CLC4K_HUMAN
ID CLC4K_HUMAN Reviewed; 328 AA.
AC Q9UJ71;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=C-type lectin domain family 4 member K;
DE AltName: Full=Langerin;
DE AltName: CD_antigen=CD207;
GN Name=CD207; Synonyms=CLEC4K;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND VARIANT ALA-278.
RX PubMed=10661407; DOI=10.1016/s1074-7613(00)80160-0;
RA Valladeau J., Ravel O., Dezutter-Dambuyant C., Moore K., Kleijmeer M.,
RA Liu Y., Duvert-Frances V., Vincent C., Schmitt D., Davoust J., Caux C.,
RA Lebecque S., Saeland S.;
RT "Langerin, a novel C-type lectin specific to Langerhans cells, is an
RT endocytic receptor that induces the formation of Birbeck granules.";
RL Immunity 12:71-81(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [4]
RP SUBUNIT.
RX PubMed=12626394; DOI=10.1093/glycob/cwg045;
RA Stambach N.S., Taylor M.E.;
RT "Characterization of carbohydrate recognition by langerin, a C-type lectin
RT of Langerhans cells.";
RL Glycobiology 13:401-410(2003).
RN [5]
RP REVIEW.
RX PubMed=14610287; DOI=10.1385/ir:28:2:93;
RA Valladeau J., Dezutter-Dambuyant C., Saeland S.;
RT "Langerin/CD207 sheds light on formation of Birbeck granules and their
RT possible function in Langerhans cells.";
RL Immunol. Res. 28:93-107(2003).
RN [6]
RP FUNCTION.
RX PubMed=17334373; DOI=10.1038/nm1541;
RA de Witte L., Nabatov A., Pion M., Fluitsma D., de Jong M.A., de Gruijl T.,
RA Piguet V., van Kooyk Y., Geijtenbeek T.B.;
RT "Langerin is a natural barrier to HIV-1 transmission by Langerhans cells.";
RL Nat. Med. 13:367-371(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DOMAIN C-TYPE LECTIN, AND MUTAGENESIS OF
RP GLU-285; ASN-287; LYS-299 AND LYS-313.
RX PubMed=20026605; DOI=10.1074/jbc.m109.041863;
RA Tateno H., Ohnishi K., Yabe R., Hayatsu N., Sato T., Takeya M.,
RA Narimatsu H., Hirabayashi J.;
RT "Dual specificity of langerin to sulfated and mannosylated glycans via a
RT single C-type carbohydrate recognition domain.";
RL J. Biol. Chem. 285:6390-6400(2010).
RN [9]
RP FUNCTION.
RX PubMed=20097424; DOI=10.1016/j.molimm.2009.12.016;
RA de Jong M.A., Vriend L.E., Theelen B., Taylor M.E., Fluitsma D.,
RA Boekhout T., Geijtenbeek T.B.;
RT "C-type lectin Langerin is a beta-glucan receptor on human Langerhans cells
RT that recognizes opportunistic and pathogenic fungi.";
RL Mol. Immunol. 47:1216-1225(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 188-328, AND DISULFIDE BONDS.
RX PubMed=19175323; DOI=10.1021/bi802151w;
RA Thepaut M., Valladeau J., Nurisso A., Kahn R., Arnou B., Vives C.,
RA Saeland S., Ebel C., Monnier C., Dezutter-Dambuyant C., Imberty A.,
RA Fieschi F.;
RT "Structural studies of langerin and Birbeck granule: a macromolecular
RT organization model.";
RL Biochemistry 48:2684-2698(2009).
RN [11]
RP VARIANT BIRGD ARG-264.
RX PubMed=15816828; DOI=10.1111/j.0022-202x.2005.23645.x;
RA Verdijk P., Dijkman R., Plasmeijer E.I., Mulder A.A., Zoutman W.H.,
RA Mieke Mommaas A., Tensen C.P.;
RT "A lack of Birbeck granules in Langerhans cells is associated with a
RT naturally occurring point mutation in the human Langerin gene.";
RL J. Invest. Dermatol. 124:714-717(2005).
RN [12]
RP VARIANTS ALA-278; ASP-288 AND PRO-300, CHARACTERIZATION OF VARIANT BIRGD
RP ARG-264, AND CHARACTERIZATION OF VARIANTS ALA-278; ASP-288 AND PRO-300.
