Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

CD180 antigen

Gene

Cd180

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Biological processi

  • B cell proliferation involved in immune response Source: MGI
  • cellular response to lipopolysaccharide Source: MGI
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • positive regulation of lipopolysaccharide-mediated signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiR-MMU-166016. Toll Like Receptor 4 (TLR4) Cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
CD180 antigen
Alternative name(s):
Lymphocyte antigen 78
Short name:
Ly-78
Radioprotective 105 kDa protein
CD_antigen: CD180
Gene namesi
Name:Cd180
Synonyms:Ly78, Rp105
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1194924. Cd180.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 626606ExtracellularAdd
BLAST
Transmembranei627 – 65024HelicalSequence analysisAdd
BLAST
Topological domaini651 – 66111CytoplasmicAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 661641CD180 antigenPRO_0000034742Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341N-linked (GlcNAc...)1 Publication
Glycosylationi53 – 531N-linked (GlcNAc...)1 Publication
Glycosylationi70 – 701N-linked (GlcNAc...)1 Publication
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence analysis
Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence analysis
Glycosylationi244 – 2441N-linked (GlcNAc...)1 Publication
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence analysis
Glycosylationi394 – 3941N-linked (GlcNAc...)1 Publication
Glycosylationi402 – 4021N-linked (GlcNAc...)1 Publication
Glycosylationi451 – 4511N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ62192.
PaxDbiQ62192.
PRIDEiQ62192.

PTM databases

PhosphoSiteiQ62192.

Expressioni

Tissue specificityi

B-lymphocytes and spleen. Not detected in thymus, kidney, muscle, heart, brain or liver.

Gene expression databases

BgeeiQ62192.
CleanExiMM_CD180.
ExpressionAtlasiQ62192. baseline and differential.
GenevisibleiQ62192. MM.

Interactioni

Subunit structurei

M-shaped tetramer of two CD180-LY86 heterodimers.1 Publication

Protein-protein interaction databases

DIPiDIP-30961N.
IntActiQ62192. 1 interaction.
STRINGi10090.ENSMUSP00000022124.

