P29016 (CD1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
T-cell surface glycoprotein CD1b

Alternative name(s):
CD_antigen=CD1b

Gene names

Name:

CD1B

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	333 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.6 Ref.8
Subunit structure	Heterodimer with B2M (beta-2-microglobulin). Interacts with saposin C. Ref.8
Subcellular location	Cell membrane; Single-pass type I membrane protein. Endosome membrane. Lysosome membrane. Note: Subject to intracellular trafficking between the cell membrane, endosomes and lysosomes. Localizes to cell surface lipid rafts. Ref.6 Ref.7 Ref.8
Tissue specificity	Expressed on cortical thymocytes, on certain T-cell leukemias, and in various other tissues.
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 or lysosomes, before trafficking back to the cell surface. Interaction with saposin C is required for the loading of bacterial lipid antigens onto CD1B in the lysosome.
Sequence similarities	Contains 1 Ig-like (immunoglobulin-like) domain.
Sequence caution	The sequence CAI10852.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity
Cellular component	Cell membrane Endosome Lysosome Membrane
Coding sequence diversity	Alternative splicing
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 Inferred from electronic annotation. Source: InterPro
Cellular_component	endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Traceable author statement PubMed 1702817. Source: ProtInc lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Traceable author statement Ref.1Ref.2. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
B2M	P61769	3	EBI-1033762,EBI-714718

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P29016-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P29016-2)

The sequence of this isoform differs from the canonical sequence as follows:
     242-296: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Potential

Chain

18 – 333

316

T-cell surface glycoprotein CD1b

PRO_0000014579

Regions

Topological domain

18 – 303

286

Extracellular Potential

Transmembrane

304 – 324

21

Helical; Potential

Topological domain

325 – 333

9

Cytoplasmic Potential

Domain

185 – 295

111

Ig-like

Motif

329 – 332

4

Internalization signal

Amino acid modifications

Glycosylation

38

1

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

Glycosylation

75

1

N-linked (GlcNAc...) Ref.10 Ref.13

Glycosylation

146

1

N-linked (GlcNAc...) Potential

Glycosylation

258

1

N-linked (GlcNAc...) Potential

Disulfide bond

120 ↔ 184

Ref.11 Ref.12 Ref.13

Disulfide bond

149 ↔ 163

Ref.11 Ref.12 Ref.13

Disulfide bond

224 ↔ 279

Ref.11 Ref.12 Ref.13

Natural variations

Alternative sequence

242 – 296

55

Missing in isoform 2.

VSP_016911

Experimental info

Mutagenesis

329 – 330

2

YQ → AA: Strongly reduced internalization and trafficking to endosomes. Ref.6

Secondary structure

1

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333

Helix Strand Turn

Details...