RX PubMed=16567809; DOI=10.1074/jbc.m511502200;
RA Ward E.M., Stambach N.S., Drickamer K., Taylor M.E.;
RT "Polymorphisms in human langerin affect stability and sugar binding
RT activity.";
RL J. Biol. Chem. 281:15450-15456(2006).
CC -!- FUNCTION: Calcium-dependent lectin displaying mannose-binding
CC specificity. Induces the formation of Birbeck granules (BGs); is a
CC potent regulator of membrane superimposition and zippering. Binds to
CC sulfated as well as mannosylated glycans, keratan sulfate (KS) and
CC beta-glucans. Facilitates uptake of antigens and is involved in the
CC routing and/or processing of antigen for presentation to T cells. Major
CC receptor on primary Langerhans cells for Candida species, Saccharomyces
CC species, and Malassezia furfur. Protects against human immunodeficiency
CC virus-1 (HIV-1) infection. Binds to high-mannose structures present on
CC the envelope glycoprotein which is followed by subsequent targeting of
CC the virus to the Birbeck granules leading to its rapid degradation.
CC {ECO:0000269|PubMed:10661407, ECO:0000269|PubMed:17334373,
CC ECO:0000269|PubMed:20026605, ECO:0000269|PubMed:20097424}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12626394}.
CC -!- INTERACTION:
CC Q9UJ71; O43889-2: CREB3; NbExp=3; IntAct=EBI-2873235, EBI-625022;
CC Q9UJ71; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2873235, EBI-781551;
CC Q9UJ71; Q96HH9: GRAMD2B; NbExp=6; IntAct=EBI-2873235, EBI-2832937;
CC Q9UJ71; O00767: SCD; NbExp=3; IntAct=EBI-2873235, EBI-2684237;
CC Q9UJ71; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-2873235, EBI-8652744;
CC Q9UJ71; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-2873235, EBI-748373;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10661407}; Single-
CC pass type II membrane protein {ECO:0000269|PubMed:10661407}. Note=Found
CC in Birbeck granules (BGs), which are organelles consisting of
CC superimposed and zippered membranes.
CC -!- TISSUE SPECIFICITY: Exclusively expressed by Langerhans cells.
CC Expressed in astrocytoma and malignant ependymoma, but not in normal
CC brain tissues. {ECO:0000269|PubMed:10661407,
CC ECO:0000269|PubMed:20026605}.
CC -!- DOMAIN: The C-type lectin domain mediates dual recognition of both
CC sulfated and mannosylated glycans. {ECO:0000269|PubMed:20026605}.
CC -!- DISEASE: Birbeck granule deficiency (BIRGD) [MIM:613393]: A condition
CC characterized by the absence of Birbeck granules in epidermal
CC Langerhans cells. Despite the lack of Birbeck granules, Langerhans
CC cells are present in normal numbers and have normal morphologic
CC characteristics and antigen-presenting capacity.
CC {ECO:0000269|PubMed:15816828, ECO:0000269|PubMed:16567809}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Langerin;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_00126";
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DR EMBL; AJ242859; CAB62403.1; -; mRNA.
DR EMBL; AC007395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022278; AAH22278.1; -; mRNA.
DR CCDS; CCDS74520.1; -.
DR RefSeq; NP_056532.4; NM_015717.4.
DR RefSeq; XP_011531176.1; XM_011532874.1.
DR PDB; 3C22; X-ray; 1.50 A; A/B/C/D=188-328.
DR PDB; 3KQG; X-ray; 2.30 A; A/B/C/D/E/F=147-328.
DR PDB; 3P5D; X-ray; 1.80 A; A/B/C/D=193-328.
DR PDB; 3P5E; X-ray; 1.70 A; A/B/C/D=193-328.
DR PDB; 3P5F; X-ray; 1.75 A; A/B/C/D=193-328.
DR PDB; 3P5G; X-ray; 1.60 A; A/B/C/D=193-328.
DR PDB; 3P5H; X-ray; 1.61 A; A/B/C/D=193-328.
DR PDB; 3P5I; X-ray; 1.80 A; A/B/C/D=193-328.
DR PDB; 3P7F; X-ray; 2.50 A; A/B/C/D=193-328.
DR PDB; 3P7G; X-ray; 1.60 A; A/B/C/D=193-328.
