DQA2_HUMAN
ID DQA2_HUMAN Reviewed; 255 AA.
AC P01906; A2BF37; B0V0E7; O19789; Q5SQ94; Q5SR04;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=HLA class II histocompatibility antigen, DQ alpha 2 chain;
DE AltName: Full=DX alpha chain;
DE AltName: Full=HLA class II histocompatibility antigen, DQ(6) alpha chain;
DE AltName: Full=HLA-DQA1;
DE AltName: Full=MHC class II DQA2;
DE Flags: Precursor;
GN Name=HLA-DQA2; Synonyms=HLA-DXA;
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 [GENOMIC DNA].
RX PubMed=3036828; DOI=10.1016/s0021-9258(18)47482-0;
RA Jonsson A.-K., Hyldig-Nielsen J.-J., Servenius B., Larhammar D.,
RA Andersson G., Joergensen F., Peterson P.A., Rask L.;
RT "Class II genes of the human major histocompatibility complex. Comparisons
RT of the DQ and DX alpha and beta genes.";
RL J. Biol. Chem. 262:8767-8777(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONE LAMBDA DCH-10).
RX PubMed=6584734; DOI=10.1038/308327a0;
RA Auffray C., Lillie J.W., Arnot D., Grossberger D., Kappes D.,
RA Strominger J.L.;
RT "Isotypic and allotypic variation of human class II histocompatibility
RT antigen alpha-chain genes.";
RL Nature 308:327-333(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3610256; DOI=10.1007/bf00345456;
RA Auffray C., Lillie J.W., Korman A.J., Boss J.M., Frechin N., Guillemot F.,
RA Cooper J., Mulligan R.C., Strominger J.L.;
RT "Structure and expression of HLA-DQ alpha and -DX alpha genes: interallelic
RT alternate splicing of the HLA-DQ alpha gene and functional splicing of the
RT HLA-DQ alpha gene using a retroviral vector.";
RL Immunogenetics 26:63-73(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ALA-227 AND
RP ASP-247.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RX PubMed=8026991; DOI=10.1016/0198-8859(94)90264-x;
RA Rudy G., Lew A.M.;
RT "Limited polymorphism of the HLA-DQA2 promoter and identification of a
RT variant octamer.";
RL Hum. Immunol. 39:225-229(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-103.
RX PubMed=2513578; DOI=10.1073/pnas.86.24.9986;
RA Gyllensten U.B., Erlich H.A.;
RT "Ancient roots for polymorphism at the HLA-DQ alpha locus in primates.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9986-9990(1989).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=9036956;
RA Rudy G.B., Lew A.M.;
RT "The nonpolymorphic MHC class II isotype, HLA-DQA2, is expressed on the
RT surface of B lymphoblastoid cells.";
RL J. Immunol. 158:2116-2125(1997).
RN [8]
RP REVIEW.
RX PubMed=8598037; DOI=10.1016/s0092-8674(00)81025-9;
RA Cresswell P.;
RT "Invariant chain structure and MHC class II function.";
RL Cell 84:505-507(1996).
RN [9]
RP REVIEW.
RX PubMed=11684289; DOI=10.1016/s0161-5890(01)00069-4;
RA Villadangos J.A.;
RT "Presentation of antigens by MHC class II molecules: getting the most out
RT of them.";
RL Mol. Immunol. 38:329-346(2001).
RN [10]
RP REVIEW.
RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945;
RA Rocha N., Neefjes J.;
RT "MHC class II molecules on the move for successful antigen presentation.";
RL EMBO J. 27:1-5(2008).
RN [11]
RP REVIEW.
RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005;
RA Menendez-Benito V., Neefjes J.;
RT "Autophagy in MHC class II presentation: sampling from within.";
RL Immunity 26:1-3(2007).
RN [12]
RP REVIEW.
RX PubMed=19092054; DOI=10.1242/jcs.035089;
RA Berger A.C., Roche P.A.;
RT "MHC class II transport at a glance.";
RL J. Cell Sci. 122:1-4(2009).
