CD48_HUMAN
ID CD48_HUMAN Reviewed; 243 AA.
AC P09326; Q5U055; Q8MGR0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=CD48 antigen;
DE AltName: Full=B-lymphocyte activation marker BLAST-1;
DE AltName: Full=BCM1 surface antigen;
DE AltName: Full=Leukocyte antigen MEM-102;
DE AltName: Full=SLAM family member 2;
DE Short=SLAMF2;
DE AltName: Full=Signaling lymphocytic activation molecule 2;
DE AltName: Full=TCT.1;
DE AltName: CD_antigen=CD48;
DE Flags: Precursor;
GN Name=CD48; Synonyms=BCM1, BLAST1;
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), AND SUBCELLULAR LOCATION.
RX PubMed=1999351; DOI=10.1007/bf00210824;
RA Vaughan H.A., Henning M.M., Purcell D.F.J., McKenzie I.F.C., Sandrin M.S.;
RT "The isolation of cDNA clones for CD48.";
RL Immunogenetics 33:113-117(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1999350; DOI=10.1007/bf00210823;
RA Korinek V., Stefanova I., Angelisova P., Hilbert I., Horejsi V.;
RT "The human leucocyte antigen CD48 (MEM-102) is closely related to the
RT activation marker Blast-1.";
RL Immunogenetics 33:108-112(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2828034; DOI=10.1002/j.1460-2075.1987.tb02703.x;
RA Staunton D.E., Thorley-Lawson D.A.;
RT "Molecular cloning of the lymphocyte activation marker Blast-1.";
RL EMBO J. 6:3695-3701(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=B-cell, and Pancreas;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX PubMed=1847502; DOI=10.1128/mcb.11.3.1614-1623.1991;
RA Fisher R.C., Thorley-Lawson D.A.;
RT "Characterization of the Epstein-Barr virus-inducible gene encoding the
RT human leukocyte adhesion and activation antigen BLAST-1 (CD48).";
RL Mol. Cell. Biol. 11:1614-1623(1991).
RN [9]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1827826; DOI=10.1084/jem.173.6.1339;
RA del Porto P., Mami-Chouaib F., Bruneau J.-M., Jitsukawa S., Dumas J.,
RA Harnois M., Hercend T.;
RT "TCT.1, a target molecule for gamma/delta T cells, is encoded by an
RT immunoglobulin superfamily gene (Blast-1) located in the CD1 region of
RT human chromosome 1.";
RL J. Exp. Med. 173:1339-1344(1991).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=9418191; DOI=10.1023/a:1027327912204;
RA Smith G.M., Biggs J., Norris B., Anderson-Stewart P., Ward R.;
RT "Detection of a soluble form of the leukocyte surface antigen CD48 in
RT plasma and its elevation in patients with lymphoid leukemias and
RT arthritis.";
RL J. Clin. Immunol. 17:502-509(1997).
RN [11]
RP INDUCTION BY INTERFERONS, AND SUBCELLULAR LOCATION.
RX PubMed=9041467; DOI=10.1089/jir.1997.17.17;
RA Tissot C., Rebouissou C., Klein B., Mechti N.;
RT "Both human alpha/beta and gamma interferons upregulate the expression of
RT CD48 cell surface molecules.";
RL J. Interferon Cytokine Res. 17:17-26(1997).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=9893294; DOI=10.1111/j.1442-200x.1998.tb01994.x;
RA Katsuura M., Shimizu Y., Akiba K., Kanazawa C., Mitsui T., Sendo D.,
RA Kawakami T., Hayasaka K., Yokoyama S.;
RT "CD48 expression on leukocytes in infectious diseases: flow cytometric
RT analysis of surface antigen.";
RL Acta Paediatr. Jpn. Overseas Ed. 40:580-585(1998).
RN [13]
RP FUNCTION, AND INTERACTION WITH CD244.
RX PubMed=9841922; DOI=10.1084/jem.188.11.2083;
RA Brown M.H., Boles K., van der Merwe P.A., Kumar V., Mathew P.A.,
RA Barclay A.N.;
RT "2B4, the natural killer and T cell immunoglobulin superfamily surface
RT protein, is a ligand for CD48.";
RL J. Exp. Med. 188:2083-2090(1998).
RN [14]
RP FUNCTION, AND INTERACTION WITH LCK.
RX PubMed=12007789; DOI=10.1016/s0167-4889(02)00165-9;
RA Hawash I.Y., Hu X.E., Adal A., Cassady J.M., Geahlen R.L., Harrison M.L.;
RT "The oxygen-substituted palmitic acid analogue, 13-oxypalmitic acid,
RT inhibits Lck localization to lipid rafts and T cell signaling.";
RL Biochim. Biophys. Acta 1589:140-150(2002).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-104 AND ASN-189.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [16]
RP FUNCTION.
