GenomeNet

Database: UniProt
Entry: Q13241
LinkDB: Q13241
Original site: Q13241 
ID   KLRD1_HUMAN             Reviewed;         179 AA.
AC   Q13241; O43321; O43773; Q9UBE3; Q9UEQ0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   10-APR-2019, entry version 170.
DE   RecName: Full=Natural killer cells antigen CD94;
DE   AltName: Full=KP43;
DE   AltName: Full=Killer cell lectin-like receptor subfamily D member 1;
DE   AltName: Full=NK cell receptor;
DE   AltName: CD_antigen=CD94 {ECO:0000303|PubMed:18083576};
GN   Name=KLRD1; Synonyms=CD94;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-25.
RC   TISSUE=Blood;
RX   PubMed=7589107; DOI=10.1002/eji.1830250904;
RA   Chang C., Rodriguez A., Carretero M., Lopez-Botet M., Phillips J.H.,
RA   Lanier L.L.;
RT   "Molecular characterization of human CD94: a type II membrane
RT   glycoprotein related to the C-type lectin superfamily.";
RL   Eur. J. Immunol. 25:2433-2437(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-25.
RC   TISSUE=Placenta;
RX   PubMed=9472066; DOI=10.1007/s002510050362;
RA   Rodriguez A., Carretero M., Glienke J., Bellon T., Ramirez A.,
RA   Lehrach H., Francis F., Lopez-Botet M.;
RT   "Structure of the human CD94 C-type lectin gene.";
RL   Immunogenetics 47:305-309(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA   Biassoni R.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3).
RX   PubMed=9601951; DOI=10.1007/s002510050407;
RA   Furukawa H., Yabe T., Watanabe K., Miyamoto R., Akaza T., Tadokoro K.,
RA   Tohma S., Inoue T., Yamamoto K., Juji T.;
RT   "A alternatively spliced form of the human CD94 gene.";
RL   Immunogenetics 48:87-88(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   ALA-25.
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH TYROBP.
RX   PubMed=9655483;
RA   Lanier L.L., Corliss B., Wu J., Phillips J.H.;
RT   "Association of DAP12 with activating CD94/NKG2C NK cell receptors.";
RL   Immunity 8:693-701(1998).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 52-179, FUNCTION, AND
RP   DISULFIDE BONDS.
RX   PubMed=10023772; DOI=10.1016/S1074-7613(00)80008-4;
RA   Boyington J.C., Riaz A.N., Patamawenu A., Coligan J.E., Brooks A.G.,
RA   Sun P.D.;
RT   "Structure of CD94 reveals a novel C-type lectin fold: implications
RT   for the NK cell-associated CD94/NKG2 receptors.";
RL   Immunity 10:75-82(1999).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 57-179 IN COMPLEX WITH NGK2A,
RP   FUNCTION, SUBUNIT, DISULFIDE BONDS, AND MUTAGENESIS OF GLN-79;
RP   GLN-112; PHE-114; THR-146; ASN-148; ASN-158; ASN-160; LEU-162;
RP   ASP-163; GLU-164 AND ASP-168.
RX   PubMed=18083576; DOI=10.1016/j.immuni.2007.10.013;
RA   Sullivan L.C., Clements C.S., Beddoe T., Johnson D., Hoare H.L.,
RA   Lin J., Huyton T., Hopkins E.J., Reid H.H., Wilce M.C., Kabat J.,
RA   Borrego F., Coligan J.E., Rossjohn J., Brooks A.G.;
RT   "The heterodimeric assembly of the CD94-NKG2 receptor family and
RT   implications for human leukocyte antigen-E recognition.";
RL   Immunity 27:900-911(2007).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (4.41 ANGSTROMS) OF 59-179 IN COMPLEX WITH
RP   NGK2A, SUBUNIT, AND DISULFIDE BONDS.
RX   PubMed=18448674; DOI=10.1073/pnas.0802736105;
RA   Kaiser B.K., Pizarro J.C., Kerns J., Strong R.K.;
RT   "Structural basis for NKG2A/CD94 recognition of HLA-E.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:6696-6701(2008).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 57-179 IN COMPLEX WITH NGK2A,
RP   SUBUNIT, AND DISULFIDE BONDS.
