LFA3_HUMAN
ID LFA3_HUMAN Reviewed; 250 AA.
AC P19256; A8K7G5; Q5U053; Q6IB65; Q96KI9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Lymphocyte function-associated antigen 3;
DE Short=Ag3;
DE AltName: Full=Surface glycoprotein LFA-3;
DE AltName: CD_antigen=CD58;
DE Flags: Precursor;
GN Name=CD58; Synonyms=LFA3;
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), PARTIAL PROTEIN SEQUENCE, AND
RP INTERACTION WITH CD2.
RC TISSUE=Erythrocyte;
RX PubMed=3309127; DOI=10.1084/jem.166.4.923;
RA Wallner B.P., Frey A.Z., Tizard R., Mattaliano R.J., Hession C.,
RA Sanders M.E., Dustin M.L., Springer T.A.;
RT "Primary structure of lymphocyte function-associated antigen 3 (LFA-3). The
RT ligand of the T lymphocyte CD2 glycoprotein.";
RL J. Exp. Med. 166:923-932(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=3313052; DOI=10.1038/329840a0;
RA Seed B.;
RT "An LFA-3 cDNA encodes a phospholipid-linked membrane protein homologous to
RT its receptor CD2.";
RL Nature 329:840-842(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=9510189;
RA Wallich R., Brenner C., Brand Y., Roux M., Reister M., Meuer S.;
RT "Gene structure, promoter characterization, and basis for alternative mRNA
RT splicing of the human CD58 gene.";
RL J. Immunol. 160:2862-2871(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17566972; DOI=10.1002/pmic.200700068;
RA Omaetxebarria M.J., Elortza F., Rodriguez-Suarez E., Aloria K.,
RA Arizmendi J.M., Jensen O.N., Matthiesen R.;
RT "Computational approach for identification and characterization of GPI-
RT anchored peptides in proteomics experiments.";
RL Proteomics 7:1951-1960(2007).
RN [11]
RP INTERACTION WITH CMTM6, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28813417; DOI=10.1038/nature23643;
RA Burr M.L., Sparbier C.E., Chan Y.C., Williamson J.C., Woods K.,
RA Beavis P.A., Lam E.Y.N., Henderson M.A., Bell C.C., Stolzenburg S.,
RA Gilan O., Bloor S., Noori T., Morgens D.W., Bassik M.C., Neeson P.J.,
RA Behren A., Darcy P.K., Dawson S.J., Voskoboinik I., Trapani J.A., Cebon J.,
RA Lehner P.J., Dawson M.A.;
RT "CMTM6 maintains the expression of PD-L1 and regulates anti-tumour
RT immunity.";
RL Nature 549:101-105(2017).
RN [12]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL148 (MICROBIAL INFECTION).
RX PubMed=29691324; DOI=10.1073/pnas.1720950115;
RA Wang E.C.Y., Pjechova M., Nightingale K., Vlahava V.M., Patel M.,
RA Ruckova E., Forbes S.K., Nobre L., Antrobus R., Roberts D., Fielding C.A.,
RA Seirafian S., Davies J., Murrell I., Lau B., Wilkie G.S., Suarez N.M.,
RA Stanton R.J., Vojtesek B., Davison A., Lehner P.J., Weekes M.P.,
RA Wilkinson G.W.G., Tomasec P.;
RT "Suppression of costimulation by human cytomegalovirus promotes evasion of
RT cellular immune defenses.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:4998-5003(2018).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 29-123 IN COMPLEX WITH CD2, AND
RP MUTAGENESIS OF PHE-29; VAL-37; VAL-49; VAL-86; THR-113 AND LEU-121.
RX PubMed=10380930; DOI=10.1016/s0092-8674(00)80790-4;
RA Wang J.H., Smolyar A., Tan K., Liu J.H., Kim M., Sun Z.Y., Wagner G.,
RA Reinherz E.L.;
RT "Structure of a heterophilic adhesion complex between the human CD2 and
RT CD58 (LFA-3) counterreceptors.";
RL Cell 97:791-803(1999).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 29-122.
RX PubMed=10200255; DOI=10.1073/pnas.96.8.4289;
RA Ikemizu S., Sparks L.M., van der Merwe P.A., Harlos K., Stuart D.I.,
RA Jones E.Y., Davis S.J.;
RT "Crystal structure of the CD2-binding domain of CD58 (lymphocyte function-
RT associated antigen 3) at 1.8-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4289-4294(1999).