RN [13]
RP REVIEW.
RX PubMed=19533806; DOI=10.3748/wjg.15.2855;
RA Beswick E.J., Reyes V.E.;
RT "CD74 in antigen presentation, inflammation, and cancers of the
RT gastrointestinal tract.";
RL World J. Gastroenterol. 15:2855-2861(2009).
RN [14]
RP FUNCTION, INTERACTION WITH CD74; HLA-DMA; HLA-DQB1 AND HLA-DQB2,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22407913; DOI=10.4049/jimmunol.1103048;
RA Lenormand C., Bausinger H., Gross F., Signorino-Gelo F., Koch S.,
RA Peressin M., Fricker D., Cazenave J.P., Bieber T., Hanau D.,
RA de la Salle H., Tourne S.;
RT "HLA-DQA2 and HLA-DQB2 genes are specifically expressed in human Langerhans
RT cells and encode a new HLA class II molecule.";
RL J. Immunol. 188:3903-3911(2012).
CC -!- FUNCTION: Binds peptides derived from antigens that access the
CC endocytic route of antigen presenting cells (APC) and presents them on
CC the cell surface for recognition by the CD4 T-cells. The peptide
CC binding cleft accommodates peptides of 10-30 residues. The peptides
CC presented by MHC class II molecules are generated mostly by degradation
CC of proteins that access the endocytic route, where they are processed
CC by lysosomal proteases and other hydrolases. Exogenous antigens that
CC have been endocytosed by the APC are thus readily available for
CC presentation via MHC II molecules, and for this reason this antigen
CC presentation pathway is usually referred to as exogenous. As membrane
CC proteins on their way to degradation in lysosomes as part of their
CC normal turn-over are also contained in the endosomal/lysosomal
CC compartments, exogenous antigens must compete with those derived from
CC endogenous components. Autophagy is also a source of endogenous
CC peptides, autophagosomes constitutively fuse with MHC class II loading
CC compartments. In addition to APCs, other cells of the gastrointestinal
CC tract, such as epithelial cells, express MHC class II molecules and
CC CD74 and act as APCs, which is an unusual trait of the GI tract. To
CC produce a MHC class II molecule that presents an antigen, three MHC
CC class II molecules (heterodimers of an alpha and a beta chain)
CC associate with a CD74 trimer in the ER to form a heterononamer. Soon
CC after the entry of this complex into the endosomal/lysosomal system
CC where antigen processing occurs, CD74 undergoes a sequential
CC degradation by various proteases, including CTSS and CTSL, leaving a
CC small fragment termed CLIP (class-II-associated invariant chain
CC peptide). The removal of CLIP is facilitated by HLA-DM via direct
CC binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM
CC stabilizes MHC class II molecules until primary high affinity antigenic
CC peptides are bound. The MHC II molecule bound to a peptide is then
CC transported to the cell membrane surface. In B-cells, the interaction
CC between HLA-DM and MHC class II molecules is regulated by HLA-DO.
CC Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal
CC microenvironment has been implicated in the regulation of antigen
CC loading into MHC II molecules, increased acidification produces
CC increased proteolysis and efficient peptide loading.
CC {ECO:0000269|PubMed:22407913}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred as
CC MHC class II molecule. Dimer formation with HLA-DQB2, but not with HLA-
CC DQB1, is required for efficient exit from the endoplasmic reticulum
CC (ER). In the ER, forms a heterononamer; 3 MHC class II molecules bind
CC to a CD74 homotrimer (also known as invariant chain or HLA class II
CC histocompatibility antigen gamma chain). In the endosomal/lysosomal
CC system; CD74 undergoes sequential degradation by various proteases;
CC leaving a small fragment termed CLIP on each MHC class II molecule. MHC
CC class II molecule interacts with HLA_DM, and HLA_DO in B-cells, in
CC order to release CLIP and facilitate the binding of antigenic peptides.
