CD1E_HUMAN
ID CD1E_HUMAN Reviewed; 388 AA.
AC P15812; B4DZV3; E7EP01; Q5TDJ9; Q5TDK3; Q5TDK4; Q5TDK5; Q5TDK6; Q5TDK8;
AC Q5TDL1; Q712E4; Q712E5; Q712E6; Q712E7; Q712E8; Q712E9; Q712F0; Q712F1;
AC Q712F2; Q712F3; Q712F4; Q712F5; Q96TD0; Q96TD1; Q9UMM1; Q9Y5M3;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=T-cell surface glycoprotein CD1e, membrane-associated;
DE Short=hCD1e;
DE AltName: Full=R2G1;
DE AltName: CD_antigen=CD1e;
DE Contains:
DE RecName: Full=T-cell surface glycoprotein CD1e, soluble;
DE Short=sCD1e;
DE Flags: Precursor;
GN Name=CD1E;
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 [GENOMIC DNA].
RX PubMed=2467814; DOI=10.1002/eji.1830190211;
RA Calabi F., Jarvis J.M., Martin L., Milstein C.;
RT "Two classes of CD1 genes.";
RL Eur. J. Immunol. 19:285-292(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10; 11 AND
RP 12), VARIANT ARG-106, FUNCTION, INTERACTION WITH B2M, PROTEOLYTIC
RP PROCESSING, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=10948205; DOI=10.1074/jbc.m007082200;
RA Angenieux C., Salamero J., Fricker D., Cazenave J.-P., Goud B., Hanau D.,
RA de La Salle H.;
RT "Characterization of CD1e, a third type of CD1 molecule expressed in
RT dendritic cells.";
RL J. Biol. Chem. 275:37757-37764(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-386 (ISOFORM 13).
RC TISSUE=Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE CD1E*01).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES CD1E*01).
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-118, AND VARIANT ARG-106.
RX PubMed=10488738; DOI=10.1034/j.1399-0039.1999.540202.x;
RA Han M., Hannick L.I., DiBrino M., Robinson M.A.;
RT "Polymorphism of human CD1 genes.";
RL Tissue Antigens 54:122-127(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-208 (ALLELES CD1E*05 AND CD1E*06),
RP POLYMORPHISM, AND VARIANTS ARG-102; ARG-106; ASN-149 AND TRP-164.
RX PubMed=12144626; DOI=10.1034/j.1399-0039.2002.590509.x;
RA Tamouza R., Sghiri R., Ramasawmy R., Neonato M.G., Mombo L.E.,
RA Poirier J.C., Schaeffer V., Fortier C., Labie D., Girot R., Toubert A.,
RA Krishnamoorthy R., Charron D.;
RT "Two novel CD1 E alleles identified in black African individuals.";
RL Tissue Antigens 59:417-420(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-208 (ALLELES CD1E*03 AND CD1E*04),
RP POLYMORPHISM, AND VARIANTS TRP-164 AND PRO-194.
RX PubMed=11019917; DOI=10.1034/j.1399-0039.2000.560208.x;
RA Mirones I., Oteo M., Parra-Cuadrado J.F., Martinez-Naves E.;
RT "Identification of two novel human CD1E alleles.";
RL Tissue Antigens 56:159-161(2000).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 209-301.
RX PubMed=3097645; DOI=10.1073/pnas.83.23.9154;
RA Martin L.H., Calabi F., Milstein C.;
RT "Isolation of CD1 genes: a family of major histocompatibility complex-
RT related differentiation antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9154-9158(1986).
RN [10]
RP FUNCTION.
RX PubMed=16311334; DOI=10.1126/science.1115301;
RA de la Salle H., Mariotti S., Angenieux C., Gilleron M., Garcia-Alles L.-F.,
RA Malm D., Berg T., Paoletti S., Maitre B., Mourey L., Salamero J.,
RA Cazenave J.-P., Hanau D., Mori L., Puzo G., De Libero G.;
RT "Assistance of microbial glycolipid antigen processing by CD1e.";
RL Science 310:1321-1324(2005).
