KI2L3_HUMAN
ID KI2L3_HUMAN Reviewed; 341 AA.
AC P43628; O43472; P78402; Q14944; Q14945; Q9UM51; Q9UQ70;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Killer cell immunoglobulin-like receptor 2DL3 {ECO:0000305};
DE AltName: Full=CD158 antigen-like family member B2;
DE AltName: Full=KIR-023GB;
DE AltName: Full=Killer inhibitory receptor cl 2-3;
DE AltName: Full=NKAT2a;
DE AltName: Full=NKAT2b;
DE AltName: Full=Natural killer-associated transcript 2;
DE Short=NKAT-2;
DE AltName: Full=p58 natural killer cell receptor clone CL-6;
DE Short=p58 NK receptor CL-6;
DE AltName: Full=p58.2 MHC class-I-specific NK receptor;
DE AltName: CD_antigen=CD158b2;
DE Flags: Precursor;
GN Name=KIR2DL3 {ECO:0000312|HGNC:HGNC:6331};
GN Synonyms=CD158B2, KIRCL23, NKAT2;
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=Natural killer cell;
RX PubMed=7716543; DOI=10.1126/science.7716543;
RA Colonna M., Samaridis J.;
RT "Cloning of immunoglobulin-superfamily members associated with HLA-C and
RT HLA-B recognition by human natural killer cells.";
RL Science 268:405-408(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Natural killer cell;
RX PubMed=7749980; DOI=10.1016/1074-7613(95)90025-x;
RA Wagtmann N., Biassoni R., Cantoni C., Verdiani S., Malnati M.S., Vitale M.,
RA Bottino C., Moretta L., Moretta A., Long E.O.;
RT "Molecular clones of the p58 NK cell receptor reveal immunoglobulin-related
RT molecules with diversity in both the extra- and intracellular domains.";
RL Immunity 2:439-449(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS LEU-229;
RP THR-304 AND HIS-318.
RX PubMed=8662091; DOI=10.1007/bf02602590;
RA Doehring C., Samaridis J., Colonna M.;
RT "Alternatively spliced forms of human killer inhibitory receptors.";
RL Immunogenetics 44:227-230(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1), AND VARIANTS ALA-9; ARG-32; GLU-56; ARG-71
RP AND HIS-318.
RX PubMed=9430221; DOI=10.1016/s1074-7613(00)80394-5;
RA Uhrberg M., Valiante N.M., Shum B.P., Shilling H.G., Lienert-Weidenbach K.,
RA Corliss B., Tyan D., Lanier L.L., Parham P.;
RT "Human diversity in killer cell inhibitory receptor genes.";
RL Immunity 7:753-763(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-9; ARG-32; GLU-56;
RP ARG-71; ILE-242 AND HIS-318.
RX PubMed=9059894; DOI=10.1111/j.1600-065x.1997.tb00951.x;
RA Selvakumar A., Steffens U., Dupont B.;
RT "Polymorphism and domain variability of human killer cell inhibitory
RT receptors.";
RL Immunol. Rev. 155:183-196(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS LEU-229
RP AND HIS-318.
RC TISSUE=Blood;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-298 (ISOFORM 1), AND VARIANT
RP LEU-229.
RX PubMed=9234478; DOI=10.1111/j.1399-0039.1997.tb02804.x;
RA Wilson M.J., Torkar M., Trowsdale J.;
RT "Genomic organization of a human killer cell inhibitory receptor gene.";
RL Tissue Antigens 49:574-579(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-341, AND VARIANT GLN-34.
RC TISSUE=Placenta;
RA Chae J.H., Kim Y.M., Ahn J.M., Kim C.G., Kim J., Kim S.J., Park J.H.;
RT "Genomic organization of novel genes encoding human killer inhibitory
RT receptors.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP INTERACTION WITH ARRB2.
RX PubMed=18604210; DOI=10.1038/ni.1635;
RA Yu M.-C., Su L.-L., Zou L., Liu Y., Wu N., Kong L., Zhuang Z.-H., Sun L.,
RA Liu H.P., Hu J.-H., Li D., Strominger J.L., Zang J.-W., Pei G., Ge B.-X.;
RT "An essential function for beta-arrestin 2 in the inhibitory signaling of
RT natural killer cells.";
RL Nat. Immunol. 9:898-907(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-245.