DR PDB; 3P7H; X-ray; 2.30 A; A/B/C/D=193-328.
DR PDB; 4AK8; X-ray; 1.40 A; A/B/C/D=188-328.
DR PDB; 4N32; X-ray; 1.75 A; A/B/C/D=193-328.
DR PDB; 4N33; X-ray; 1.85 A; A/B/C/D=193-328.
DR PDB; 4N34; X-ray; 1.75 A; A/B/C/D=193-328.
DR PDB; 4N35; X-ray; 1.85 A; A/B/C/D=193-328.
DR PDB; 4N36; X-ray; 1.85 A; A/B/C/D=193-328.
DR PDB; 4N37; X-ray; 2.00 A; A/B/C/D=193-328.
DR PDB; 4N38; X-ray; 2.00 A; A/B/C/D=193-328.
DR PDB; 5G6U; X-ray; 1.84 A; A/B/C/D=68-328.
DR PDBsum; 3C22; -.
DR PDBsum; 3KQG; -.
DR PDBsum; 3P5D; -.
DR PDBsum; 3P5E; -.
DR PDBsum; 3P5F; -.
DR PDBsum; 3P5G; -.
DR PDBsum; 3P5H; -.
DR PDBsum; 3P5I; -.
DR PDBsum; 3P7F; -.
DR PDBsum; 3P7G; -.
DR PDBsum; 3P7H; -.
DR PDBsum; 4AK8; -.
DR PDBsum; 4N32; -.
DR PDBsum; 4N33; -.
DR PDBsum; 4N34; -.
DR PDBsum; 4N35; -.
DR PDBsum; 4N36; -.
DR PDBsum; 4N37; -.
DR PDBsum; 4N38; -.
DR PDBsum; 5G6U; -.
DR AlphaFoldDB; Q9UJ71; -.
DR SMR; Q9UJ71; -.
DR BioGRID; 119076; 25.
DR IntAct; Q9UJ71; 13.
DR STRING; 9606.ENSP00000386378; -.
DR BindingDB; Q9UJ71; -.
DR ChEMBL; CHEMBL2176853; -.
DR UniLectin; Q9UJ71; -.
DR GlyGen; Q9UJ71; 3 sites.
DR iPTMnet; Q9UJ71; -.
DR PhosphoSitePlus; Q9UJ71; -.
DR BioMuta; CD207; -.
DR DMDM; 229784129; -.
DR jPOST; Q9UJ71; -.
DR MassIVE; Q9UJ71; -.
DR PaxDb; Q9UJ71; -.
DR PeptideAtlas; Q9UJ71; -.
DR PRIDE; Q9UJ71; -.
DR ProteomicsDB; 84594; -.
DR Antibodypedia; 2366; 504 antibodies from 36 providers.
DR DNASU; 50489; -.
DR Ensembl; ENST00000410009.5; ENSP00000386378.3; ENSG00000116031.9.
DR GeneID; 50489; -.
DR KEGG; hsa:50489; -.
DR MANE-Select; ENST00000410009.5; ENSP00000386378.3; NM_015717.5; NP_056532.4.
DR UCSC; uc002shg.4; human.
DR CTD; 50489; -.
DR DisGeNET; 50489; -.
DR GeneCards; CD207; -.
DR HGNC; HGNC:17935; CD207.
DR HPA; ENSG00000116031; Tissue enriched (skin).
DR MalaCards; CD207; -.
DR MIM; 604862; gene.
DR MIM; 613393; phenotype.
DR neXtProt; NX_Q9UJ71; -.
DR OpenTargets; ENSG00000116031; -.
DR PharmGKB; PA134986203; -.
DR VEuPathDB; HostDB:ENSG00000116031; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000161863; -.
DR HOGENOM; CLU_081746_0_0_1; -.
DR InParanoid; Q9UJ71; -.
DR OMA; QFCVSRN; -.
DR OrthoDB; 988771at2759; -.
DR PhylomeDB; Q9UJ71; -.
DR TreeFam; TF333341; -.
DR PathwayCommons; Q9UJ71; -.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR SignaLink; Q9UJ71; -.
DR BioGRID-ORCS; 50489; 9 hits in 318 CRISPR screens.
DR EvolutionaryTrace; Q9UJ71; -.
DR GeneWiki; Langerin; -.
DR GenomeRNAi; 50489; -.