CC -!- FUNCTION: Ligand of the T-lymphocyte CD2 glycoprotein. This interaction
CC is important in mediating thymocyte interactions with thymic epithelial
CC cells, antigen-independent and -dependent interactions of T-lymphocytes
CC with target cells and antigen-presenting cells and the T-lymphocyte
CC rosetting with erythrocytes. In addition, the LFA-3/CD2 interaction may
CC prime response by both the CD2+ and LFA-3+ cells.
CC -!- SUBUNIT: Interacts with CD2 (PubMed:10380930, PubMed:3309127).
CC Interacts with CMTM6 (PubMed:28813417). {ECO:0000269|PubMed:10380930,
CC ECO:0000269|PubMed:28813417, ECO:0000269|PubMed:3309127}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC protein UL148; this interaction retains immature CD58 intracellularly.
CC {ECO:0000269|PubMed:29691324}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=P19256-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P19256-2; Sequence=VSP_002522, VSP_002523;
CC Name=3;
CC IsoId=P19256-3; Sequence=VSP_038693;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000269|PubMed:14759258}.
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DR EMBL; Y00636; CAA68668.1; -; mRNA.
DR EMBL; X06296; CAA29622.1; -; mRNA.
DR EMBL; Y14780; CAA75083.1; -; Genomic_DNA.
DR EMBL; Y14781; CAA75083.1; JOINED; Genomic_DNA.
DR EMBL; Y14782; CAA75083.1; JOINED; Genomic_DNA.
DR EMBL; Y14783; CAA75083.1; JOINED; Genomic_DNA.
DR EMBL; Y14784; CAA75083.1; JOINED; Genomic_DNA.
DR EMBL; Y14780; CAA75084.1; -; Genomic_DNA.
DR EMBL; Y14781; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; Y14782; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; Y14783; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; Y14784; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; Y14785; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; AK291980; BAF84669.1; -; mRNA.
DR EMBL; CR456939; CAG33220.1; -; mRNA.
DR EMBL; BT019816; AAV38619.1; -; mRNA.
DR EMBL; BT019817; AAV38620.1; -; mRNA.
DR EMBL; AL390066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56652.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56653.1; -; Genomic_DNA.
DR CCDS; CCDS44199.1; -. [P19256-3]
DR CCDS; CCDS888.1; -. [P19256-1]
DR PIR; A28564; A28564.
DR RefSeq; NP_001138294.1; NM_001144822.1. [P19256-3]
DR RefSeq; NP_001770.1; NM_001779.2. [P19256-1]
DR PDB; 1CCZ; X-ray; 1.80 A; A=29-122.
DR PDB; 1CI5; NMR; -; A=29-123.
DR PDB; 1QA9; X-ray; 3.20 A; B/D=30-123.
DR PDBsum; 1CCZ; -.
DR PDBsum; 1CI5; -.
DR PDBsum; 1QA9; -.
DR AlphaFoldDB; P19256; -.
DR SMR; P19256; -.
DR BioGRID; 107403; 17.
DR IntAct; P19256; 12.
DR MINT; P19256; -.
DR STRING; 9606.ENSP00000358501; -.
DR ChEMBL; CHEMBL3790; -.
DR GlyConnect; 1474; 1 N-Linked glycan (1 site).
DR GlyGen; P19256; 6 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P19256; -.
DR PhosphoSitePlus; P19256; -.
DR SwissPalm; P19256; -.
DR BioMuta; CD58; -.
DR DMDM; 126225; -.
DR EPD; P19256; -.
DR jPOST; P19256; -.
DR MassIVE; P19256; -.
DR MaxQB; P19256; -.
DR PaxDb; P19256; -.
DR PeptideAtlas; P19256; -.
DR PRIDE; P19256; -.
DR ProteomicsDB; 53642; -. [P19256-1]
DR ProteomicsDB; 53643; -. [P19256-2]
DR ProteomicsDB; 53644; -. [P19256-3]
DR TopDownProteomics; P19256-1; -. [P19256-1]
DR TopDownProteomics; P19256-2; -. [P19256-2]
DR Antibodypedia; 20181; 926 antibodies from 43 providers.
DR DNASU; 965; -.
DR Ensembl; ENST00000369489.10; ENSP00000358501.5; ENSG00000116815.16. [P19256-1]
DR Ensembl; ENST00000457047.6; ENSP00000409080.2; ENSG00000116815.16. [P19256-3]
DR Ensembl; ENST00000464088.5; ENSP00000432773.1; ENSG00000116815.16. [P19256-2]
DR GeneID; 965; -.
