P06126 (CD1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
T-cell surface glycoprotein CD1a

Alternative name(s):
T-cell surface antigen T6/Leu-6
Short name=hTa1 thymocyte antigen
CD_antigen=CD1a

Gene names

Name:

CD1A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells. Ref.10 Ref.11 Ref.12
Subunit structure	Heterodimer with B2M (beta-2-microglobulin). Interacts with CD74. Ref.12
Subcellular location	Cell membrane; Single-pass type I membrane protein. Endosome membrane. Note: Subject to intracellular trafficking between the cell membrane and endosomes. Localizes to cell surface lipid rafts. Ref.10 Ref.12 Ref.15
Tissue specificity	Expressed on cortical thymocytes, epidermal Langerhans cells, dendritic cells, on certain T-cell leukemias, and in various other tissues. Ref.10 Ref.12
Miscellaneous	During protein synthesis and maturation, CD1 family members bind endogenous lipids that are replaced by lipid or glycolipid antigens when the proteins are internalized and pass through endosomes, before trafficking back to the cell surface.
Sequence similarities	Contains 1 Ig-like (immunoglobulin-like) domain.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity
Cellular component	Cell membrane Endosome Membrane
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation Inferred from electronic annotation. Source: InterPro immune response Non-traceable author statement Ref.2. Source: UniProtKB
Cellular_component	MHC class I protein complex Inferred from electronic annotation. Source: InterPro endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
B2M	P61769	2	EBI-1036766,EBI-714718

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Chain

17 – 327

311

T-cell surface glycoprotein CD1a

PRO_0000014578

Regions

Topological domain

17 – 300

284

Extracellular Potential

Transmembrane

301 – 321

21

Helical; Potential

Topological domain

322 – 327

6

Cytoplasmic Potential

Domain

184 – 291

108

Ig-like

Region

90 – 94

5

Glycolipid binding

Sites

Binding site

171

1

Glycolipid

Amino acid modifications

Glycosylation

37

1

N-linked (GlcNAc...) Ref.13 Ref.14

Glycosylation

60

1

N-linked (GlcNAc...) Potential

Glycosylation

74

1

N-linked (GlcNAc...) Ref.13 Ref.14

Glycosylation

145

1

N-linked (GlcNAc...) Ref.13 Ref.14

Disulfide bond

119 ↔ 183

By similarity

Disulfide bond

223 ↔ 278

Ref.13 Ref.14

Natural variations

Natural variant

22

1

K → N.
Corresponds to variant rs3087217 [ dbSNP | Ensembl ].

VAR_062522

Natural variant

30

1

T → I. Ref.1 Ref.15
Corresponds to variant rs2269714 [ dbSNP | Ensembl ].

VAR_010209

Natural variant

68

1

C → W. Ref.1 Ref.15
Corresponds to variant rs2269715 [ dbSNP | Ensembl ].

VAR_010210

Experimental info

Sequence conflict

70 – 71

2

WS → V in AAA51933. Ref.7

Secondary structure

1

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327

Helix Strand Turn

Details...