RX PubMed=10196125; DOI=10.1016/s0969-2126(99)80052-5;
RA Maenaka K., Juji T., Stuart D.I., Jones E.Y.;
RT "Crystal structure of the human p58 killer cell inhibitory receptor
RT (KIR2DL3) specific for HLA-Cw3-related MHC class I.";
RL Structure 7:391-398(1999).
CC -!- FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles (HLA-
CC Cw1, HLA-Cw3 and HLA-Cw7). Inhibits the activity of NK cells thus
CC preventing cell lysis.
CC -!- SUBUNIT: Interacts with ARRB2. {ECO:0000269|PubMed:18604210}.
CC -!- INTERACTION:
CC P43628; Q9UHX3: ADGRE2; NbExp=3; IntAct=EBI-8632435, EBI-11277970;
CC P43628; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-8632435, EBI-11522760;
CC P43628; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-8632435, EBI-11957045;
CC P43628; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-8632435, EBI-12109402;
CC P43628; P02652: APOA2; NbExp=3; IntAct=EBI-8632435, EBI-1171525;
CC P43628; P05090: APOD; NbExp=3; IntAct=EBI-8632435, EBI-715495;
CC P43628; Q96PS8: AQP10; NbExp=3; IntAct=EBI-8632435, EBI-12820279;
CC P43628; P07306: ASGR1; NbExp=3; IntAct=EBI-8632435, EBI-1172335;
CC P43628; O15342: ATP6V0E1; NbExp=3; IntAct=EBI-8632435, EBI-12935759;
CC P43628; O95393: BMP10; NbExp=3; IntAct=EBI-8632435, EBI-3922513;
CC P43628; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-8632435, EBI-12244618;
CC P43628; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-8632435, EBI-8648738;
CC P43628; O14735: CDIPT; NbExp=3; IntAct=EBI-8632435, EBI-358858;
CC P43628; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-8632435, EBI-1045797;
CC P43628; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-8632435, EBI-12256978;
CC P43628; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-8632435, EBI-6165897;
CC P43628; O75208: COQ9; NbExp=3; IntAct=EBI-8632435, EBI-724524;
CC P43628; Q07325: CXCL9; NbExp=3; IntAct=EBI-8632435, EBI-3911467;
CC P43628; O43169: CYB5B; NbExp=3; IntAct=EBI-8632435, EBI-1058710;
CC P43628; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-8632435, EBI-2680384;
CC P43628; P50402: EMD; NbExp=3; IntAct=EBI-8632435, EBI-489887;
CC P43628; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-8632435, EBI-18304435;
CC P43628; Q92520: FAM3C; NbExp=3; IntAct=EBI-8632435, EBI-2876774;
CC P43628; Q9BWH2: FUNDC2; NbExp=3; IntAct=EBI-8632435, EBI-714482;
CC P43628; P01350: GAST; NbExp=3; IntAct=EBI-8632435, EBI-3436637;
CC P43628; P48165: GJA8; NbExp=3; IntAct=EBI-8632435, EBI-17458373;
CC P43628; Q9NPR9: GPR108; NbExp=3; IntAct=EBI-8632435, EBI-11343451;
CC P43628; Q8TED1: GPX8; NbExp=3; IntAct=EBI-8632435, EBI-11721746;
CC P43628; P01889: HLA-B; NbExp=2; IntAct=EBI-8632435, EBI-1046513;
CC P43628; P10321: HLA-C; NbExp=9; IntAct=EBI-8632435, EBI-1051396;
CC P43628; Q53YP1: HLA-C; NbExp=2; IntAct=EBI-8632435, EBI-13917186;
CC P43628; Q01628: IFITM3; NbExp=3; IntAct=EBI-8632435, EBI-7932862;
CC P43628; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-8632435, EBI-8503746;
CC P43628; P11215: ITGAM; NbExp=3; IntAct=EBI-8632435, EBI-2568251;
CC P43628; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-8632435, EBI-10266796;
CC P43628; P43628: KIR2DL3; NbExp=3; IntAct=EBI-8632435, EBI-8632435;
CC P43628; Q86UP2-3: KTN1; NbExp=3; IntAct=EBI-8632435, EBI-12007212;
CC P43628; O43561-2: LAT; NbExp=3; IntAct=EBI-8632435, EBI-8070286;
