Q99467 (CD180_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CD180 antigen

Alternative name(s):
Lymphocyte antigen 64
Radioprotective 105 kDa protein
CD_antigen=CD180

Gene names

Name:	CD180
Synonyms:	LY64, RP105

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	661 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	May cooperate with MD-1 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) in B-cells. Leads to NF-kappa-B activation. Also involved in the life/death decision of B-cells By similarity.
Subunit structure	M-shaped tetramer of two CD180-LY86 heterodimers. Ref.9
Subcellular location	Cell membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed mainly on mature peripherical B cells. Detected in spleen, lymph node and appendix. Not detected in pre-B and -T cells.
Sequence similarities	Belongs to the Toll-like receptor family. Contains 19 LRR (leucine-rich) repeats. Contains 1 LRRCT domain. Contains 1 LRRNT domain.

Ontologies

Keywords
Biological process	Immunity Inflammatory response Innate immunity
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Leucine-rich repeat Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of lipopolysaccharide-mediated signaling pathway Inferred from genetic interaction PubMed 10880523. Source: MGI
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.6

Chain

24 – 661

638

CD180 antigen

PRO_0000034741

Regions

Topological domain

24 – 626

603

Extracellular Potential

Transmembrane

627 – 650

24

Helical; Potential

Topological domain

651 – 661

11

Cytoplasmic Potential

Domain

33 – 53

21

LRRNT

Repeat

54 – 75

22

LRR 1

Repeat

78 – 99

22

LRR 2

Repeat

102 – 123

22

LRR 3

Repeat

126 – 147

22

LRR 4

Repeat

150 – 171

22

LRR 5

Repeat

174 – 195

22

LRR 6

Repeat

201 – 221

21

LRR 7

Repeat

275 – 296

22

LRR 8

Repeat

299 – 320

22

LRR 9

Repeat

322 – 343

22

LRR 10

Repeat

346 – 366

21

LRR 11

Repeat

371 – 391

21

LRR 12

Repeat

397 – 418

22

LRR 13

Repeat

421 – 442

22

LRR 14

Repeat

446 – 466

21

LRR 15

Repeat

470 – 493

24

LRR 16

Repeat

497 – 518

22

LRR 17

Repeat

521 – 544

24

LRR 18

Repeat

546 – 564

19

LRR 19

Domain

577 – 627

51

LRRCT

Amino acid modifications

Glycosylation

34

1

N-linked (GlcNAc...) Potential

Glycosylation

53

1

N-linked (GlcNAc...) Potential

Glycosylation

70

1

N-linked (GlcNAc...) Potential

Glycosylation

78

1

N-linked (GlcNAc...) Ref.8

Glycosylation

201

1

N-linked (GlcNAc...) Potential

Glycosylation

234

1

N-linked (GlcNAc...) Potential

Glycosylation

244

1

N-linked (GlcNAc...) Potential

Glycosylation

394

1

N-linked (GlcNAc...) Potential

Glycosylation

402

1

N-linked (GlcNAc...) Ref.9

Glycosylation

451

1

N-linked (GlcNAc...) Ref.9

Glycosylation

573

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

20

1

V → L.
Corresponds to variant rs5744463 [ dbSNP | Ensembl ].

VAR_057298

Natural variant

53

1

N → K.
Corresponds to variant rs16875312 [ dbSNP | Ensembl ].

VAR_021978

Natural variant

99

1

S → R.
Corresponds to variant rs2230520 [ dbSNP | Ensembl ].

VAR_021979

Natural variant

259

1

D → N.
Corresponds to variant rs5744525 [ dbSNP | Ensembl ].

VAR_057299

Natural variant

356

1

V → M.
Corresponds to variant rs56752081 [ dbSNP | Ensembl ].

VAR_061859

Natural variant

430

1

T → A.
Corresponds to variant rs2230523 [ dbSNP | Ensembl ].

