KLRA3_MOUSE
ID KLRA3_MOUSE Reviewed; 266 AA.
AC Q64329; Q3TWQ1; Q3ZB40; Q499I4; Q61154; Q61198; Q64257;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Killer cell lectin-like receptor 3;
DE AltName: Full=5E6;
DE AltName: Full=Lymphocyte antigen 49c;
DE Short=Ly-49c;
DE AltName: Full=Nk2.1;
DE AltName: Full=T-cell surface glycoprotein Ly-49C;
GN Name=Klra3; Synonyms=Ly-49c, Ly49C;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX PubMed=1869832;
RA Wong S., Freeman J.D., Kelleher C., Mager D., Takei F.;
RT "Ly-49 multigene family. New members of a superfamily of type II membrane
RT proteins with lectin-like domains.";
RL J. Immunol. 147:1417-1423(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ, C57BL/6 X BALB/c, C57BL/6J, CB-17/SCID, and NZB;
RX PubMed=7629496; DOI=10.1084/jem.182.2.305;
RA Stoneman E.R., Bennett M., An J., Chesnut K.A., Wakeland E.K.,
RA Scheerer J.B., Siciliano M.J., Kumar V., Mathew P.A.;
RT "Cloning and characterization of 5E6(Ly-49C), a receptor molecule expressed
RT on a subset of murine natural killer cells.";
RL J. Exp. Med. 182:305-313(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Natural killer cell;
RX PubMed=8976165; DOI=10.1084/jem.184.6.2085;
RA Brennan J., Lemieux S., Freeman J.D., Mager D.L., Takei F.;
RT "Heterogeneity among Ly-49C natural killer (NK) cells: characterization of
RT highly related receptors with differing functions and expression
RT patterns.";
RL J. Exp. Med. 184:2085-2090(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=A/Sn, and C57BL/6J;
RX PubMed=8892625;
RA Sundbaeck J., Kaerre K., Sentman C.L.;
RT "Cloning of minimally divergent allelic forms of the natural killer (NK)
RT receptor Ly-49C, differentially controlled by host genes in the MHC and NK
RT gene complexes.";
RL J. Immunol. 157:3936-3942(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MUTAGENESIS OF ASN-160; LYS-161; THR-162; ALA-169; ASN-170; HIS-173;
RP TYR-174; ILE-195; PRO-196; LYS-225; ILE-226; ARG-234; ASP-248; ASN-250 AND
RP ILE-251.
RX PubMed=11777974; DOI=10.4049/jimmunol.168.2.793;
RA Sundback J., Achour A., Michaelsson J., Lindstrom H., Karre K.;
RT "NK cell inhibitory receptor Ly-49C residues involved in MHC class I
RT binding.";
RL J. Immunol. 168:793-800(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 142-263 OF WILD-TYPE AND MUTANT
RP ARG-121/SER-175/GLU-197/ARG-227 IN COMPLEX WITH H-2K, SUBUNIT, DISULFIDE
RP BONDS, AND MUTAGENESIS OF ARG-121; SER-175; GLU-197 AND ARG-227.
RX PubMed=14595439; DOI=10.1038/ni1006;
RA Dam J., Guan R., Natarajan K., Dimasi N., Chlewicki L.K., Kranz D.M.,
RA Schuck P., Margulies D.H., Mariuzza R.A.;
RT "Variable MHC class I engagement by Ly49 natural killer cell receptors
RT demonstrated by the crystal structure of Ly49C bound to H-2K(b).";
RL Nat. Immunol. 4:1213-1222(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 67-266 ALONE AND IN COMPLEX WITH
RP H-2K, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=18426793; DOI=10.1074/jbc.m801526200;
RA Deng L., Cho S., Malchiodi E.L., Kerzic M.C., Dam J., Mariuzza R.A.;
RT "Molecular architecture of the major histocompatibility complex class I-
RT binding site of Ly49 natural killer cell receptors.";
RL J. Biol. Chem. 283:16840-16849(2008).
CC -!- FUNCTION: Receptor on natural killer (NK) cells for class I MHC.
CC {ECO:0000269|PubMed:8976165}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:14595439,
CC ECO:0000269|PubMed:18426793}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U10305; AAA19053.1; -; mRNA.