RX   PubMed=18332182; DOI=10.1084/jem.20072525;
RA   Petrie E.J., Clements C.S., Lin J., Sullivan L.C., Johnson D.,
RA   Huyton T., Heroux A., Hoare H.L., Beddoe T., Reid H.H., Wilce M.C.,
RA   Brooks A.G., Rossjohn J.;
RT   "CD94-NKG2A recognition of human leukocyte antigen (HLA)-E bound to an
RT   HLA class I leader sequence.";
RL   J. Exp. Med. 205:725-735(2008).
CC   -!- FUNCTION: Plays a role as a receptor for the recognition of MHC
CC       class I HLA-E molecules by NK cells and some cytotoxic T-cells.
CC       {ECO:0000269|PubMed:10023772, ECO:0000269|PubMed:18083576,
CC       ECO:0000269|PubMed:9655483}.
CC   -!- SUBUNIT: Can form disulfide-bonded heterodimer with NKG2 family
CC       members (PubMed:18083576, PubMed:18332182, PubMed:18448674).
CC       KLRD1-KLRC1 heterodimer interacts with peptide-bound HLA-E-B2M
CC       heterotrimeric complex. KLRD1 plays a prominent role in directly
CC       interacting with HLA-E (PubMed:18083576). Interacts with the
CC       adapter protein TYROBP/DAP12; the interaction leads to natural
CC       killer cell activation (PubMed:9655483).
CC       {ECO:0000269|PubMed:18083576, ECO:0000269|PubMed:18332182,
CC       ECO:0000269|PubMed:18448674, ECO:0000269|PubMed:9655483}.
CC   -!- INTERACTION:
CC       P26715:KLRC1; NbExp=5; IntAct=EBI-9018174, EBI-9018187;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
CC       type II membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=CD94-A;
CC         IsoId=Q13241-1; Sequence=Displayed;
CC       Name=2; Synonyms=CD94-B;
CC         IsoId=Q13241-2; Sequence=VSP_003053;
CC       Name=3; Synonyms=CD94 alt;
CC         IsoId=Q13241-3; Sequence=VSP_003052;
CC   -!- TISSUE SPECIFICITY: Natural killer cells.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=CD94;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_238";
DR   EMBL; U30610; AAC50291.1; -; mRNA.
DR   EMBL; Y14287; CAA74663.1; -; Genomic_DNA.
DR   EMBL; Y14288; CAA74663.1; JOINED; Genomic_DNA.
DR   EMBL; AJ000673; CAA04230.1; -; Genomic_DNA.
DR   EMBL; AJ000001; CAA03845.1; -; mRNA.
DR   EMBL; AB009597; BAA24450.1; -; mRNA.
DR   EMBL; AB010084; BAA24451.1; -; Genomic_DNA.
DR   EMBL; AC022075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC028009; AAH28009.1; -; mRNA.
DR   CCDS; CCDS8621.1; -. [Q13241-1]
DR   CCDS; CCDS8622.1; -. [Q13241-3]
DR   RefSeq; NP_001107868.1; NM_001114396.1. [Q13241-1]
DR   RefSeq; NP_002253.1; NM_002262.3. [Q13241-1]
DR   RefSeq; NP_031360.1; NM_007334.2. [Q13241-3]
DR   RefSeq; XP_016874780.1; XM_017019291.1.
DR   UniGene; Hs.562457; -.
DR   PDB; 1B6E; X-ray; 2.60 A; A=52-179.
DR   PDB; 3BDW; X-ray; 2.50 A; A/C=57-179.
DR   PDB; 3CDG; X-ray; 3.40 A; E/J=57-179.
DR   PDB; 3CII; X-ray; 4.41 A; G/I=59-179.
DR   PDBsum; 1B6E; -.
DR   PDBsum; 3BDW; -.
DR   PDBsum; 3CDG; -.
DR   PDBsum; 3CII; -.
DR   ProteinModelPortal; Q13241; -.
DR   SMR; Q13241; -.
DR   BioGrid; 110023; 25.
DR   IntAct; Q13241; 2.
DR   STRING; 9606.ENSP00000371333; -.