VAR_057300

Natural variant

648

1

F → L.
Corresponds to variant rs2230524 [ dbSNP | Ensembl ].

VAR_057301

Experimental info

Sequence conflict

223

1

I → V in BAA12019. Ref.1

Sequence conflict

223

1

I → V in BAG35994. Ref.2

Sequence conflict

223

1

I → V in EAW51318. Ref.4

Sequence conflict

223

1

I → V in AAI09070. Ref.5

Sequence conflict

223

1

I → V in AAI09071. Ref.5

Secondary structure

1

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661

Helix Strand Turn

Details...

Beta strand

29 – 32

4

Turn

33 – 35

3

Beta strand

36 – 38

3

Beta strand

57 – 59

3

Beta strand

66 – 68

3

Turn

70 – 75

6

Beta strand

80 – 83

4

Turn

94 – 99

6

Beta strand

105 – 107

3

Turn

118 – 121

4

Beta strand

129 – 131

3

Helix

140 – 142

3

Beta strand

153 – 155

3

Beta strand

177 – 179

3

Helix

190 – 194

5

Turn

195 – 198

4

Beta strand

200 – 205

6

Turn

216 – 221

6

Beta strand

223 – 228

6

Helix

235 – 241

7

Turn

242 – 244

3

Beta strand

246 – 251

6

Turn

265 – 268

4

Helix

269 – 273

5

Beta strand

274 – 280

7

Beta strand

286 – 288

3

Turn

291 – 294

4

Helix

296 – 299

4

Beta strand

301 – 304

4

Beta strand

325 – 327

3

Helix

336 – 339

4

Helix

341 – 343

3

Beta strand

349 – 351

3

Turn

365 – 368

4

Beta strand

374 – 376

3

Beta strand

384 – 388

5

Turn

389 – 391

3

Beta strand

400 – 402

3

Beta strand

409 – 411

3

Turn

413 – 418

6

Beta strand

424 – 426

3

Turn

440 – 443

4

Beta strand

449 – 451

3

Turn

462 – 467

6

Beta strand

473 – 475

3

Helix

482 – 484

3

Helix

491 – 494

4

Beta strand

500 – 502

3

Turn

513 – 518

6

Beta strand

524 – 526

3

Helix

534 – 540

7

Beta strand

547 – 549

3

Helix

563 – 567

5

Beta strand

569 – 573

5

Helix

583 – 585

3

Helix

586 – 594

9

Beta strand

598 – 600

3

Beta strand

607 – 613

7

Turn

618 – 620

3

Sequences

	Sequence		Length	Mass (Da)
	Q99467 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 93DE3178594B3383	FASTA	661	74,179
	10 20 30 40 50 60 MAFDVSCFFW VVLFSAGCKV ITSWDQMCIE KEANKTYNCE NLGLSEIPDT LPNTTEFLEF 70 80 90 100 110 120 SFNFLPTIHN RTFSRLMNLT FLDLTRCQIN WIHEDTFQSH HQLSTLVLTG NPLIFMAETS 130 140 150 160 170 180 LNGPKSLKHL FLIQTGISNL EFIPVHNLEN LESLYLGSNH ISSIKFPKDF PARNLKVLDF 190 200 210 220 230 240 QNNAIHYISR EDMRSLEQAI NLSLNFNGNN VKGIELGAFD STIFQSLNFG GTPNLSVIFN 250 260 270 280 290 300 GLQNSTTQSL WLGTFEDIDD EDISSAMLKG LCEMSVESLN LQEHRFSDIS STTFQCFTQL 310 320 330 340 350 360 QELDLTATHL KGLPSGMKGL NLLKKLVLSV NHFDQLCQIS AANFPSLTHL YIRGNVKKLH 370 380 390 400 410 420 LGVGCLEKLG NLQTLDLSHN DIEASDCCSL QLKNLSHLQT LNLSHNEPLG LQSQAFKECP 430 440 450 460 470 480 QLELLDLAFT RLHINAPQSP FQNLHFLQVL NLTYCFLDTS NQHLLAGLPV LRHLNLKGNH 490 500 510 520 530 540 FQDGTITKTN LLQTVGSLEV LILSSCGLLS IDQQAFHSLG KMSHVDLSHN SLTCDSIDSL 550 560 570 580 590 600 SHLKGIYLNL AANSINIISP RLLPILSQQS TINLSHNPLD CTCSNIHFLT WYKENLHKLE 610 620 630 640 650 660 GSEETTCANP PSLRGVKLSD VKLSCGITAI GIFFLIVFLL LLAILLFFAV KYLLRWKYQH I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a human RP105 homologue and chromosomal localization of the mouse and human RP105 genes (Ly64 and LY64)." Miura Y., Miyake K., Yamashita Y., Shimazu R., Copeland N.G., Gilbert D.J., Jenkins N.A., Inazawa J., Abe T., Kimoto M. Genomics 38:299-304(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: B-cell lymphoma.