CC Association with HLA-DMA also occurs in skin Langerhans cells, in post-
CC Golgi compartments. {ECO:0000269|PubMed:22407913}.
CC -!- INTERACTION:
CC P01906; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-19949550, EBI-2820517;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22407913};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:22407913}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:22407913}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:22407913};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}.
CC Endosome membrane {ECO:0000269|PubMed:22407913}; Single-pass type I
CC membrane protein {ECO:0000269|PubMed:22407913}. Lysosome membrane
CC {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:22407913}. Note=The MHC class II complex transits
CC through a number of intracellular compartments in the endocytic pathway
CC until it reaches the cell membrane for antigen presentation.
CC -!- TISSUE SPECIFICITY: Restricted to skin Langerhans cells, although some
CC expression at low levels may occur at the surface of B lymphoblastoid
CC cells. {ECO:0000269|PubMed:22407913, ECO:0000269|PubMed:9036956}.
CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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DR EMBL; M29615; AAA59834.1; -; Genomic_DNA.
DR EMBL; M29614; AAA59834.1; JOINED; Genomic_DNA.
DR EMBL; X00453; CAA25142.1; -; Genomic_DNA.
DR EMBL; X00454; CAA25142.1; JOINED; Genomic_DNA.
DR EMBL; X00455; CAA25142.1; JOINED; Genomic_DNA.
DR EMBL; X00456; CAA25142.1; JOINED; Genomic_DNA.
DR EMBL; M17237; AAA59605.1; -; Genomic_DNA.
DR EMBL; M17235; AAA59605.1; JOINED; Genomic_DNA.
DR EMBL; AL773543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927131; CAM26196.1; -; Genomic_DNA.
DR EMBL; BX248406; CAM26196.1; JOINED; Genomic_DNA.
DR EMBL; AL672104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR936921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S71248; AAD14077.1; -; Genomic_DNA.
DR CCDS; CCDS4753.1; -.
DR PIR; A02210; HLHUDX.
DR PIR; I54439; I54439.
DR RefSeq; NP_064440.1; NM_020056.4.
DR AlphaFoldDB; P01906; -.
DR SMR; P01906; -.
DR BioGRID; 109363; 2.
DR IntAct; P01906; 1.
DR STRING; 9606.ENSP00000364076; -.
DR GlyGen; P01906; 3 sites.
DR iPTMnet; P01906; -.
DR PhosphoSitePlus; P01906; -.
DR BioMuta; HLA-DQA2; -.
DR DMDM; 122192; -.
DR jPOST; P01906; -.
DR MassIVE; P01906; -.
DR PaxDb; P01906; -.
DR PeptideAtlas; P01906; -.
DR PRIDE; P01906; -.
DR Antibodypedia; 48442; 241 antibodies from 28 providers.
DR DNASU; 3118; -.
DR Ensembl; ENST00000241802.9; ENSP00000241802.5; ENSG00000206301.9.
DR Ensembl; ENST00000374940.4; ENSP00000364076.3; ENSG00000237541.4.
DR Ensembl; ENST00000415898.2; ENSP00000400695.2; ENSG00000231526.3.
DR Ensembl; ENST00000443184.2; ENSP00000405833.2; ENSG00000257473.7.
DR Ensembl; ENST00000446482.2; ENSP00000390725.2; ENSG00000225103.3.
DR Ensembl; ENST00000447735.5; ENSP00000393431.1; ENSG00000223793.7.
DR Ensembl; ENST00000449560.5; ENSP00000401098.1; ENSG00000233192.7.
DR Ensembl; ENST00000453672.2; ENSP00000387768.2; ENSG00000231823.3.
DR Ensembl; ENST00000546801.2; ENSP00000447668.1; ENSG00000233192.7.
DR Ensembl; ENST00000551533.1; ENSP00000448003.1; ENSG00000223793.7.
DR GeneID; 3118; -.
DR KEGG; hsa:3118; -.