RX PubMed=19494291; DOI=10.4049/jimmunol.0800691;
RA Muhammad A., Schiller H.B., Forster F., Eckerstorfer P., Geyeregger R.,
RA Leksa V., Zlabinger G.J., Sibilia M., Sonnleitner A., Paster W.,
RA Stockinger H.;
RT "Sequential cooperation of CD2 and CD48 in the buildup of the early TCR
RT signalosome.";
RL J. Immunol. 182:7672-7680(2009).
RN [17]
RP FUNCTION, AND INTERACTION WITH CD244.
RX PubMed=27249817; DOI=10.1098/rsob.160010;
RA Claus M., Wingert S., Watzl C.;
RT "Modulation of natural killer cell functions by interactions between 2B4
RT and CD48 in cis and in trans.";
RL Open Biol. 6:0-0(2016).
RN [18]
RP STRUCTURE BY NMR OF 24-140.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first Ig-like domain from human CD48 antigen.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Glycosylphosphatidylinositol (GPI)-anchored cell surface
CC glycoprotein that interacts via its N-terminal immunoglobulin domain
CC with cell surface receptors including 2B4/CD244 or CD2 to regulate
CC immune cell function and activation (PubMed:27249817, PubMed:12007789).
CC Participates in T-cell signaling transduction by associating with CD2
CC and efficiently bringing the Src family protein kinase LCK and LAT to
CC the TCR/CD3 complex (PubMed:19494291). In turn, promotes LCK
CC phosphorylation and subsequent activation (PubMed:12007789). Induces
CC the phosphorylation of the cytoplasmic immunoreceptortyrosine switch
CC motifs (ITSMs) of CD244 initiating a series of signaling events that
CC leads to the generation of the immunological synapse and the directed
CC release of cytolytic granules containing perforin and granzymes by T-
CC lymphocytes and NK-cells (PubMed:9841922, PubMed:27249817).
CC {ECO:0000269|PubMed:12007789, ECO:0000269|PubMed:19494291,
CC ECO:0000269|PubMed:27249817, ECO:0000269|PubMed:9841922}.
CC -!- SUBUNIT: Interacts with CD2. Interacts with CD244 (PubMed:9841922,
CC PubMed:27249817). Interacts with LCK (PubMed:12007789).
CC {ECO:0000269|PubMed:12007789, ECO:0000269|PubMed:27249817,
CC ECO:0000269|PubMed:9841922}.
CC -!- INTERACTION:
CC P09326; Q9BZW8: CD244; NbExp=4; IntAct=EBI-714770, EBI-1580565;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1999351,
CC ECO:0000269|PubMed:9041467}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:1999351}. Secreted {ECO:0000269|PubMed:9418191}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P09326-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09326-2; Sequence=VSP_055598, VSP_055599;
CC -!- TISSUE SPECIFICITY: Widely expressed on all hematopoietic cells.
CC {ECO:0000269|PubMed:9893294}.
CC -!- INDUCTION: By IFN-alpha/beta and IFN-gamma both at the level of CD48
CC mRNA and cell surface expression. {ECO:0000269|PubMed:9041467}.
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DR EMBL; M59904; AAA62834.1; -; mRNA.
DR EMBL; X06341; CAA29647.1; -; mRNA.
DR EMBL; M37766; AAA36211.1; -; mRNA.
DR EMBL; BT019813; AAV38616.1; -; mRNA.
DR EMBL; AL121985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52705.1; -; Genomic_DNA.
DR EMBL; BC016182; AAH16182.1; -; mRNA.
DR EMBL; BC030224; AAH30224.1; -; mRNA.
DR EMBL; M63911; AAA35602.1; -; Genomic_DNA.
DR CCDS; CCDS1208.1; -. [P09326-1]
DR PIR; A53244; A53244.
DR RefSeq; NP_001769.2; NM_001778.3. [P09326-1]
DR PDB; 2EDO; NMR; -; A=27-140.
DR PDBsum; 2EDO; -.
DR AlphaFoldDB; P09326; -.
DR SMR; P09326; -.
DR BioGRID; 107400; 47.
DR IntAct; P09326; 5.
DR STRING; 9606.ENSP00000484431; -.
DR TCDB; 8.A.23.1.36; the basigin (basigin) family.
DR GlyConnect; 1926; 7 N-Linked glycans (3 sites).
DR GlyGen; P09326; 7 sites, 7 N-linked glycans (3 sites).
DR iPTMnet; P09326; -.
DR PhosphoSitePlus; P09326; -.
DR SwissPalm; P09326; -.
DR BioMuta; CD48; -.
DR DMDM; 114871; -.
DR CPTAC; CPTAC-1199; -.
DR EPD; P09326; -.
DR jPOST; P09326; -.