DR Pharos; Q9UJ71; Tbio.
DR PRO; PR:Q9UJ71; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UJ71; protein.
DR Bgee; ENSG00000116031; Expressed in upper leg skin and 87 other tissues.
DR Genevisible; Q9UJ71; HS.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0030139; C:endocytic vesicle; TAS:ProtInc.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0005537; F:mannose binding; TAS:ProtInc.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR CDD; cd03590; CLECT_DC-SIGN_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; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..328
FT /note="C-type lectin domain family 4 member K"
FT /id="PRO_0000223693"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..328
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 202..320
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT COILED 145..190
FT /evidence="ECO:0000255"
FT CARBOHYD 87
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 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 223..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19175323"
FT DISULFID 295..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19175323"
FT VARIANT 55
FT /note="A -> V (in dbSNP:rs10489990)"
FT /id="VAR_054781"
FT VARIANT 136
FT /note="Q -> E (in dbSNP:rs17718987)"
FT /id="VAR_056151"
FT VARIANT 213
FT /note="P -> S (in dbSNP:rs17006436)"
FT /id="VAR_054782"
FT VARIANT 264
FT /note="W -> R (in BIRGD; abolishes mannose-binding ability;
FT dbSNP:rs200837270)"
FT /evidence="ECO:0000269|PubMed:15816828,
FT ECO:0000269|PubMed:16567809"
FT /id="VAR_063828"
FT VARIANT 278
FT /note="V -> A (no effect on mannose-binding ability;
FT dbSNP:rs741326)"
FT /evidence="ECO:0000269|PubMed:10661407,
FT ECO:0000269|PubMed:16567809"
FT /id="VAR_054783"
FT VARIANT 288
FT /note="N -> D (significant reduction in mannose-binding
FT ability; dbSNP:rs13383830)"
FT /evidence="ECO:0000269|PubMed:16567809"
FT /id="VAR_054784"
FT VARIANT 300
FT /note="A -> P (significant reduction in mannose-binding
FT ability; significant decrease in thermal stability;
FT increased sensitivity of sugar binding to pH change;
FT dbSNP:rs2080391)"
FT /evidence="ECO:0000269|PubMed:16567809"
FT /id="VAR_059448"
FT MUTAGEN 285
FT /note="E->A: Loss of binding to 6'-sulfo-LacNAc and
FT invertase."
FT /evidence="ECO:0000269|PubMed:20026605"
FT MUTAGEN 287
FT /note="N->A: Loss of binding to 6'-sulfo-LacNAc and
FT invertase."
FT /evidence="ECO:0000269|PubMed:20026605"
FT MUTAGEN 299
FT /note="K->A: Loss of binding to 6'-sulfo-LacNAc."
FT /evidence="ECO:0000269|PubMed:20026605"
FT MUTAGEN 313
FT /note="K->A: Loss of binding to 6'-sulfo-LacNAc and 6-
FT sulfo-GlcNAc."
FT /evidence="ECO:0000269|PubMed:20026605"
FT HELIX 160..195
FT /evidence="ECO:0007829|PDB:3KQG"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:3KQG"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:4AK8"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:4AK8"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:4AK8"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:4AK8"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:4AK8"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:4AK8"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:4AK8"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:4AK8"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:4AK8"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:4AK8"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:4AK8"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:4AK8"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:4AK8"
FT STRAND 315..322
FT /evidence="ECO:0007829|PDB:4AK8"
SQ SEQUENCE 328 AA; 36725 MW; 83DF432682BF4B62 CRC64;
MTVEKEAPDA HFTVDKQNIS LWPREPPPKS GPSLVPGKTP TVRAALICLT LVLVASVLLQ
AVLYPRFMGT ISDVKTNVQL LKGRVDNIST LDSEIKKNSD GMEAAGVQIQ MVNESLGYVR
SQFLKLKTSV EKANAQIQIL TRSWEEVSTL NAQIPELKSD LEKASALNTK IRALQGSLEN
MSKLLKRQND ILQVVSQGWK YFKGNFYYFS LIPKTWYSAE QFCVSRNSHL TSVTSESEQE
FLYKTAGGLI YWIGLTKAGM EGDWSWVDDT PFNKVQSVRF WIPGEPNNAG NNEHCGNIKA
PSLQAWNDAP CDKTFLFICK RPYVPSEP