CC P43628; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-8632435, EBI-17490413;
CC P43628; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-8632435, EBI-2820517;
CC P43628; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-8632435, EBI-10317425;
CC P43628; Q8IXM6: NRM; NbExp=3; IntAct=EBI-8632435, EBI-10262547;
CC P43628; P42857: NSG1; NbExp=3; IntAct=EBI-8632435, EBI-6380741;
CC P43628; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-8632435, EBI-2804156;
CC P43628; P26678: PLN; NbExp=3; IntAct=EBI-8632435, EBI-692836;
CC P43628; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-8632435, EBI-12955265;
CC P43628; Q06124: PTPN11; NbExp=4; IntAct=EBI-8632435, EBI-297779;
CC P43628; P29350: PTPN6; NbExp=13; IntAct=EBI-8632435, EBI-78260;
CC P43628; Q8N8N0: RNF152; NbExp=3; IntAct=EBI-8632435, EBI-2129725;
CC P43628; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-8632435, EBI-10244780;
CC P43628; O75396: SEC22B; NbExp=3; IntAct=EBI-8632435, EBI-1058865;
CC P43628; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-8632435, EBI-10314552;
CC P43628; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-8632435, EBI-12188413;
CC P43628; Q6UX34: SNORC; NbExp=3; IntAct=EBI-8632435, EBI-11957067;
CC P43628; P07204: THBD; NbExp=3; IntAct=EBI-8632435, EBI-941422;
CC P43628; A2RU14: TMEM218; NbExp=3; IntAct=EBI-8632435, EBI-10173151;
CC P43628; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-8632435, EBI-347385;
CC P43628; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-8632435, EBI-12887458;
CC P43628; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-8632435, EBI-2548832;
CC P43628; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-8632435, EBI-12111910;
CC P43628; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-8632435, EBI-765817;
CC P43628; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-8632435, EBI-10243654;
CC P43628; O75841: UPK1B; NbExp=3; IntAct=EBI-8632435, EBI-12237619;
CC P43628; O00526: UPK2; NbExp=3; IntAct=EBI-8632435, EBI-10179682;
CC P43628; O95183: VAMP5; NbExp=3; IntAct=EBI-8632435, EBI-10191195;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43628-1; Sequence=Displayed;
CC Name=2; Synonyms=NKAT2a-delta-Ig2;
CC IsoId=P43628-2; Sequence=VSP_007814;
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; L41268; AAA69869.1; -; mRNA.
DR EMBL; U24074; AAC50333.1; -; mRNA.
DR EMBL; L76662; AAB36590.1; -; mRNA.
DR EMBL; L76663; AAB36591.1; -; mRNA.
DR EMBL; AF022048; AAB95321.1; -; mRNA.
DR EMBL; U73395; AAC51147.1; -; mRNA.
DR EMBL; BC032422; AAH32422.1; -; mRNA.
DR EMBL; BC050730; AAH50730.1; -; mRNA.
DR EMBL; AH006692; AAC51651.1; -; Genomic_DNA.
DR EMBL; AH007572; AAD24477.1; -; Genomic_DNA.
DR CCDS; CCDS33107.1; -. [P43628-1]
DR PIR; I61725; I61725.
DR RefSeq; NP_056952.2; NM_015868.2. [P43628-1]
DR PDB; 1B6U; X-ray; 3.00 A; A=22-245.
DR PDB; 6PAG; X-ray; 2.50 A; D=22-225.
DR PDBsum; 1B6U; -.
DR PDBsum; 6PAG; -.
DR AlphaFoldDB; P43628; -.
DR SMR; P43628; -.
DR BioGRID; 110005; 63.
DR IntAct; P43628; 76.
DR MINT; P43628; -.
DR STRING; 9606.ENSP00000342215; -.
DR ChEMBL; CHEMBL3713026; -.
DR GlyGen; P43628; 3 sites.
DR iPTMnet; P43628; -.
DR PhosphoSitePlus; P43628; -.
DR BioMuta; KIR2DL3; -.
DR DMDM; 1171727; -.
DR jPOST; P43628; -.
DR MassIVE; P43628; -.
DR PaxDb; P43628; -.
DR PeptideAtlas; P43628; -.