RN [11]
RP SUBCELLULAR LOCATION, UBIQUITINATION, AND PROTEOLYTIC PROCESSING.
RX PubMed=18208508; DOI=10.1111/j.1600-0854.2008.00707.x;
RA Maitre B., Angenieux C., Salamero J., Hanau D., Fricker D., Signorino F.,
RA Proamer F., Cazenave J.-P., Goud B., Tourne S., de la Salle H.;
RT "Control of the intracellular pathway of CD1e.";
RL Traffic 9:431-445(2008).
RN [12]
RP PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION.
RX PubMed=19196239; DOI=10.1042/bj20082204;
RA Maitre B., Angenieux C., Wurtz V., Layre E., Gilleron M., Collmann A.,
RA Mariotti S., Mori L., Fricker D., Cazenave J.P., van Dorsselaer A.,
RA Gachet C., de Libero G., Puzo G., Hanau D., de la Salle H.;
RT "The assembly of CD1e is controlled by an N-terminal propeptide which is
RT processed in endosomal compartments.";
RL Biochem. J. 419:661-668(2009).
RN [13]
RP POLYMORPHISM, AND VARIANT PRO-194.
RX PubMed=18325888; DOI=10.4049/jimmunol.180.6.3642;
RA Tourne S., Maitre B., Collmann A., Layre E., Mariotti S.,
RA Signorino-Gelo F., Loch C., Salamero J., Gilleron M., Angenieux C.,
RA Cazenave J.P., Mori L., Hanau D., Puzo G., De Libero G., de la Salle H.;
RT "A naturally occurring mutation in CD1e impairs lipid antigen
RT presentation.";
RL J. Immunol. 180:3642-3646(2008).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 32-303 IN COMPLEX WITH B2M,
RP FUNCTION, LIPID-BINDING, AND SUBUNIT.
RX PubMed=21788486; DOI=10.1073/pnas.1105627108;
RA Garcia-Alles L.F., Giacometti G., Versluis C., Maveyraud L., de Paepe D.,
RA Guiard J., Tranier S., Gilleron M., Prandi J., Hanau D., Heck A.J.,
RA Mori L., De Libero G., Puzo G., Mourey L., de la Salle H.;
RT "Crystal structure of human CD1e reveals a groove suited for lipid-exchange
RT processes.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13230-13235(2011).
CC -!- FUNCTION: T-cell surface glycoprotein CD1e, soluble binds diacetylated
CC lipids, including phosphatidyl inositides and diacylated
CC sulfoglycolipids, and is required for the presentation of glycolipid
CC antigens on the cell surface. The membrane-associated form is not
CC active. {ECO:0000269|PubMed:10948205, ECO:0000269|PubMed:16311334,
CC ECO:0000269|PubMed:21788486}.
CC -!- SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). The association
CC with B2M appears to be facilitated by the presence of the propeptide.
CC {ECO:0000269|PubMed:21788486}.
CC -!- SUBCELLULAR LOCATION: [T-cell surface glycoprotein CD1e, membrane-
CC associated]: Golgi apparatus membrane; Single-pass type I membrane
CC protein. Early endosome. Late endosome. Note=Predominantly localized in
CC the trans-Golgi network in immature dendritic cells, and as a cleaved,
CC soluble protein in the lysosome lumen of mature dendritic cells.
CC -!- SUBCELLULAR LOCATION: [T-cell surface glycoprotein CD1e, soluble]:
CC Lysosome lumen.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=13;
CC Name=1;
CC IsoId=P15812-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15812-2; Sequence=VSP_037713;
CC Name=3;
CC IsoId=P15812-3; Sequence=VSP_037711, VSP_037712;
CC Name=4;
CC IsoId=P15812-4; Sequence=VSP_037710, VSP_037713;
CC Name=5;
CC IsoId=P15812-5; Sequence=VSP_037709;
CC Name=6;
CC IsoId=P15812-6; Sequence=VSP_037709, VSP_037713;
CC Name=7;
CC IsoId=P15812-7; Sequence=VSP_037709, VSP_037710, VSP_037713;
CC Name=8;
CC IsoId=P15812-8; Sequence=VSP_037708;
CC Name=9;
CC IsoId=P15812-9; Sequence=VSP_037708, VSP_037713;
CC Name=10;
CC IsoId=P15812-10; Sequence=VSP_037708, VSP_037711, VSP_037712;
CC Name=11;
CC IsoId=P15812-11; Sequence=VSP_037708, VSP_037710;
CC Name=12;
CC IsoId=P15812-12; Sequence=VSP_037708, VSP_037710, VSP_037713;
CC Name=13;
CC IsoId=P15812-13; Sequence=VSP_046961;
CC -!- TISSUE SPECIFICITY: Expressed on cortical thymocytes, dendritic cells,
CC Langerhans cells, on certain T-cell leukemias, and in various other
CC tissues. {ECO:0000269|PubMed:10948205}.
