRNWGQAS
LECLRMGSSL VSIESAAESS FLSYRVEPLK SKTNFWIGLF RNVEGTWLWI NNSPVSFVNW
NTGDPSGERN DCVALHASSG FWSNIHCSSY KGYICKRPKI IDAKPTHELL TTKADTRKMD
PSKPSSNVAG VVIIVILLIL TGAGLAAYFF YKKRRVHLPQ EGAFENTLYF NSQSSPGTSD
MKDLVGNIEQ NEHSVI


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