DR PRIDE; P43628; -.
DR ProteomicsDB; 55641; -. [P43628-1]
DR ProteomicsDB; 55642; -. [P43628-2]
DR TopDownProteomics; P43628-1; -. [P43628-1]
DR ABCD; P43628; 1 sequenced antibody.
DR Antibodypedia; 35081; 535 antibodies from 32 providers.
DR DNASU; 3804; -.
DR Ensembl; ENST00000342376.4; ENSP00000342215.3; ENSG00000243772.8. [P43628-1]
DR Ensembl; ENST00000610407.4; ENSP00000478848.1; ENSG00000274830.5.
DR Ensembl; ENST00000611207.4; ENSP00000478657.1; ENSG00000276218.5. [P43628-1]
DR Ensembl; ENST00000611369.4; ENSP00000483975.1; ENSG00000277484.5. [P43628-1]
DR Ensembl; ENST00000611821.4; ENSP00000484459.1; ENSG00000276590.5. [P43628-1]
DR Ensembl; ENST00000611990.4; ENSP00000479121.1; ENSG00000278327.5. [P43628-1]
DR Ensembl; ENST00000614792.4; ENSP00000481237.1; ENSG00000277554.5. [P43628-1]
DR Ensembl; ENST00000615091.4; ENSP00000483551.1; ENSG00000275658.5. [P43628-1]
DR Ensembl; ENST00000615739.1; ENSP00000478136.1; ENSG00000273887.1.
DR Ensembl; ENST00000617150.4; ENSP00000481159.1; ENSG00000274952.5.
DR Ensembl; ENST00000617242.4; ENSP00000483883.1; ENSG00000274410.5. [P43628-1]
DR Ensembl; ENST00000617404.1; ENSP00000481478.1; ENSG00000275008.1. [P43628-1]
DR Ensembl; ENST00000617593.4; ENSP00000483192.1; ENSG00000274108.5. [P43628-1]
DR Ensembl; ENST00000617790.4; ENSP00000481355.1; ENSG00000275623.5. [P43628-1]
DR Ensembl; ENST00000619702.1; ENSP00000480464.1; ENSG00000274402.1. [P43628-1]
DR Ensembl; ENST00000619995.4; ENSP00000480087.1; ENSG00000277317.5. [P43628-1]
DR Ensembl; ENST00000620549.4; ENSP00000483419.1; ENSG00000277924.5. [P43628-1]
DR Ensembl; ENST00000622644.4; ENSP00000482830.1; ENSG00000276459.5. [P43628-1]
DR Ensembl; ENST00000638813.2; ENSP00000492856.1; ENSG00000284333.2. [P43628-1]
DR Ensembl; ENST00000638851.2; ENSP00000491452.1; ENSG00000283708.2. [P43628-1]
DR Ensembl; ENST00000639089.2; ENSP00000491264.1; ENSG00000283702.2. [P43628-1]
DR Ensembl; ENST00000639101.2; ENSP00000492356.1; ENSG00000283790.2. [P43628-1]
DR Ensembl; ENST00000639176.2; ENSP00000491273.1; ENSG00000284504.2. [P43628-1]
DR Ensembl; ENST00000640485.2; ENSP00000491955.1; ENSG00000284510.2. [P43628-1]
DR GeneID; 3804; -.
DR KEGG; hsa:3804; -.
DR MANE-Select; ENST00000342376.4; ENSP00000342215.3; NM_015868.3; NP_056952.2.
DR UCSC; uc002qgx.4; human. [P43628-1]
DR CTD; 3804; -.
DR DisGeNET; 3804; -.
DR GeneCards; KIR2DL3; -.
DR HGNC; HGNC:6331; KIR2DL3.
DR HPA; ENSG00000243772; Tissue enhanced (lymphoid).
DR MIM; 604938; gene.
DR neXtProt; NX_P43628; -.
DR OpenTargets; ENSG00000243772; -.
DR PharmGKB; PA30116; -.
DR VEuPathDB; HostDB:ENSG00000243772; -.
DR eggNOG; ENOG502RU21; Eukaryota.
DR GeneTree; ENSGT01000000214458; -.
DR InParanoid; P43628; -.
DR OMA; PELHGHH; -.
DR PhylomeDB; P43628; -.