DR MANE-Select; ENST00000374940.4; ENSP00000364076.3; NM_020056.5; NP_064440.1.
DR UCSC; uc003obx.4; human.
DR CTD; 3118; -.
DR DisGeNET; 3118; -.
DR GeneCards; HLA-DQA2; -.
DR HGNC; HGNC:4943; HLA-DQA2.
DR HPA; ENSG00000237541; Tissue enhanced (lung, lymphoid tissue).
DR MIM; 613503; gene.
DR neXtProt; NX_P01906; -.
DR OpenTargets; ENSG00000237541; -.
DR PharmGKB; PA35067; -.
DR VEuPathDB; HostDB:ENSG00000237541; -.
DR eggNOG; ENOG502RXYJ; Eukaryota.
DR GeneTree; ENSGT00940000162892; -.
DR HOGENOM; CLU_069380_0_0_1; -.
DR InParanoid; P01906; -.
DR OMA; VADLQIC; -.
DR OrthoDB; 1132781at2759; -.
DR PhylomeDB; P01906; -.
DR TreeFam; TF333797; -.
DR PathwayCommons; P01906; -.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
DR Reactome; R-HSA-202433; Generation of second messenger molecules.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-389948; PD-1 signaling.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; P01906; -.
DR SIGNOR; P01906; -.
DR BioGRID-ORCS; 3118; 10 hits in 1063 CRISPR screens.
DR ChiTaRS; HLA-DQA2; human.
DR GeneWiki; HLA-DQA2; -.
DR GenomeRNAi; 3118; -.
DR Pharos; P01906; Tbio.
DR PRO; PR:P01906; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P01906; protein.
DR Bgee; ENSG00000206301; Expressed in nasopharynx and 8 other tissues.
DR ExpressionAtlas; P01906; baseline and differential.
DR Genevisible; P01906; HS.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0042613; C:MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
DR GO; GO:0023026; F:MHC class II protein complex binding; IBA:GO_Central.
DR GO; GO:0032395; F:MHC class II receptor activity; NAS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.320.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR014745; MHC_II_a/b_N.
DR InterPro; IPR001003; MHC_II_a_N.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00993; MHC_II_alpha; 1.
DR SMART; SM00407; IGc1; 1.
DR SMART; SM00920; MHC_II_alpha; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Endosome; Glycoprotein; Golgi apparatus; Immunity; Lysosome; Membrane;
KW MHC II; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT CHAIN 24..255
FT /note="HLA class II histocompatibility antigen, DQ alpha 2
FT chain"
FT /id="PRO_0000018973"
FT TOPO_DOM 24..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 113..205
FT /note="Ig-like C1-type"
FT REGION 24..110
FT /note="Alpha-1"
FT REGION 111..204
FT /note="Alpha-2"
FT REGION 205..217
FT /note="Connecting peptide"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 133..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 227
FT /note="V -> A (in dbSNP:rs9276436)"
FT /evidence="ECO:0000269|PubMed:14574404"
FT /id="VAR_033431"
FT VARIANT 247
FT /note="G -> D (in dbSNP:rs2071800)"
FT /evidence="ECO:0000269|PubMed:14574404"
FT /id="VAR_050392"
FT CONFLICT 84
FT /note="S -> T (in Ref. 1; AAA59834)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="R -> G (in Ref. 4; CAM26196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 28033 MW; 85B13D9FDF2905FE CRC64;
MILNKALLLG ALALTAVMSP CGGEDIVADH VASYGVNFYQ SHGPSGQYTH EFDGDEEFYV
DLETKETVWQ LPMFSKFISF DPQSALRNMA VGKHTLEFMM RQSNSTAATN EVPEVTVFSK
FPVTLGQPNT LICLVDNIFP PVVNITWLSN GHSVTEGVSE TSFLSKSDHS FFKISYLTFL
PSADEIYDCK VEHWGLDEPL LKHWEPEIPA PMSELTETLV CALGLSVGLM GIVVGTVFII
QGLRSVGASR HQGLL