DR   iPTMnet; Q13241; -.
DR   PhosphoSitePlus; Q13241; -.
DR   BioMuta; KLRD1; -.
DR   DMDM; 334302835; -.
DR   PaxDb; Q13241; -.
DR   PeptideAtlas; Q13241; -.
DR   PRIDE; Q13241; -.
DR   ProteomicsDB; 59243; -.
DR   ProteomicsDB; 59244; -. [Q13241-2]
DR   ProteomicsDB; 59245; -. [Q13241-3]
DR   DNASU; 3824; -.
DR   Ensembl; ENST00000336164; ENSP00000338130; ENSG00000134539. [Q13241-1]
DR   Ensembl; ENST00000350274; ENSP00000310929; ENSG00000134539. [Q13241-3]
DR   Ensembl; ENST00000381908; ENSP00000371333; ENSG00000134539. [Q13241-1]
DR   GeneID; 3824; -.
DR   KEGG; hsa:3824; -.
DR   UCSC; uc001qxw.5; human. [Q13241-1]
DR   CTD; 3824; -.
DR   DisGeNET; 3824; -.
DR   EuPathDB; HostDB:ENSG00000134539.16; -.
DR   GeneCards; KLRD1; -.
DR   HGNC; HGNC:6378; KLRD1.
DR   HPA; HPA069688; -.
DR   MIM; 602894; gene.
DR   neXtProt; NX_Q13241; -.
DR   OpenTargets; ENSG00000134539; -.
DR   PharmGKB; PA30167; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   eggNOG; ENOG410XPJ1; LUCA.
DR   GeneTree; ENSGT00940000160107; -.
DR   HOGENOM; HOG000220925; -.
DR   HOVERGEN; HBG099800; -.
DR   InParanoid; Q13241; -.
DR   KO; K06516; -.
DR   OMA; YSEEHHA; -.
DR   TreeFam; TF336674; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-2172127; DAP12 interactions.
DR   Reactome; R-HSA-2424491; DAP12 signaling.
DR   ChiTaRS; KLRD1; human.
DR   EvolutionaryTrace; Q13241; -.
DR   GeneWiki; KLRD1; -.
DR   GenomeRNAi; 3824; -.
DR   PRO; PR:Q13241; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000134539; Expressed in 114 organ(s), highest expression level in leukocyte.
DR   ExpressionAtlas; Q13241; baseline and differential.
DR   Genevisible; Q13241; HS.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0023024; F:MHC class I protein complex binding; IPI:UniProtKB.
DR   GO; GO:0023030; F:MHC class Ib protein binding, via antigen binding groove; IPI:UniProtKB.
DR   GO; GO:1990405; F:protein antigen binding; IDA:UniProtKB.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0002228; P:natural killer cell mediated immunity; IDA:UniProtKB.
DR   GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
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; IPR033992; NKR-like_CTLD.
DR   Pfam; PF00059; Lectin_C; 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; Alternative splicing; Cell membrane; Complete proteome;
KW   Disulfide bond; Glycoprotein; Lectin; Membrane; Polymorphism;
KW   Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    179       Natural killer cells antigen CD94.
FT                                /FTId=PRO_0000046587.
FT   TOPO_DOM      1     10       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     11     31       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     32    179       Extracellular. {ECO:0000255}.
FT   DOMAIN       68    175       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   CARBOHYD     83     83       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    132    132       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     58     70       {ECO:0000269|PubMed:18083576,
FT                                ECO:0000269|PubMed:18332182}.
FT   DISULFID     59     59       Interchain (with C-116 in NGK2A).
FT                                {ECO:0000269|PubMed:18083576,
FT                                ECO:0000269|PubMed:18332182}.
FT   DISULFID     61     72       {ECO:0000269|PubMed:10023772,
FT                                ECO:0000269|PubMed:18083576,
FT                                ECO:0000269|PubMed:18332182,
FT                                ECO:0000269|PubMed:18448674}.
FT   DISULFID     89    174       {ECO:0000269|PubMed:10023772,
FT                                ECO:0000269|PubMed:18083576,
FT                                ECO:0000269|PubMed:18332182,
FT                                ECO:0000269|PubMed:18448674}.
