Q02223 (TNR17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tumor necrosis factor receptor superfamily member 17

Alternative name(s):
B-cell maturation protein
CD_antigen=CD269

Gene names

Name:	TNFRSF17
Synonyms:	BCM, BCMA

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	184 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for TNFSF13B/BLyS/BAFF and TNFSF13/APRIL. Promotes B-cell survival and plays a role in the regulation of humoral immunity. Activates NF-kappa-B and JNK. Ref.7 Ref.8 Ref.9
Subunit structure	Associates with TRAF1, TRAF2, TRAF3, TRAF5 and TRAF6.
Subcellular location	Cell membrane; Single-pass type III membrane protein. Endomembrane system; Single-pass type III membrane protein. Note: Perinuclear Golgi-like structures.
Tissue specificity	Expressed in mature B-cells, but not in T-cells or monocytes.
Involvement in disease	A chromosomal aberration involving TNFRSF17 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(4;16)(q26;p13) with IL2.
Sequence similarities	Contains 1 TNFR-Cys repeat.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity
Cellular component	Cell membrane Membrane
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Traceable author statement Ref.10. Source: ProtInc multicellular organismal development Traceable author statement Ref.2. Source: ProtInc signal transduction Traceable author statement Ref.10. Source: ProtInc
Cellular_component	endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Traceable author statement Ref.1. Source: ProtInc plasma membrane Traceable author statement Ref.10. Source: ProtInc
Molecular_function	receptor activity Traceable author statement Ref.10. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 184

184

Tumor necrosis factor receptor superfamily member 17

PRO_0000058935

Regions

Topological domain

1 – 54

54

Extracellular Potential

Transmembrane

55 – 77

23

Helical; Signal-anchor for type III membrane protein; Potential

Topological domain

78 – 184

107

Cytoplasmic Potential

Repeat

7 – 41

35

TNFR-Cys

Sites

Site

3 – 4

2

Breakpoint for translocation to form IL2/TNFRSF17 oncogene

Amino acid modifications

Disulfide bond

8 ↔ 21

Ref.11 Ref.12

Disulfide bond

24 ↔ 37

Ref.11 Ref.12

Disulfide bond

28 ↔ 41

Ref.11 Ref.12

Natural variations

Natural variant

54

1

A → V. Ref.4
Corresponds to variant rs11570146 [ dbSNP | Ensembl ].

VAR_018755

Natural variant

65

1

I → V. Ref.4
Corresponds to variant rs11570147 [ dbSNP | Ensembl ].

VAR_018756

Natural variant

75

1

F → V. Ref.4
Corresponds to variant rs11570148 [ dbSNP | Ensembl ].

VAR_018757

Natural variant

81

1

N → S. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5
Corresponds to variant rs373496 [ dbSNP | Ensembl ].

VAR_018758

Natural variant

153

1

A → T. Ref.3

VAR_012234

Natural variant

165

1

C → S. Ref.4
Corresponds to variant rs11570159 [ dbSNP | Ensembl ].

VAR_018759

Natural variant

176

1

E → D.
Corresponds to variant rs34546237 [ dbSNP | Ensembl ].

VAR_061855

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

184

Helix Strand Turn

Details...