Beta strand

25 – 37

13

Beta strand

40 – 49

10

Beta strand

52 – 58

7

Turn

59 – 62

4

Beta strand

63 – 68

6

Turn

69 – 74

6

Helix

77 – 105

29

Beta strand

109 – 122

14

Beta strand

125 – 135

11

Beta strand

138 – 144

7

Beta strand

147 – 150

4

Helix

152 – 154

3

Helix

156 – 165

10

Helix

169 – 180

12

Helix

182 – 193

12

Helix

195 – 198

4

Beta strand

205 – 211

7

Beta strand

218 – 231

14

Beta strand

234 – 239

6

Beta strand

260 – 269

10

Helix

270 – 272

3

Beta strand

276 – 281

6

Helix

283 – 285

3

Beta strand

290 – 293

4

Sequences

	Sequence		Length	Mass (Da)
	P06126 [UniParc]. Last modified February 9, 2010. Version 4. Checksum: C575C3C538F0AA29	FASTA	327	37,077
	10 20 30 40 50 60 MLFLLLPLLA VLPGDGNADG LKEPLSFHVT WIASFYNHSW KQNLVSGWLS DLQTHTWDSN 70 80 90 100 110 120 SSTIVFLCPW SRGNFSNEEW KELETLFRIR TIRSFEGIRR YAHELQFEYP FEIQVTGGCE 130 140 150 160 170 180 LHSGKVSGSF LQLAYQGSDF VSFQNNSWLP YPVAGNMAKH FCKVLNQNQH ENDITHNLLS 190 200 210 220 230 240 DTCPRFILGL LDAGKAHLQR QVKPEAWLSH GPSPGPGHLQ LVCHVSGFYP KPVWVMWMRG 250 260 270 280 290 300 EQEQQGTQRG DILPSADGTW YLRATLEVAA GEAADLSCRV KHSSLEGQDI VLYWEHHSSV 310 320 GFIILAVIVP LLLLIGLALW FRKRCFC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c demonstrates a hierarchy of exclusion in fibroblasts." Aruffo A., Seed B. J. Immunol. 143:1723-1730(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ILE-30 AND TRP-68.
[2]	"Structure and expression of the human thymocyte antigens CD1a, CD1b, and CD1c." Martin L.H., Calabi F., Lefebvre F.-A., Bilsland C.A.G., Milstein C. Proc. Natl. Acad. Sci. U.S.A. 84:9189-9193(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thymus.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Polymorphism of human CD1 genes." Han M., Hannick L.I., DiBrino M., Robinson M.A. Tissue Antigens 54:122-127(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-108.
[7]	"Molecular cloning of CD1a (T6), a human epidermal dendritic cell marker related to class I MHC molecules." Longley J., Kraus J., Alonso M., Edelson R. J. Invest. Dermatol. 92:628-631(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-327.
[8]	"A novel family of human major histocompatibility complex-related genes not mapping to chromosome 6." Calabi F., Milstein C. Nature 323:540-543(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 99-327. Tissue: T-cell.
[9]	"Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens." Martin L.H., Calabi F., Milstein C. Proc. Natl. Acad. Sci. U.S.A. 83:9154-9158(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-294.
[10]	"CD1a molecules traffic through the early recycling endosomal pathway in human Langerhans cells." Salamero J., Bausinger H., Mommaas A.M., Lipsker D., Proamer F., Cazenave J.-P., Goud B., de la Salle H., Hanau D. J. Invest. Dermatol. 116:401-408(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[11]	"CD1a-, b-, and c-restricted TCRs recognize both self and foreign antigens." Vincent M.S., Xiong X., Grant E.P., Peng W., Brenner M.B. J. Immunol. 175:6344-6351(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Regulation of CD1a surface expression and antigen presentation by invariant chain and lipid rafts." Sloma I., Zilber M.-T., Vasselon T., Setterblad N., Cavallari M., Mori L., De Libero G., Charron D., Mooney N., Gelin C. J. Immunol. 180:980-987(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CD47, TISSUE SPECIFICITY.
[13]	"Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A." Zajonc D.M., Elsliger M.-A., Teyton L., Wilson I.A. Nat. Immunol. 4:808-815(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 18-300 IN COMPLEX WITH B2M AND SULFATIDE SELF-ANTIGEN, MASS SPECTROMETRY, GLYCOSYLATION AT ASN-37; ASN-74 AND ASN-145, DISULFIDE BOND.
[14]	"Molecular mechanism of lipopeptide presentation by CD1a." Zajonc D.M., Crispin M.D., Bowden T.A., Young D.C., Cheng T.-Y., Hu J., Costello C.E., Rudd P.M., Dwek R.A., Miller M.J., Brenner M.B., Moody D.B., Wilson I.A. Immunity 22:209-219(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-294 IN COMPLEX WITH B2M AND LIPOPEPTIDE, GLYCOSYLATION AT ASN-37; ASN-74 AND ASN-145, DISULFIDE BOND.
[15]	"Structural characterization of two CD1A allelic variants." Oteo M., Arribas P., Setien F., Parra J.F., Mirones I., Gomez del Moral M., Martinez-Naves E. Hum. Immunol. 62:1137-1141(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ILE-30 AND TRP-68, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M28825 mRNA. Translation: AAA51931.1.
M22167 , M22080, M22163, M22164, M22165, M22166 Genomic DNA. Translation: AAA51932.1.
AK312945 mRNA. Translation: BAG35786.1.
AL121986 Genomic DNA. Translation: CAI10848.1.
CH471121 Genomic DNA. Translation: EAW52843.1.
CH471121 Genomic DNA. Translation: EAW52844.1.
AF142665 Genomic DNA. Translation: AAD37578.1.
M27735 mRNA. Translation: AAA51933.1.
X04450 mRNA. Translation: CAA28049.1.
M14663 Genomic DNA. Translation: AAA51934.1.

IPI

IPI00025382.

PIR

HLHUCD. A39957.

RefSeq

NP_001754.2. NM_001763.2.

UniGene

Hs.1309.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ONQ	X-ray	2.15	A/C	18-297	[»]
1XZ0	X-ray	2.80	A/C	18-294	[»]

ProteinModelPortal

P06126.

SMR

P06126. Positions 24-294.

ModBase

Search...

Protein-protein interaction databases

IntAct

P06126. 4 interactions.

MINT

MINT-4655994.

STRING

9606.ENSP00000289429.

Polymorphism databases

DMDM

288558852.

Proteomic databases

PaxDb

P06126.

PRIDE

P06126.

Protocols and materials databases

DNASU

909.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000289429; ENSP00000289429; ENSG00000158477.

GeneID

909.

KEGG

hsa:909.

UCSC

uc001frt.3. human.

Organism-specific databases

CTD

909.

GeneCards

GC01P158224.

H-InvDB

HIX0001190.

HGNC

HGNC:1634. CD1A.

HPA

CAB000009.
HPA010734.

MIM

188370. gene.

neXtProt

NX_P06126.

PharmGKB

PA26193.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG26626.

HOGENOM

HOG000111666.

HOVERGEN

HBG004453.

InParanoid

P06126.

KO

K06448.

OMA

NDITHNL.

OrthoDB

EOG40ZQZZ.

PhylomeDB

P06126.

Gene expression databases

Bgee

P06126.

CleanEx

HS_CD1A.

Genevestigator

P06126.

GermOnline

ENSG00000158477. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.
3.30.500.10. 1 hit.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003597. Ig_C1-set.
IPR011161. MHC_I-like_Ag-recog.
IPR011162. MHC_I/II-like_Ag-recog.
IPR001039. MHC_I_a_a1/a2.
[Graphical view]

Pfam

PF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
[Graphical view]

SMART

SM00407. IGc1. 1 hit.
[Graphical view]

SUPFAM

SSF54452. MHC_I/II-like_Ag-recog. 1 hit.

PROSITE

PS50835. IG_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00098. Antithymocyte globulin.

EvolutionaryTrace

P06126.

GenomeRNAi

909.

NextBio

3750.

SOURCE

Search...

Entry information

Entry name

CD1A_HUMAN

Accession

Primary (citable) accession number: P06126
Secondary accession number(s): D3DVD7 , Q13962, Q5TDJ8, Q9UMM4, Q9Y5M5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	February 9, 2010
Last modified:	May 29, 2013
This is version 133 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.