FT   DISULFID    152    166       {ECO:0000269|PubMed:10023772,
FT                                ECO:0000269|PubMed:18083576,
FT                                ECO:0000269|PubMed:18332182,
FT                                ECO:0000269|PubMed:18448674}.
FT   VAR_SEQ       1     34       MAVFKTTLWRLISGTLGIICLSLMSTLGILLKNS -> MAA
FT                                (in isoform 3).
FT                                {ECO:0000303|PubMed:9601951}.
FT                                /FTId=VSP_003052.
FT   VAR_SEQ     105    105       L -> LQ (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_003053.
FT   VARIANT      25     25       S -> A (in dbSNP:rs10772256).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:7589107,
FT                                ECO:0000269|PubMed:9472066}.
FT                                /FTId=VAR_050103.
FT   MUTAGEN      79     79       Q->A: Has no impact on the affinity for
FT                                HLA-E. {ECO:0000269|PubMed:18083576}.
FT   MUTAGEN     112    112       Q->A: Abolishes binding to HLA-E.
FT                                {ECO:0000269|PubMed:18083576}.
FT   MUTAGEN     114    114       F->A: Abolishes binding to HLA-E.
FT                                {ECO:0000269|PubMed:18083576}.
FT   MUTAGEN     146    146       T->A: Has no impact on the affinity for
FT                                HLA-E. {ECO:0000269|PubMed:18083576}.
FT   MUTAGEN     148    148       N->A: Has no impact on the affinity for
FT                                HLA-E. {ECO:0000269|PubMed:18083576}.
FT   MUTAGEN     158    158       N->A: Has no impact on the affinity for
FT                                HLA-E. {ECO:0000269|PubMed:18083576}.
FT   MUTAGEN     160    160       N->A: Abolishes binding to HLA-E.
FT                                {ECO:0000269|PubMed:18083576}.
FT   MUTAGEN     162    162       L->A: Abolishes binding to HLA-E.
FT                                {ECO:0000269|PubMed:18083576}.
FT   MUTAGEN     163    163       D->A: Impairs binding to HLA-E.
FT                                {ECO:0000269|PubMed:18083576}.
FT   MUTAGEN     164    164       E->A: Impairs binding to HLA-E.
FT                                {ECO:0000269|PubMed:18083576}.
FT   MUTAGEN     168    168       D->A: Reduces binding to HLA-E.
FT                                {ECO:0000269|PubMed:18083576}.
FT   TURN         62     64       {ECO:0000244|PDB:3BDW}.
FT   STRAND       66     68       {ECO:0000244|PDB:3BDW}.
FT   STRAND       71     75       {ECO:0000244|PDB:3BDW}.
FT   HELIX        82     91       {ECO:0000244|PDB:3BDW}.
FT   HELIX       102    108       {ECO:0000244|PDB:3BDW}.
FT   STRAND      118    122       {ECO:0000244|PDB:3BDW}.
FT   TURN        123    126       {ECO:0000244|PDB:3BDW}.
FT   STRAND      127    130       {ECO:0000244|PDB:3BDW}.
FT   TURN        138    140       {ECO:0000244|PDB:3BDW}.
FT   HELIX       142    146       {ECO:0000244|PDB:3BDW}.
FT   STRAND      151    156       {ECO:0000244|PDB:3BDW}.
FT   TURN        157    159       {ECO:0000244|PDB:3BDW}.
FT   STRAND      160    164       {ECO:0000244|PDB:3BDW}.
FT   STRAND      170    176       {ECO:0000244|PDB:3BDW}.
SQ   SEQUENCE   179 AA;  20513 MW;  01634D3832D4B1A7 CRC64;
     MAVFKTTLWR LISGTLGIIC LSLMSTLGIL LKNSFTKLSI EPAFTPGPNI ELQKDSDCCS
     CQEKWVGYRC NCYFISSEQK TWNESRHLCA SQKSSLLQLQ NTDELDFMSS SQQFYWIGLS
     YSEEHTAWLW ENGSALSQYL FPSFETFNTK NCIAYNPNGN ALDESCEDKN RYICKQQLI
//
DBGET integrated database retrieval system