DR KEGG; hsa:965; -.
DR MANE-Select; ENST00000369489.10; ENSP00000358501.5; NM_001779.3; NP_001770.1.
DR UCSC; uc001egm.4; human. [P19256-1]
DR CTD; 965; -.
DR DisGeNET; 965; -.
DR GeneCards; CD58; -.
DR HGNC; HGNC:1688; CD58.
DR HPA; ENSG00000116815; Low tissue specificity.
DR MIM; 153420; gene.
DR neXtProt; NX_P19256; -.
DR OpenTargets; ENSG00000116815; -.
DR PharmGKB; PA26227; -.
DR VEuPathDB; HostDB:ENSG00000116815; -.
DR eggNOG; ENOG502SB68; Eukaryota.
DR GeneTree; ENSGT00510000049596; -.
DR HOGENOM; CLU_1291581_0_0_1; -.
DR InParanoid; P19256; -.
DR OMA; DKVIEWE; -.
DR OrthoDB; 801938at2759; -.
DR PhylomeDB; P19256; -.
DR TreeFam; TF341787; -.
DR PathwayCommons; P19256; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P19256; -.
DR BioGRID-ORCS; 965; 17 hits in 1078 CRISPR screens.
DR ChiTaRS; CD58; human.
DR EvolutionaryTrace; P19256; -.
DR GenomeRNAi; 965; -.
DR Pharos; P19256; Tbio.
DR PRO; PR:P19256; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P19256; protein.
DR Bgee; ENSG00000116815; Expressed in jejunal mucosa and 194 other tissues.
DR ExpressionAtlas; P19256; baseline and differential.
DR Genevisible; P19256; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015714; Lymphocyte_func-assoc_Ag_3.
DR PANTHER; PTHR12080:SF91; PTHR12080:SF91; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT CHAIN 29..250
FT /note="Lymphocyte function-associated antigen 3"
FT /id="PRO_0000014814"
FT TOPO_DOM 29..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..121
FT /note="Ig-like"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..187
FT /evidence="ECO:0000250"
FT VAR_SEQ 236..237
FT /note="GI -> VL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3313052, ECO:0000303|Ref.5"
FT /id="VSP_002522"
FT VAR_SEQ 238..250
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3313052, ECO:0000303|Ref.5"
FT /id="VSP_002523"
FT VAR_SEQ 248..250
FT /note="NSN -> K (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038693"
FT VARIANT 15
FT /note="S -> G (in dbSNP:rs17426456)"
FT /id="VAR_049885"
FT MUTAGEN 29
FT /note="F->S: No effect on CD2-binding."
FT /evidence="ECO:0000269|PubMed:10380930"
FT MUTAGEN 37
FT /note="V->K: No effect on CD2-binding."
FT /evidence="ECO:0000269|PubMed:10380930"
FT MUTAGEN 49
FT /note="V->Q: No effect on CD2-binding."
FT /evidence="ECO:0000269|PubMed:10380930"
FT MUTAGEN 86
FT /note="V->K: No effect on CD2-binding."
FT /evidence="ECO:0000269|PubMed:10380930"
FT MUTAGEN 113
FT /note="T->S: No effect on CD2-binding."
FT /evidence="ECO:0000269|PubMed:10380930"
FT MUTAGEN 121
FT /note="L->G: No effect on CD2-binding."
FT /evidence="ECO:0000269|PubMed:10380930"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:1CCZ"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1CCZ"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1CCZ"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1CCZ"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1CCZ"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1CCZ"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1CCZ"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1CCZ"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1CCZ"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1CCZ"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1CCZ"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1CCZ"
SQ SEQUENCE 250 AA; 28147 MW; 34D635DF1D14FE2E CRC64;
MVAGSDAGRA LGVLSVVCLL HCFGFISCFS QQIYGVVYGN VTFHVPSNVP LKEVLWKKQK
DKVAELENSE FRAFSSFKNR VYLDTVSGSL TIYNLTSSDE DEYEMESPNI TDTMKFFLYV
LESLPSPTLT CALTNGSIEV QCMIPEHYNS HRGLIMYSWD CPMEQCKRNS TSIYFKMEND
LPQKIQCTLS NPLFNTTSSI ILTTCIPSSG HSRHRYALIP IPLAVITTCI VLYMNGILKC
DRKPDRTNSN