Beta strand

12 – 15

4

Turn

16 – 19

4

Beta strand

20 – 23

4

Helix

24 – 26

3

Turn

27 – 29

3

Beta strand

30 – 32

3

Helix

35 – 37

3

Helix

38 – 42

5

Sequences

	Sequence		Length	Mass (Da)
	Q02223 [UniParc]. Last modified November 30, 2010. Version 2. Checksum: B6D87B3685F66022	FASTA	184	20,165
	10 20 30 40 50 60 MLQMAGQCSQ NEYFDSLLHA CIPCQLRCSS NTPPLTCQRY CNASVTNSVK GTNAILWTCL 70 80 90 100 110 120 GLSLIISLAV FVLMFLLRKI NSEPLKDEFK NTGSGLLGMA NIDLEKSRTG DEIILPRGLE 130 140 150 160 170 180 YTVEECTCED CIKSKPKVDS DHCFPLPAME EGATILVTTK TNDYCKSLPA ALSATEIEKS ISAR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new gene, BCM, on chromosome 16 is fused to the interleukin 2 gene by a t(4;16)(q26;p13) translocation in a malignant T cell lymphoma." Laabi Y., Gras M.P., Carbonnel F., Brouet J.C., Berger R., Larsen C.-J., Tsapis A. EMBO J. 11:3897-3904(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION, VARIANT SER-81. Tissue: Lymph node and Peripheral blood leukocyte.
[2]	"The BCMA gene, preferentially expressed during B lymphoid maturation, is bidirectionally transcribed." Laabi Y., Gras M.P., Brouet J.C., Berger R., Larsen C.J., Tsapis A. Nucleic Acids Res. 22:1147-1154(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT SER-81.
[3]	"Presence of four major haplotypes in human BCMA gene: lack of association with systemic lupus erythematosus and rheumatoid arthritis." Kawasaki A., Tsuchiya N., Fukazawa T., Hashimoto H., Tokunaga K. Genes Immun. 2:276-279(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-81 AND THR-153.
[4]	NIEHS SNPs program Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-54; VAL-65; VAL-75; SER-81 AND SER-165.
[5]	"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q." Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D. Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-81.
[6]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"TNF receptor family member BCMA (B cell maturation) associates with TNF receptor-associated factor (TRAF) 1, TRAF2, and TRAF3 and activates NF-kappa B, elk-1, c-Jun N-terminal kinase, and p38 mitogen-activated protein kinase." Hatzoglou A., Roussel J., Bourgeade M.-F., Rogier E., Madry C., Inoue J., Devergne O., Tsapis A. J. Immunol. 165:1322-1330(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TRAF1 AND TRAF3.
[8]	"TACI and BCMA are receptors for a TNF homologue implicated in B-cell autoimmune disease." Gross J.A., Johnston J., Mudri S., Enselman R., Dillon S.R., Madden K., Xu W., Parrish-Novak J., Foster D., Lofton-Day C., Moore M., Littau A., Grossman A., Haugen H., Foley K., Blumberg H., Harrison K., Kindsvogel W., Clegg C.H. Nature 404:995-999(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"APRIL and TALL-I and receptors BCMA and TACI: system for regulating humoral immunity." Yu G., Boone T., Delaney J., Hawkins N., Kelley M.J., Ramakrishnan M., McCabe S., Qiu W.R., Kornuc M., Xia X.-Z., Guo J., Stolina M., Boyle W.J., Sarosi I., Hsu H., Senaldi G., Theill L.E. Nat. Immunol. 1:252-256(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH APRIL AND BAFF.
[10]	"B cell maturation protein is a receptor for the tumor necrosis factor family member TALL-1." Shu H.-B., Johnson H. Proc. Natl. Acad. Sci. U.S.A. 97:9156-9161(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRAF5 AND TRAF6.
[11]	"Ligand-receptor binding revealed by the TNF family member TALL-1." Liu Y., Hong X., Kappler J., Jiang L., Zhang R., Xu L., Pan C.-H., Martin W.E., Murphy R.C., Shu H.-B., Dai S., Zhang G. Nature 423:49-56(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 8-46 IN COMPLEX WITH TNFSF13B, DISULFIDE BONDS.
[12]	"Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high affinity ligand binding." Hymowitz S.G., Patel D.R., Wallweber H.J., Runyon S., Yan M., Yin J., Shriver S.K., Gordon N.C., Pan B., Skelton N.J., Kelley R.F., Starovasnik M.A. J. Biol. Chem. 280:7218-7227(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 5-51 IN COMPLEX WITH MOUSE TNFSF13B, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z14954 mRNA. Translation: CAA78679.1.
Z29574 Genomic DNA. Translation: CAA82690.1.
Z29575 mRNA. Translation: CAA82691.1.
AB052772 Genomic DNA. Translation: BAB60895.1.
AY509112 Genomic DNA. Translation: AAR84240.1.
U95742 Genomic DNA. Translation: AAB67251.1.
AC007216 Genomic DNA. No translation available.

IPI

IPI00293877.

PIR

S43486.

RefSeq

NP_001183.2. NM_001192.2.

UniGene

Hs.2556.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OQD	X-ray	2.60	K/L/M/N/O/P/Q/R	8-46	[»]
1XU2	X-ray	2.35	R/S/T	5-51	[»]
2KN1	NMR	-	A	2-50	[»]

ProteinModelPortal

Q02223.

SMR

Q02223. Positions 8-46.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q02223. 4 interactions.

STRING

9606.ENSP00000053243.

PTM databases

PhosphoSite

Q02223.

Polymorphism databases

DMDM

399104.

Proteomic databases

PaxDb

Q02223.

PRIDE

Q02223.

Protocols and materials databases

DNASU

608.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000053243; ENSP00000053243; ENSG00000048462.

GeneID

608.

KEGG

hsa:608.

UCSC

uc002dbv.3. human.

Organism-specific databases

CTD

608.

GeneCards

GC16P012058.

HGNC

HGNC:11913. TNFRSF17.

HPA

HPA010569.

MIM

109545. gene.

neXtProt

NX_Q02223.

PharmGKB

PA36606.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG46220.

HOGENOM

HOG000129926.

HOVERGEN

HBG062796.

InParanoid

Q02223.

KO

K05153.

OMA

FPLPAME.

OrthoDB

EOG495ZT0.

PhylomeDB

Q02223.

Gene expression databases

ArrayExpress

Q02223.

Bgee

Q02223.

CleanEx

HS_TNFRSF17.

Genevestigator

Q02223.

GermOnline

ENSG00000048462. Homo sapiens.

Family and domain databases

InterPro

IPR015337. BCMA_Tall-1-bd.
IPR022320. TNFR_17.
[Graphical view]

Pfam

PF09257. BCMA-Tall_bind. 1 hit.
[Graphical view]

PIRSF

PIRSF011859. BCMA_Tall-1_bd. 1 hit.

PRINTS

PR01967. TNFACTORR17.

PROSITE

PS00652. TNFR_NGFR_1. False negative.
PS50050. TNFR_NGFR_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TNFRSF17. human.

EvolutionaryTrace

Q02223.

GenomeRNAi

608.

NextBio

2473.

SOURCE

Search...

Entry information

Entry name

TNR17_HUMAN

Accession

Primary (citable) accession number: Q02223

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	November 30, 2010
Last modified:	May 1, 2013
This is version 138 of the entry and version 2 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.