DR EMBL; U09739; AAA86873.1; -; mRNA.
DR EMBL; U49865; AAA92951.1; -; mRNA.
DR EMBL; U49866; AAA92952.1; -; mRNA.
DR EMBL; U49867; AAA92953.1; -; mRNA.
DR EMBL; U49868; AAA92954.1; -; mRNA.
DR EMBL; U56404; AAB19100.1; -; mRNA.
DR EMBL; U56405; AAB19101.1; -; mRNA.
DR EMBL; AK159595; BAE35215.1; -; mRNA.
DR EMBL; AC087336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099867; AAH99867.1; -; mRNA.
DR EMBL; BC099878; AAH99878.1; -; mRNA.
DR EMBL; BC099879; AAH99879.1; -; mRNA.
DR EMBL; BC099880; AAH99880.1; -; mRNA.
DR EMBL; BC101952; AAI01953.1; -; mRNA.
DR EMBL; BC103543; AAI03544.1; -; mRNA.
DR EMBL; BC103544; AAI03545.1; -; mRNA.
DR EMBL; BC103545; AAI03546.1; -; mRNA.
DR EMBL; BC132524; AAI32525.1; -; mRNA.
DR EMBL; BC132526; AAI32527.1; -; mRNA.
DR EMBL; BC145192; AAI45193.1; -; mRNA.
DR EMBL; BC145193; AAI45194.1; -; mRNA.
DR CCDS; CCDS20601.1; -.
DR PIR; I49059; I49059.
DR PIR; I49363; I49363.
DR RefSeq; NP_001276533.1; NM_001289604.1.
DR RefSeq; NP_001276534.1; NM_001289605.1.
DR RefSeq; NP_034778.2; NM_010648.3.
DR RefSeq; NP_034781.2; NM_010651.3.
DR RefSeq; XP_011239535.1; XM_011241233.1.
DR RefSeq; XP_011239537.1; XM_011241235.1.
DR PDB; 1P1Z; X-ray; 3.26 A; D=143-262.
DR PDB; 1P4L; X-ray; 2.90 A; D=142-263.
DR PDB; 3C8J; X-ray; 2.60 A; A/B/C/D=67-266.
DR PDB; 3C8K; X-ray; 2.90 A; D=142-266.
DR PDB; 5J6G; X-ray; 3.30 A; G/H=136-266.
DR PDBsum; 1P1Z; -.
DR PDBsum; 1P4L; -.
DR PDBsum; 3C8J; -.
DR PDBsum; 3C8K; -.
DR PDBsum; 5J6G; -.
DR AlphaFoldDB; Q64329; -.
DR SMR; Q64329; -.
DR BioGRID; 200995; 1.
DR STRING; 10090.ENSMUSP00000107629; -.
DR GlyGen; Q64329; 5 sites.
DR EPD; Q64329; -.
DR PaxDb; Q64329; -.
DR PRIDE; Q64329; -.
DR DNASU; 16640; -.
DR Ensembl; ENSMUST00000088017; ENSMUSP00000085333; ENSMUSG00000067591.
DR Ensembl; ENSMUST00000111998; ENSMUSP00000107629; ENSMUSG00000067591.
DR GeneID; 16634; -.
DR GeneID; 16640; -.
DR KEGG; mmu:16634; -.
DR KEGG; mmu:16640; -.
DR UCSC; uc009eik.2; mouse.
DR CTD; 16634; -.
DR CTD; 16640; -.
DR MGI; MGI:101905; Klra3.
DR VEuPathDB; HostDB:ENSMUSG00000067591; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00390000008117; -.
DR HOGENOM; CLU_049894_1_0_1; -.
DR InParanoid; Q64329; -.
DR OMA; HDSAWID; -.
DR OrthoDB; 945977at2759; -.
DR PhylomeDB; Q64329; -.
DR TreeFam; TF336674; -.
DR BioGRID-ORCS; 16634; 1 hit in 40 CRISPR screens.
DR BioGRID-ORCS; 16640; 1 hit in 39 CRISPR screens.
DR ChiTaRS; Klra3; mouse.
DR EvolutionaryTrace; Q64329; -.
DR PRO; PR:Q64329; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q64329; protein.