CC -!- PTM: Mono-ubiquitinated. {ECO:0000269|PubMed:18208508}.
CC -!- PTM: Proteolytically cleaved in late endosomes to yield a soluble form.
CC {ECO:0000269|PubMed:10948205, ECO:0000269|PubMed:18208508,
CC ECO:0000269|PubMed:19196239}.
CC -!- POLYMORPHISM: Six alleles of CD1E are known. CD1E*01 has His-102/Gln-
CC 106/Ser-149/Arg-164/Leu-194, CD1E*02 has His-102/Arg-106/Ser-149/Arg-
CC 164/Leu-194, CD1E*03 (9L) has His-102/Gln-106/Ser-149/Trp-164/Leu-194,
CC CD1E*04 (15L) has His-102/Gln-106/Ser-149/Arg-164/Pro-194, CD1E*05 has
CC Arg-102/Arg-106/Ser-149/Arg-164/Leu-194 and CD1E*06 has His-102/Arg-
CC 106/Asn-149/Arg-164/Leu-194 (PubMed:12144626, PubMed:11019917,
CC PubMed:18325888). The sequence shown is that of allele CD1E*01.
CC {ECO:0000269|PubMed:11019917, ECO:0000269|PubMed:12144626,
CC ECO:0000269|PubMed:18325888}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA33100.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X14975; CAA33100.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ289111; CAB93150.1; -; mRNA.
DR EMBL; AJ289112; CAB93151.1; -; mRNA.
DR EMBL; AJ289113; CAB93152.1; -; mRNA.
DR EMBL; AJ289114; CAB93153.1; -; mRNA.
DR EMBL; AJ289115; CAB93154.1; -; mRNA.
DR EMBL; AJ289116; CAB93155.1; -; mRNA.
DR EMBL; AJ289117; CAB93156.1; -; mRNA.
DR EMBL; AJ289118; CAB93157.1; -; mRNA.
DR EMBL; AJ289119; CAB93158.1; -; mRNA.
DR EMBL; AJ289120; CAB93159.1; -; mRNA.
DR EMBL; AJ289121; CAB93160.1; -; mRNA.
DR EMBL; AJ289122; CAB93161.1; -; mRNA.
DR EMBL; AK303108; BAG64215.1; -; mRNA.
DR EMBL; AK311643; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL121986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52828.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52830.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52831.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52832.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52833.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52834.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52835.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52837.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52838.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52839.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52840.1; -; Genomic_DNA.
DR EMBL; AF142669; AAD37582.1; -; Genomic_DNA.
DR EMBL; AH010757; AAK52913.1; -; Genomic_DNA.
DR EMBL; AH010758; AAK52914.1; -; Genomic_DNA.
DR EMBL; AJ251334; CAB82829.1; -; Genomic_DNA.
DR EMBL; AJ251335; CAC07175.1; -; Genomic_DNA.
DR EMBL; M14666; AAA51937.1; -; Genomic_DNA.