[2]	"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: Lung.
[3]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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].
[5]	"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].
[6]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-38.
[7]	"RP105 is associated with MD-1 and transmits an activation signal in human B cells." Miura Y., Shimazu R., Miyake K., Akashi S., Ogata H., Yamashita Y., Narisawa Y., Kimoto M. Blood 92:2815-2822(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LY86.
[8]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, MASS SPECTROMETRY. Tissue: Liver.
[9]	"Crystal structures of mouse and human RP105/MD-1 complexes reveal unique dimer organization of the toll-like receptor family." Ohto U., Miyake K., Shimizu T. J. Mol. Biol. 413:815-825(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-626 IN COMPLEX WITH LY86, SUBUNIT, GLYCOSYLATION AT ASN-402 AND ASN-451.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D83597 mRNA. Translation: BAA12019.1.
AK313177 mRNA. Translation: BAG35994.1.
AC026445 Genomic DNA. No translation available.
CH471137 Genomic DNA. Translation: EAW51318.1.
BC109069 mRNA. Translation: AAI09070.1.
BC109070 mRNA. Translation: AAI09071.1.

IPI

IPI00023722.

RefSeq

NP_005573.2. NM_005582.2.

UniGene

Hs.87205.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3B2D	X-ray	2.80	A/B	24-626	[»]

ProteinModelPortal

Q99467.

SMR

Q99467. Positions 26-626.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59104N.

STRING

9606.ENSP00000256447.

PTM databases

PhosphoSite

Q99467.

Polymorphism databases

DMDM

296434437.

Proteomic databases

PaxDb

Q99467.

PRIDE

Q99467.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256447; ENSP00000256447; ENSG00000134061.

GeneID

4064.

KEGG

hsa:4064.

UCSC

uc003juy.2. human.

Organism-specific databases

CTD

4064.

GeneCards

GC05M066514.

H-InvDB

HIX0032100.

HGNC

HGNC:6726. CD180.

HPA

HPA003740.

MIM

602226. gene.

neXtProt

NX_Q99467.

PharmGKB

PA30490.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG319009.

HOGENOM

HOG000146395.

HOVERGEN

HBG050848.

InParanoid

Q99467.

KO

K06555.

OMA

KGLCEMS.

OrthoDB

EOG4W3SMG.

PhylomeDB

Q99467.

Gene expression databases

Bgee

Q99467.

CleanEx

HS_CD180.

Genevestigator

Q99467.

GermOnline

ENSG00000134061. Homo sapiens.

Family and domain databases

InterPro

IPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
[Graphical view]

SMART

SM00082. LRRCT. 1 hit.
[Graphical view]

PROSITE

PS51450. LRR. 12 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CD180. human.

GenomeRNAi

4064.

NextBio

15932.

SOURCE

Search...

Entry information

Entry name

CD180_HUMAN

Accession

Primary (citable) accession number: Q99467
Secondary accession number(s): B2R7Z7, Q32MM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 114 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.