DR Bgee; ENSMUSG00000067591; Expressed in spleen and 11 other tissues.
DR Genevisible; Q64329; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR013600; Ly49_N.
DR InterPro; IPR033992; NKR-like_CTLD.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF08391; Ly49; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Disulfide bond; Glycoprotein; Lectin;
KW Membrane; Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..266
FT /note="Killer cell lectin-like receptor 3"
FT /id="PRO_0000046681"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 150..258
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 147..151
FT /note="Involved in dimerization"
FT REGION 160..162
FT /note="Implicated in MHC class I binding"
FT REGION 195..196
FT /note="Implicated in MHC class I binding"
FT REGION 207..208
FT /note="Implicated in MHC class I binding"
FT REGION 224..233
FT /note="Implicated in MHC class I binding"
FT REGION 240..245
FT /note="Implicated in MHC class I binding"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 149..154
FT DISULFID 167..255
FT DISULFID 171..257
FT DISULFID 236..249
FT VARIANT 2
FT /note="S -> N (in strain: C57BL/6 and C57BL/6 X BALB/c)"
FT VARIANT 22
FT /note="L -> Q (in strain: A/Sn, BALB/c, C57BL/6, C57BL/6 X
FT BALB/c, C57BL/6 X CBA, CB-17/SCID and NZB)"
FT VARIANT 34
FT /note="V -> A (in strain: C57BL/6, C57BL/6 X BALB/c and
FT NZB)"
FT VARIANT 41..42
FT /note="AP -> VS (in strain: C57BL/6 X BALB/c, NZB and
FT C57BL/6)"
FT VARIANT 60
FT /note="T -> I (in strain: C57BL/6, C57BL/6 X BALB/c and
FT NZB)"
FT VARIANT 65..66
FT /note="AV -> TI (in strain: C57BL/6, C57BL/6 X BALB/c and
FT NZB)"
FT VARIANT 72
FT /note="N -> S (in strain: C57BL/6, C57BL/6 X BALB/c and
FT NZB)"
FT VARIANT 85
FT /note="H -> Y (in strain: C57BL/6, C57BL/6 X BALB/c and
FT NZB)"
FT VARIANT 93..94
FT /note="RA -> SD (in strain: A/Sn, BALB/c, C57BL/6, C57BL/6
FT X BALB/c, C57BL/6 X CBA, CB-17/SCID and NZB)"
FT VARIANT 115
FT /note="T -> L (in strain: C57BL/6, C57BL/6 X BALB/c and
FT NZB; requires 2 nucleotide substitutions)"
FT VARIANT 117
FT /note="E -> D (in strain: C57BL/6 and C57BL/6 X BALB/c)"
FT VARIANT 127
FT /note="D -> N (in strain: C57BL/6 and C57BL/6 X BALB/c)"
FT VARIANT 129
FT /note="K -> E (in strain: C57BL/6, C57BL/6 X BALB/c and
FT NZB)"
FT VARIANT 131
FT /note="K -> N (in strain: NZB)"
FT VARIANT 133
FT /note="V -> I (in strain: NZB)"
FT VARIANT 146
FT /note="Y -> H (in strain: C57BL/6 and C57BL/6 X BALB/c)"
FT VARIANT 151
FT /note="S -> G (in strain: C57BL/6, C57BL/6 X BALB/c and
FT NZB)"
FT VARIANT 174
FT /note="Y -> F (in strain: A/Sn, BALB/c, C57BL/6, C57BL/6 X
FT BALB/c, C57BL/6 X CBA, CB-17/SCID and NZB)"
FT VARIANT 179
FT /note="L -> V (in strain: C57BL/6, C57BL/6 X BALB/c and
FT NZB)"
FT VARIANT 189
FT /note="F -> S (in strain: NZB)"
FT VARIANT 198
FT /note="N -> S (in strain: C57BL/6, C57BL/6 X BALB/c and
FT NZB)"
FT VARIANT 219
FT /note="P -> Q (in strain: C57BL/6, C57BL/6 X BALB/c and
FT NZB)"
FT VARIANT 226
FT /note="I -> T (in strain: C57BL/6, C57BL/6 X BALB/c and
FT NZB)"
FT VARIANT 232
FT /note="K -> T (in strain: NZB)"
FT VARIANT 247
FT /note="I -> T (in strain: C57BL/6, C57BL/6 X BALB/c and
FT NZB)"
FT VARIANT 251
FT /note="I -> T (in strain: NZB)"
FT VARIANT 260
FT /note="K -> R (in strain: NZB)"
FT MUTAGEN 121
FT /note="R->G: Increases stability and improves binding to
FT MHC I class ligand; when associated with G-175; G-197 and
FT K-227."