DR CCDS; CCDS41417.1; -. [P15812-1]
DR CCDS; CCDS41418.1; -. [P15812-2]
DR CCDS; CCDS41419.1; -. [P15812-4]
DR CCDS; CCDS41420.1; -. [P15812-9]
DR CCDS; CCDS41421.1; -. [P15812-3]
DR CCDS; CCDS41422.1; -. [P15812-10]
DR CCDS; CCDS53384.1; -. [P15812-7]
DR CCDS; CCDS53385.1; -. [P15812-5]
DR CCDS; CCDS53386.1; -. [P15812-6]
DR CCDS; CCDS53387.1; -. [P15812-13]
DR CCDS; CCDS53388.1; -. [P15812-11]
DR CCDS; CCDS53389.1; -. [P15812-12]
DR CCDS; CCDS53390.1; -. [P15812-8]
DR PIR; S07716; HLHUR2.
DR RefSeq; NP_001036048.1; NM_001042583.2. [P15812-2]
DR RefSeq; NP_001036049.1; NM_001042584.2. [P15812-3]
DR RefSeq; NP_001036050.1; NM_001042585.2. [P15812-4]
DR RefSeq; NP_001036051.1; NM_001042586.2. [P15812-9]
DR RefSeq; NP_001036052.1; NM_001042587.2. [P15812-10]
DR RefSeq; NP_001172036.1; NM_001185107.1. [P15812-5]
DR RefSeq; NP_001172037.1; NM_001185108.1. [P15812-7]
DR RefSeq; NP_001172039.1; NM_001185110.1. [P15812-12]
DR RefSeq; NP_001172041.1; NM_001185112.1. [P15812-8]
DR RefSeq; NP_001172042.1; NM_001185113.1. [P15812-11]
DR RefSeq; NP_001172043.1; NM_001185114.1. [P15812-13]
DR RefSeq; NP_001172044.1; NM_001185115.1. [P15812-6]
DR RefSeq; NP_112155.2; NM_030893.3. [P15812-1]
DR RefSeq; XP_011508436.1; XM_011510134.2. [P15812-3]
DR PDB; 3S6C; X-ray; 2.90 A; A=32-303.
DR PDBsum; 3S6C; -.
DR AlphaFoldDB; P15812; -.
DR SMR; P15812; -.
DR BioGRID; 107351; 45.
DR IntAct; P15812; 27.
DR STRING; 9606.ENSP00000357149; -.
DR GlyGen; P15812; 2 sites.
DR iPTMnet; P15812; -.
DR PhosphoSitePlus; P15812; -.
DR BioMuta; CD1E; -.
DR DMDM; 254763260; -.
DR MassIVE; P15812; -.
DR MaxQB; P15812; -.
DR PaxDb; P15812; -.
DR PeptideAtlas; P15812; -.
DR PRIDE; P15812; -.
DR ProteomicsDB; 17260; -.
DR ProteomicsDB; 53210; -. [P15812-1]
DR ProteomicsDB; 53212; -. [P15812-11]
DR ProteomicsDB; 53213; -. [P15812-12]
DR ProteomicsDB; 53214; -. [P15812-2]
DR ProteomicsDB; 53215; -. [P15812-3]
DR ProteomicsDB; 53216; -. [P15812-4]
DR ProteomicsDB; 53217; -. [P15812-5]
DR ProteomicsDB; 53218; -. [P15812-6]
DR ProteomicsDB; 53219; -. [P15812-7]
DR ProteomicsDB; 53220; -. [P15812-8]
DR ProteomicsDB; 53221; -. [P15812-9]
DR Antibodypedia; 55004; 255 antibodies from 25 providers.
DR DNASU; 913; -.