Structurei

Secondary structure

1
661
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 324Combined sources
Turni33 – 353Combined sources
Beta strandi36 – 383Combined sources
Beta strandi57 – 593Combined sources
Beta strandi66 – 683Combined sources
Beta strandi80 – 834Combined sources
Turni94 – 996Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi114 – 1163Combined sources
Turni118 – 1214Combined sources
Beta strandi129 – 1313Combined sources
Helixi140 – 1423Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi177 – 1793Combined sources
Helixi190 – 1945Combined sources
Turni195 – 1984Combined sources
Beta strandi201 – 2055Combined sources
Turni216 – 2216Combined sources
Beta strandi223 – 2286Combined sources
Helixi235 – 2417Combined sources
Turni242 – 2443Combined sources
Beta strandi246 – 2516Combined sources
Helixi265 – 2739Combined sources
Beta strandi274 – 2807Combined sources
Turni291 – 2966Combined sources
Beta strandi301 – 3044Combined sources
Beta strandi325 – 3273Combined sources
Helixi336 – 3394Combined sources
Helixi341 – 3433Combined sources
Beta strandi348 – 3514Combined sources
Turni365 – 3684Combined sources
Beta strandi374 – 3763Combined sources
Beta strandi384 – 3885Combined sources
Turni389 – 3946Combined sources
Beta strandi400 – 4023Combined sources
Beta strandi409 – 4113Combined sources
Turni413 – 4186Combined sources
Beta strandi423 – 4264Combined sources
Turni440 – 4434Combined sources
Beta strandi449 – 4513Combined sources
Turni462 – 4676Combined sources
Beta strandi473 – 4753Combined sources
Helixi482 – 4843Combined sources
Helixi491 – 4944Combined sources
Beta strandi500 – 5023Combined sources
Turni513 – 5186Combined sources
Beta strandi524 – 5263Combined sources
Helixi534 – 5407Combined sources
Beta strandi547 – 5493Combined sources
Helixi560 – 5623Combined sources
Helixi563 – 5675Combined sources
Beta strandi569 – 5735Combined sources
Helixi583 – 5853Combined sources
Helixi586 – 5949Combined sources
Helixi596 – 5983Combined sources
Helixi602 – 6043Combined sources
Beta strandi606 – 6105Combined sources
Helixi611 – 6133Combined sources
Helixi618 – 6203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3T6QX-ray1.90A/B21-626[»]
ProteinModelPortaliQ62192.
SMRiQ62192. Positions 26-626.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 5321LRRNTAdd
BLAST
Repeati54 – 7522LRR 1Add
BLAST
Repeati78 – 9922LRR 2Add
BLAST
Repeati102 – 12322LRR 3Add
BLAST
Repeati126 – 14722LRR 4Add
BLAST
Repeati150 – 17122LRR 5Add
BLAST
Repeati174 – 19522LRR 6Add
BLAST
Repeati201 – 22121LRR 7Add
BLAST
Repeati275 – 29622LRR 8Add
BLAST
Repeati299 – 32123LRR 9Add
BLAST
Repeati322 – 34322LRR 10Add
BLAST
Repeati346 – 36621LRR 11Add
BLAST
Repeati371 – 39121LRR 12Add
BLAST
Repeati397 – 41822LRR 13Add
BLAST
Repeati421 – 44222LRR 14Add
BLAST
Repeati446 – 46621LRR 15Add
BLAST
Repeati470 – 49324LRR 16Add
BLAST
Repeati497 – 51822LRR 17Add
BLAST
Repeati521 – 54424LRR 18Add
BLAST
Repeati546 – 56621LRR 19Add
BLAST
Domaini577 – 62751LRRCTAdd
BLAST

Sequence similaritiesi

Belongs to the Toll-like receptor family.Curated
Contains 19 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000146395.
HOVERGENiHBG050848.
InParanoidiQ62192.
KOiK06555.
OMAiTEAFKEC.
OrthoDBiEOG7ZKS9G.
TreeFamiTF351113.

Family and domain databases

Gene3Di3.80.10.10. 4 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamiPF13855. LRR_8. 3 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 7 hits.
SM00082. LRRCT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 3 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62192-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPDISCFFL VALFLASCRA TTSSDQKCIE KEVNKTYNCE NLGLNEIPGT
60 70 80 90 100
LPNSTECLEF SFNVLPTIQN TTFSRLINLT FLDLTRCQIY WIHEDTFQSQ
110 120 130 140 150
HRLDTLVLTA NPLIFMAETA LSGPKALKHL FFIQTGISSI DFIPLHNQKT
160 170 180 190 200
LESLYLGSNH ISSIKLPKGF PTEKLKVLDF QNNAIHYLSK EDMSSLQQAT
210 220 230 240 250
NLSLNLNGND IAGIELGAFD SAVFQSLNFG GTQNLLVIFK GLKNSTIQSL
260 270 280 290 300
WLGTFEDMDD EDISPAVFEG LCEMSVESIN LQKHYFFNIS SNTFHCFSGL
310 320 330 340 350
QELDLTATHL SELPSGLVGL STLKKLVLSA NKFENLCQIS ASNFPSLTHL
360 370 380 390 400
SIKGNTKRLE LGTGCLENLE NLRELDLSHD DIETSDCCNL QLRNLSHLQS
410 420 430 440 450
LNLSYNEPLS LKTEAFKECP QLELLDLAFT RLKVKDAQSP FQNLHLLKVL
460 470 480 490 500
NLSHSLLDIS SEQLFDGLPA LQHLNLQGNH FPKGNIQKTN SLQTLGRLEI
510 520 530 540 550
LVLSFCDLSS IDQHAFTSLK MMNHVDLSHN RLTSSSIEAL SHLKGIYLNL
560 570 580 590 600
ASNRISIILP SLLPILSQQR TINLRQNPLD CTCSNIYFLE WYKENMQKLE
610 620 630 640 650
DTEDTLCENP PLLRGVRLSD VTLSCSMAAV GIFFLIVFLL VFAILLIFAV
660
KYFLRWKYQH I
Length:661
Mass (Da):74,302
Last modified:July 27, 2011 - v2
Checksum:i12F91AAB4224602E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221T → D AA sequence (PubMed:7897216).Curated
Sequence conflicti24 – 241S → N AA sequence (PubMed:7897216).Curated
Sequence conflicti28 – 281C → L AA sequence (PubMed:7897216).Curated
Sequence conflicti216 – 2161L → P in BAA07043 (PubMed:7897216).Curated
Sequence conflicti554 – 5541R → H in BAA07043 (PubMed:7897216).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37797 mRNA. Translation: BAA07043.1.
AK089255 mRNA. Translation: BAC40816.1.
CCDSiCCDS26741.1.
PIRiI56258.
RefSeqiNP_032559.2. NM_008533.2.
UniGeneiMm.373974.