FT /evidence="ECO:0000269|PubMed:14595439"
FT MUTAGEN 160
FT /note="N->D: Greatly reduces MHC class I peptide tetramer
FT binding; when associated with L-162."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 161
FT /note="K->R: No effect on MHC class I peptide tetramer
FT binding."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 162
FT /note="T->K: Greatly reduces MHC class I peptide tetramer
FT binding; when associated with D-160."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 169
FT /note="A->Q: No effect on MHC class I peptide tetramer
FT binding; when associated with T-170."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 170
FT /note="N->T: No effect on MHC class I peptide tetramer
FT binding; when associated with Q-169."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 173
FT /note="H->S: No effect on MHC class I peptide tetramer
FT binding; when associated with S-174."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 174
FT /note="Y->S: No effect on MHC class I binding; when
FT associated with S-173."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 175
FT /note="S->G: Increases stability. Increases stability and
FT improves binding to MHC I class ligand; when associated
FT with G-121; G-197 and K-227."
FT /evidence="ECO:0000269|PubMed:14595439"
FT MUTAGEN 195
FT /note="I->P: Greatly reduces MHC class I peptide tetramer
FT binding; when associated with S-196."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 196
FT /note="P->S: Greatly reduces MHC class I peptide tetramer
FT binding; when associated with P-195."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 197
FT /note="E->G: Increases stability and improves binding to
FT MHC I class ligand; when associated with G-121; G-175 and
FT K-227."
FT /evidence="ECO:0000269|PubMed:14595439"
FT MUTAGEN 225
FT /note="K->N: Greatly reduces MHC class I peptide tetramer
FT binding; when associated with T-226."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 226
FT /note="I->T: Greatly reduces MHC class I peptide tetramer
FT binding; when associated with N-225."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 227
FT /note="R->K: Increases stability and improves binding to
FT MHC I class ligand; when associated with G-121; G-175 and
FT G-197."
FT /evidence="ECO:0000269|PubMed:14595439"
FT MUTAGEN 234
FT /note="R->G: No effect on MHC class I peptide tetramer
FT binding."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 248
FT /note="D->N: No effect on MHC class I peptide tetramer
FT binding; when associated with D-250."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 250
FT /note="N->D: No effect on MHC class I peptide tetramer
FT binding; when associated with N-248."
FT /evidence="ECO:0000269|PubMed:11777974"
FT MUTAGEN 251
FT /note="I->Q: No effect on MHC class I peptide tetramer
FT binding."
FT /evidence="ECO:0000269|PubMed:11777974"
FT CONFLICT 4
FT /note="P -> L (in Ref. 7; AAH99880/AAH99879/AAH99878/
FT AAH99867)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="T -> M (in Ref. 5; BAE35215)"
FT /evidence="ECO:0000305"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3C8J"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:3C8J"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:3C8J"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:3C8J"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:3C8J"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:3C8J"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:3C8J"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:3C8J"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:3C8J"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:3C8J"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:3C8J"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:3C8J"
SQ SEQUENCE 266 AA; 31311 MW; BF9B10D9B6EFD628 CRC64;
MSEPEVTYST VRLHKSSGLQ KLVRHEETQG PREVGNRKCS APWQLIVKAL GILCFLLLVT
VAVLAVKIFQ YNQHKQEINE TLNHHHNCSN MQRAFNLKEE MLTNKSIDCR PSNETLEYIK
REQDRWDSKT KTVLDSSRDT GRGVKYWFCY STKCYYFIMN KTTWSGCKAN CQHYSVPILK
IEDEDELKFL QRHVIPENYW IGLSYDKKKK EWAWIDNGPS KLDMKIRKMN FKSRGCVFLS
KARIEDIDCN IPYYCICGKK LDKFPD