DR TreeFam; TF352669; -.
DR PathwayCommons; P43628; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; P43628; -.
DR BioGRID-ORCS; 3804; 16 hits in 976 CRISPR screens.
DR ChiTaRS; KIR2DL3; human.
DR EvolutionaryTrace; P43628; -.
DR GenomeRNAi; 3804; -.
DR Pharos; P43628; Tbio.
DR PRO; PR:P43628; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P43628; protein.
DR Bgee; ENSG00000243772; Expressed in granulocyte and 32 other tissues.
DR ExpressionAtlas; P43628; baseline and differential.
DR Genevisible; P43628; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003823; F:antigen binding; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 2.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..341
FT /note="Killer cell immunoglobulin-like receptor 2DL3"
FT /id="PRO_0000015080"
FT TOPO_DOM 22..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..107
FT /note="Ig-like C2-type 1"
FT DOMAIN 142..205
FT /note="Ig-like C2-type 2"
FT REGION 220..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..100
FT /evidence="ECO:0000250|UniProtKB:P43626"
FT DISULFID 149..198
FT /evidence="ECO:0000250|UniProtKB:P43626"
FT VAR_SEQ 117..214
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8662091"
FT /id="VSP_007814"
FT VARIANT 9
FT /note="V -> A (in dbSNP:rs3810343)"
FT /evidence="ECO:0000269|PubMed:9059894,
FT ECO:0000269|PubMed:9430221"
FT /id="VAR_010313"
FT VARIANT 32
FT /note="L -> R (in dbSNP:rs202032116)"
FT /evidence="ECO:0000269|PubMed:9059894,
FT ECO:0000269|PubMed:9430221"
FT /id="VAR_010314"
FT VARIANT 34
FT /note="H -> Q (in dbSNP:rs683003)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_015967"
FT VARIANT 37
FT /note="P -> R (in dbSNP:rs613240)"
FT /id="VAR_049978"
FT VARIANT 56
FT /note="Q -> E (in dbSNP:rs35719984)"
FT /evidence="ECO:0000269|PubMed:9059894,
FT ECO:0000269|PubMed:9430221"
FT /id="VAR_010315"
FT VARIANT 66
FT /note="F -> Y (in dbSNP:rs78713511)"
FT /id="VAR_049979"
FT VARIANT 71
FT /note="H -> R (in dbSNP:rs138897134)"
FT /evidence="ECO:0000269|PubMed:9059894,
FT ECO:0000269|PubMed:9430221"
FT /id="VAR_010316"
FT VARIANT 229
FT /note="P -> L (in dbSNP:rs35861855)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8662091, ECO:0000269|PubMed:9234478"
FT /id="VAR_015968"
FT VARIANT 242
FT /note="R -> I"
FT /evidence="ECO:0000269|PubMed:9059894"
FT /id="VAR_015969"
FT VARIANT 304
FT /note="A -> T (in dbSNP:rs4020187)"
FT /evidence="ECO:0000269|PubMed:8662091"
FT /id="VAR_015970"
FT VARIANT 318
FT /note="R -> H (in dbSNP:rs1049267)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8662091, ECO:0000269|PubMed:9059894,
FT ECO:0000269|PubMed:9430221"
FT /id="VAR_010317"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:6PAG"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1B6U"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:6PAG"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1B6U"
SQ SEQUENCE 341 AA; 37886 MW; C21EAFF80EA9AAB2 CRC64;
MSLMVVSMVC VGFFLLQGAW PHEGVHRKPS LLAHPGPLVK SEETVILQCW SDVRFQHFLL
HREGKFKDTL HLIGEHHDGV SKANFSIGPM MQDLAGTYRC YGSVTHSPYQ LSAPSDPLDI
VITGLYEKPS LSAQPGPTVL AGESVTLSCS SRSSYDMYHL SREGEAHERR FSAGPKVNGT
FQADFPLGPA THGGTYRCFG SFRDSPYEWS NSSDPLLVSV TGNPSNSWPS PTEPSSETGN
PRHLHVLIGT SVVIILFILL LFFLLHRWCC NKKNAVVMDQ EPAGNRTVNR EDSDEQDPQE
VTYAQLNHCV FTQRKITRPS QRPKTPPTDI IVYTELPNAE P