DR MassIVE; P09326; -.
DR MaxQB; P09326; -.
DR PaxDb; P09326; -.
DR PeptideAtlas; P09326; -.
DR PRIDE; P09326; -.
DR ProteomicsDB; 52212; -. [P09326-1]
DR ProteomicsDB; 71445; -.
DR TopDownProteomics; P09326-1; -. [P09326-1]
DR Antibodypedia; 3737; 1150 antibodies from 47 providers.
DR CPTC; P09326; 1 antibody.
DR DNASU; 962; -.
DR Ensembl; ENST00000368045.3; ENSP00000357024.3; ENSG00000117091.10. [P09326-2]
DR Ensembl; ENST00000368046.8; ENSP00000357025.3; ENSG00000117091.10. [P09326-1]
DR GeneID; 962; -.
DR KEGG; hsa:962; -.
DR MANE-Select; ENST00000368046.8; ENSP00000357025.3; NM_001778.4; NP_001769.2.
DR UCSC; uc001fwn.4; human. [P09326-1]
DR CTD; 962; -.
DR DisGeNET; 962; -.
DR GeneCards; CD48; -.
DR HGNC; HGNC:1683; CD48.
DR HPA; ENSG00000117091; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 109530; gene.
DR neXtProt; NX_P09326; -.
DR OpenTargets; ENSG00000117091; -.
DR PharmGKB; PA26223; -.
DR VEuPathDB; HostDB:ENSG00000117091; -.
DR eggNOG; ENOG502SB68; Eukaryota.
DR GeneTree; ENSGT01030000234540; -.
DR HOGENOM; CLU_099885_0_0_1; -.
DR InParanoid; P09326; -.
DR OMA; YFNTKFK; -.
DR PhylomeDB; P09326; -.
DR TreeFam; TF334964; -.
DR PathwayCommons; P09326; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; P09326; -.
DR BioGRID-ORCS; 962; 15 hits in 1068 CRISPR screens.
DR EvolutionaryTrace; P09326; -.
DR GeneWiki; CD48; -.
DR GenomeRNAi; 962; -.
DR Pharos; P09326; Tbio.
DR PRO; PR:P09326; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P09326; protein.
DR Bgee; ENSG00000117091; Expressed in leukocyte and 137 other tissues.
DR ExpressionAtlas; P09326; baseline and differential.
DR Genevisible; P09326; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; TAS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003823; F:antigen binding; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR GO; GO:0002819; P:regulation of adaptive immune response; IEA:InterPro.
DR GO; GO:0042110; P:T cell activation; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR033548; CD48.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR12080:SF47; PTHR12080:SF47; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..220
FT /note="CD48 antigen"
FT /id="PRO_0000014881"
FT PROPEP 221..243
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000014882"
FT DOMAIN 29..127
FT /note="Ig-like C2-type 1"
FT DOMAIN 132..212
FT /note="Ig-like C2-type 2"
FT LIPID 220
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250|UniProtKB:P10252"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 154..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 129..169
FT /note="DPVPKPVIKIEKIEDMDDNCYLKLSCVIPGESVNYTWYGDK -> GESGEPK
FT SKSPLQWPQMDHCRASWEAWGTLGEEERKTSGQV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055598"
FT VAR_SEQ 170..243
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055599"
FT VARIANT 102
FT /note="E -> Q (in dbSNP:rs2295615)"
FT /id="VAR_020082"
FT VARIANT 241
FT /note="L -> S (in dbSNP:rs16832307)"
FT /id="VAR_049909"
FT CONFLICT 2
FT /note="C -> W (in Ref. 1; AAA62834)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="I -> N (in Ref. 3; CAA29647)"
FT /evidence="ECO:0000305"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2EDO"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2EDO"
FT STRAND 51..61
FT /evidence="ECO:0007829|PDB:2EDO"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:2EDO"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2EDO"
FT TURN 80..84
FT /evidence="ECO:0007829|PDB:2EDO"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:2EDO"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:2EDO"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2EDO"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:2EDO"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2EDO"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2EDO"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:2EDO"
SQ SEQUENCE 243 AA; 27683 MW; 9E46D76FC36A512C CRC64;
MCSRGWDSCL ALELLLLPLS LLVTSIQGHL VHMTVVSGSN VTLNISESLP ENYKQLTWFY
TFDQKIVEWD SRKSKYFESK FKGRVRLDPQ SGALYISKVQ KEDNSTYIMR VLKKTGNEQE
WKIKLQVLDP VPKPVIKIEK IEDMDDNCYL KLSCVIPGES VNYTWYGDKR PFPKELQNSV
LETTLMPHNY SRCYTCQVSN SVSSKNGTVC LSPPCTLARS FGVEWIASWL VVTVPTILGL
LLT