DR Ensembl; ENST00000368154.5; ENSP00000357136.1; ENSG00000158488.16. [P15812-11]
DR Ensembl; ENST00000368155.7; ENSP00000357137.3; ENSG00000158488.16. [P15812-7]
DR Ensembl; ENST00000368156.5; ENSP00000357138.1; ENSG00000158488.16. [P15812-6]
DR Ensembl; ENST00000368157.5; ENSP00000357139.1; ENSG00000158488.16. [P15812-12]
DR Ensembl; ENST00000368160.7; ENSP00000357142.3; ENSG00000158488.16. [P15812-2]
DR Ensembl; ENST00000368161.7; ENSP00000357143.3; ENSG00000158488.16. [P15812-3]
DR Ensembl; ENST00000368163.7; ENSP00000357145.3; ENSG00000158488.16. [P15812-4]
DR Ensembl; ENST00000368164.7; ENSP00000357146.3; ENSG00000158488.16. [P15812-10]
DR Ensembl; ENST00000368165.7; ENSP00000357147.3; ENSG00000158488.16. [P15812-5]
DR Ensembl; ENST00000368166.7; ENSP00000357148.3; ENSG00000158488.16. [P15812-9]
DR Ensembl; ENST00000368167.8; ENSP00000357149.3; ENSG00000158488.16. [P15812-1]
DR Ensembl; ENST00000444681.6; ENSP00000402906.2; ENSG00000158488.16. [P15812-13]
DR Ensembl; ENST00000452291.6; ENSP00000416228.2; ENSG00000158488.16. [P15812-8]
DR GeneID; 913; -.
DR KEGG; hsa:913; -.
DR MANE-Select; ENST00000368167.8; ENSP00000357149.3; NM_030893.4; NP_112155.2.
DR UCSC; uc001fry.4; human. [P15812-1]
DR CTD; 913; -.
DR DisGeNET; 913; -.
DR GeneCards; CD1E; -.
DR HGNC; HGNC:1638; CD1E.
DR HPA; ENSG00000158488; Tissue enriched (lymphoid).
DR MIM; 188411; gene.
DR neXtProt; NX_P15812; -.
DR OpenTargets; ENSG00000158488; -.
DR PharmGKB; PA26197; -.
DR VEuPathDB; HostDB:ENSG00000158488; -.
DR eggNOG; ENOG502SJH6; Eukaryota.
DR GeneTree; ENSGT01040000240396; -.
DR HOGENOM; CLU_047501_9_2_1; -.
DR InParanoid; P15812; -.
DR OMA; QVKPEVW; -.
DR PhylomeDB; P15812; -.
DR TreeFam; TF336723; -.
DR PathwayCommons; P15812; -.
DR SignaLink; P15812; -.
DR BioGRID-ORCS; 913; 9 hits in 1065 CRISPR screens.
DR GeneWiki; CD1E; -.
DR GenomeRNAi; 913; -.
DR Pharos; P15812; Tbio.
DR PRO; PR:P15812; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P15812; protein.
DR Bgee; ENSG00000158488; Expressed in thymus and 105 other tissues.
DR ExpressionAtlas; P15812; baseline and differential.
DR Genevisible; P15812; HS.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0030883; F:endogenous lipid antigen binding; IBA:GO_Central.
DR GO; GO:0030884; F:exogenous lipid antigen binding; IBA:GO_Central.
DR GO; GO:0071723; F:lipopeptide binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0048006; P:antigen processing and presentation, endogenous lipid antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011161; MHC_I-like_Ag-recog.
DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF16497; MHC_I_3; 1.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Disulfide bond;
KW Endosome; Glycoprotein; Golgi apparatus; Immunity; Immunoglobulin domain;
KW Lipid-binding; Lysosome; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..388
FT /note="T-cell surface glycoprotein CD1e, membrane-
FT associated"
FT /id="PRO_0000014582"
FT PROPEP 20..31
FT /note="Removed in sCD1e"
FT /id="PRO_0000379780"
FT CHAIN 32..388
FT /note="T-cell surface glycoprotein CD1e, soluble"
FT /id="PRO_0000379781"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 191..301
FT /note="Ig-like"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 230..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 20..208
FT /note="Missing (in isoform 8, isoform 9, isoform 10,
FT isoform 11 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:10948205"
FT /id="VSP_037708"
FT VAR_SEQ 20..119
FT /note="APQALQSYHLAAEEQLSFRMLQTSSFANHSWAHSEGSGWLGDLQTHGWDTVL