Beta strand

27 – 38

12

Beta strand

41 – 50

10

Beta strand

53 – 59

7

Turn

60 – 63

4

Beta strand

64 – 67

4

Turn

70 – 75

6

Helix

78 – 102

25

Turn

103 – 107

5

Beta strand

110 – 122

13

Beta strand

128 – 136

9

Beta strand

139 – 145

7

Beta strand

148 – 151

4

Helix

153 – 155

3

Helix

156 – 166

11

Helix

170 – 181

12

Helix

183 – 194

12

Helix

196 – 199

4

Beta strand

206 – 213

8

Beta strand

219 – 232

14

Beta strand

234 – 240

7

Beta strand

254 – 256

3

Turn

257 – 259

3

Beta strand

261 – 270

10

Helix

271 – 273

3

Beta strand

277 – 283

7

Helix

284 – 286

3

Beta strand

291 – 296

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 7D02B670D4DE8CC7	FASTA	333	36,939
	10 20 30 40 50 60 MLLLPFQLLA VLFPGGNSEH AFQGPTSFHV IQTSSFTNST WAQTQGSGWL DDLQIHGWDS 70 80 90 100 110 120 DSGTAIFLKP WSKGNFSDKE VAELEEIFRV YIFGFAREVQ DFAGDFQMKY PFEIQGIAGC 130 140 150 160 170 180 ELHSGGAIVS FLRGALGGLD FLSVKNASCV PSPEGGSRAQ KFCALIIQYQ GIMETVRILL 190 200 210 220 230 240 YETCPRYLLG VLNAGKADLQ RQVKPEAWLS SGPSPGPGRL QLVCHVSGFY PKPVWVMWMR 250 260 270 280 290 300 GEQEQQGTQL GDILPNANWT WYLRATLDVA DGEAAGLSCR VKHSSLEGQD IILYWRNPTS 310 320 330 IGSIVLAIIV PSLLLLLCLA LWYMRRRSYQ NIP
	Isoform 2 [UniParc]. Checksum: 087FD5FF65921339	FASTA	278	30,740
	10 20 30 40 50 60 MLLLPFQLLA VLFPGGNSEH AFQGPTSFHV IQTSSFTNST WAQTQGSGWL DDLQIHGWDS 70 80 90 100 110 120 DSGTAIFLKP WSKGNFSDKE VAELEEIFRV YIFGFAREVQ DFAGDFQMKY PFEIQGIAGC 130 140 150 160 170 180 ELHSGGAIVS FLRGALGGLD FLSVKNASCV PSPEGGSRAQ KFCALIIQYQ GIMETVRILL 190 200 210 220 230 240 YETCPRYLLG VLNAGKADLQ RQVKPEAWLS SGPSPGPGRL QLVCHVSGFY PKPVWVMWMR 250 260 270 GNPTSIGSIV LAIIVPSLLL LLCLALWYMR RRSYQNIP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"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] (ISOFORM 1).
[3]	"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].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[5]	"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 203-295.
[6]	"The alphabeta T cell response to self-glycolipids shows a novel mechanism of CD1b loading and a requirement for complex oligosaccharides." Shamshiev A., Donda A., Prigozy T.I., Mori L., Chigorno V., Benedict C.A., Kappos L., Sonnino S., Kronenberg M., De Libero G. Immunity 13:255-264(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 329-TYR-GLN-330, SUBCELLULAR LOCATION.
[7]	"Human CD1b and CD1c isoforms survey different intracellular compartments for the presentation of microbial lipid antigens." Briken V., Jackman R.M., Watts G.F.M., Rogers R.A., Porcelli S.A. J. Exp. Med. 192:281-288(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"Saposin C is required for lipid presentation by human CD1b." Winau F., Schwierzeck V., Hurwitz R., Remmel N., Sieling P.A., Modlin R.L., Porcelli S.A., Brinkmann V., Sugita M., Sandhoff K., Kaufmann S.H.E., Schaible U.E. Nat. Immunol. 5:169-174(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SAPOSIN C, SUBCELLULAR LOCATION.
[9]	Erratum Winau F., Schwierzeck V., Hurwitz R., Remmel N., Sieling P.A., Modlin R.L., Porcelli S.A., Brinkmann V., Sugita M., Sandhoff K., Kaufmann S.H.E., Schaible U.E. Nat. Immunol. 5:344-344(2004)
[10]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-75, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Structure of human CD1b with bound ligands at 2.3 A, a maze for alkyl chains." Gadola S.D., Zaccai N.R., Harlos K., Shepherd D., Castro-Palomino J.C., Ritter G., Schmidt R.R., Jones E.Y., Cerundolo V. Nat. Immunol. 3:721-726(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 18-295 IN COMPLEXES WITH B2M; GANGLIOSIDE GM2 AND PHOSPHATIDYLINOSITOL, DISULFIDE BONDS.
[12]	"The crystal structure of human CD1b with a bound bacterial glycolipid." Batuwangala T., Shepherd D., Gadola S.D., Gibson K.J.C., Zaccai N.R., Fersht A.R., Besra G.S., Cerundolo V., Jones E.Y. J. Immunol. 172:2382-2388(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 18-295 IN COMPLEX WITH B2M AND GLUCOSE MONOMYCOLATE, DISULFIDE BONDS.
[13]	"Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid-binding groove of CD1b." Garcia-Alles L.F., Versluis K., Maveyraud L., Vallina A.T., Sansano S., Bello N.F., Gober H.-J., Guillet V., de la Salle H., Puzo G., Mori L., Heck A.J.R., De Libero G., Mourey L. EMBO J. 25:3684-3692(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-298 IN COMPLEX WITH B2M; PHOSPHATIDYLCHOLINE AND SPACER LIGAND, GLYCOSYLATION AT ASN-38 AND ASN-75, MASS SPECTROMETRY, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M22173 , M22168, M22169, M22170, M22171, M22172 Genomic DNA. Translation: AAA51940.1.
M28826 mRNA. Translation: AAA51939.1.
AL121986 Genomic DNA. Translation: CAI10852.1. Sequence problems.
AL121986 Genomic DNA. Translation: CAI10853.1.
BC069481 mRNA. Translation: AAH69481.1.
BC074747 mRNA. Translation: AAH74747.1.
BC104216 mRNA. Translation: AAI04217.1.
BC104217 mRNA. Translation: AAI04218.1.
M14665 Genomic DNA. Translation: AAA51936.1.

IPI

IPI00019849.
IPI00513798.

PIR

HLHUCB. B39957.

RefSeq

NP_001755.1. NM_001764.2.

UniGene

Hs.1310.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GZP	X-ray	2.80	A	18-295	[»]
1GZQ	X-ray	2.26	A	18-295	[»]
1UQS	X-ray	3.10	A	18-295	[»]
2H26	X-ray	1.80	A	19-298	[»]
3OV6	X-ray	2.50	A	27-295	[»]
3T8X	X-ray	1.90	A/C	19-298	[»]

ProteinModelPortal

P29016.

ModBase

Search...

Protein-protein interaction databases

IntAct

P29016. 1 interaction.

MINT

MINT-242013.

STRING

9606.ENSP00000357150.

PTM databases

PhosphoSite

P29016.

Polymorphism databases

DMDM

115962.

Proteomic databases

PaxDb

P29016.

PRIDE

P29016.

Protocols and materials databases

DNASU

910.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368168; ENSP00000357150; ENSG00000158485.

GeneID

910.

KEGG

hsa:910.

UCSC

uc001frw.3. human.
uc001frx.3. human.

Organism-specific databases

CTD

910.

GeneCards

GC01M158297.

HGNC

HGNC:1635. CD1B.

HPA

HPA021824.

MIM

188360. gene.

neXtProt

NX_P29016.

PharmGKB

PA26194.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG79438.

HOGENOM

HOG000111666.

HOVERGEN

HBG004453.

InParanoid

P29016.

KO

K06448.

OMA

WAQTQGS.

OrthoDB

EOG40ZQZZ.

PhylomeDB

P29016.

Gene expression databases

ArrayExpress

P29016.

Bgee

P29016.

CleanEx

HS_CD1B.

Genevestigator

P29016.

GermOnline

ENSG00000158485. 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.
[Graphical view]

Pfam

PF07654. C1-set. 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

EvolutionaryTrace

P29016.

GenomeRNAi

910.

NextBio

3754.

SOURCE

Search...

Entry information

Entry name

CD1B_HUMAN

Accession

Primary (citable) accession number: P29016
Secondary accession number(s): Q5TDK9, Q5TDL0, Q9UMM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	May 1, 2013
This is version 127 of the entry and version 1 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.