FT GTIRFLKPWSHGNFSKQELKNLQSLFQLYFHSFIQIVQASAGQFQLEY -> D (in
FT isoform 13)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046961"
FT VAR_SEQ 119..209
FT /note="YPFEIQILAGCRMNAPQIFLNMAYQGSDFLSFQGISWEPSPGAGIRAQNICK
FT VLNRYLDIKEILQSLLGHTCPRFLAGLMEAGESELKRKV -> L (in isoform 5,
FT isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10948205"
FT /id="VSP_037709"
FT VAR_SEQ 248..302
FT /note="Missing (in isoform 4, isoform 7, isoform 11 and
FT isoform 12)"
FT /evidence="ECO:0000303|PubMed:10948205"
FT /id="VSP_037710"
FT VAR_SEQ 268..290
FT /note="YLRATLDVAAGEAAGLSCRVKHS -> WIFHLSHPDLFDCDSYPGHIGCS
FT (in isoform 3 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:10948205"
FT /id="VSP_037711"
FT VAR_SEQ 291..388
FT /note="Missing (in isoform 3 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:10948205"
FT /id="VSP_037712"
FT VAR_SEQ 334..345
FT /note="Missing (in isoform 2, isoform 4, isoform 6, isoform
FT 7, isoform 9 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:10948205"
FT /id="VSP_037713"
FT VARIANT 15
FT /note="G -> E (in dbSNP:rs3180089)"
FT /id="VAR_056035"
FT VARIANT 102
FT /note="H -> R (in allele CD1E*05; dbSNP:rs2873587)"
FT /evidence="ECO:0000269|PubMed:12144626"
FT /id="VAR_058324"
FT VARIANT 106
FT /note="Q -> R (in allele CD1E*02, allele CD1E*05 and
FT CD1E*06; dbSNP:rs1065457)"
FT /evidence="ECO:0000269|PubMed:10488738,
FT ECO:0000269|PubMed:10948205, ECO:0000269|PubMed:12144626"
FT /id="VAR_010191"
FT VARIANT 149
FT /note="S -> N (in allele CD1E*05; dbSNP:rs35116276)"
FT /evidence="ECO:0000269|PubMed:12144626"
FT /id="VAR_058325"
FT VARIANT 164
FT /note="R -> W (in allele CD1E*03; dbSNP:rs199655202)"
FT /evidence="ECO:0000269|PubMed:11019917,
FT ECO:0000269|PubMed:12144626"
FT /id="VAR_010192"
FT VARIANT 194
FT /note="L -> P (in allele CD1E*04; impairs localization to
FT late endosomal compartments and lipid antigen presentation;
FT dbSNP:rs200741122)"
FT /evidence="ECO:0000269|PubMed:11019917,
FT ECO:0000269|PubMed:18325888"
FT /id="VAR_010193"
FT CONFLICT 209
FT /note="V -> A (in Ref. 3; BAG64215)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="E -> G (in Ref. 3; BAG64215)"
FT /evidence="ECO:0000305"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3S6C"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3S6C"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:3S6C"
FT HELIX 87..111
FT /evidence="ECO:0007829|PDB:3S6C"
FT TURN 112..116
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 119..129
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:3S6C"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:3S6C"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:3S6C"
FT HELIX 176..201
FT /evidence="ECO:0007829|PDB:3S6C"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3S6C"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:3S6C"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:3S6C"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:3S6C"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:3S6C"
SQ SEQUENCE 388 AA; 43626 MW; F6503AE9608C6568 CRC64;
MLLLFLLFEG LCCPGENTAA PQALQSYHLA AEEQLSFRML QTSSFANHSW AHSEGSGWLG
DLQTHGWDTV LGTIRFLKPW SHGNFSKQEL KNLQSLFQLY FHSFIQIVQA SAGQFQLEYP
FEIQILAGCR MNAPQIFLNM AYQGSDFLSF QGISWEPSPG AGIRAQNICK VLNRYLDIKE
ILQSLLGHTC PRFLAGLMEA GESELKRKVK PEAWLSCGPS PGPGRLQLVC HVSGFYPKPV
WVMWMRGEQE QRGTQRGDVL PNADETWYLR ATLDVAAGEA AGLSCRVKHS SLGGHDLIIH
WGGYSIFLIL ICLTVIVTLV ILVVVDSRLK KQSSNKNILS PHTPSPVFLM GANTQDTKNS
RHQFCLAQVS WIKNRVLKKW KTRLNQLW