Genome annotation databases

EnsembliENSMUST00000022124; ENSMUSP00000022124; ENSMUSG00000021624.
GeneIDi17079.
KEGGimmu:17079.
UCSCiuc007rry.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37797 mRNA. Translation: BAA07043.1.
AK089255 mRNA. Translation: BAC40816.1.
CCDSiCCDS26741.1.
PIRiI56258.
RefSeqiNP_032559.2. NM_008533.2.
UniGeneiMm.373974.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3T6QX-ray1.90A/B21-626[»]
ProteinModelPortaliQ62192.
SMRiQ62192. Positions 26-626.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-30961N.
IntActiQ62192. 1 interaction.
STRINGi10090.ENSMUSP00000022124.

PTM databases

PhosphoSiteiQ62192.

Proteomic databases

MaxQBiQ62192.
PaxDbiQ62192.
PRIDEiQ62192.

Protocols and materials databases

DNASUi17079.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022124; ENSMUSP00000022124; ENSMUSG00000021624.
GeneIDi17079.
KEGGimmu:17079.
UCSCiuc007rry.1. mouse.

Organism-specific databases

CTDi4064.
MGIiMGI:1194924. Cd180.

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000146395.
HOVERGENiHBG050848.
InParanoidiQ62192.
KOiK06555.
OMAiTEAFKEC.
OrthoDBiEOG7ZKS9G.
TreeFamiTF351113.

Enzyme and pathway databases

ReactomeiR-MMU-166016. Toll Like Receptor 4 (TLR4) Cascade.

Miscellaneous databases

NextBioi291202.
PROiQ62192.
SOURCEiSearch...

Gene expression databases

BgeeiQ62192.
CleanExiMM_CD180.
ExpressionAtlasiQ62192. baseline and differential.
GenevisibleiQ62192. MM.

Family and domain databases

Gene3Di3.80.10.10. 4 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamiPF13855. LRR_8. 3 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 7 hits.
SM00082. LRRCT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RP105, a novel B cell surface molecule implicated in B cell activation, is a member of the leucine-rich repeat protein family."
    Miyake K., Yamashita Y., Ogata M., Sudo T., Kimoto M.
    J. Immunol. 154:3333-3340(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-43.
    Strain: BALB/cJ.
    Tissue: B-cell lymphoma.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
  3. "Mouse MD-1, a molecule that is physically associated with RP105 and positively regulates its expression."
    Miyake K., Shimazu R., Kondo J., Niki T., Akashi S., Ogata H., Yamashita Y., Miura Y., Kimoto M.
    J. Immunol. 161:1348-1353(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LY86.
  4. "The Toll-like receptor protein RP105 regulates lipopolysaccharide signaling in B cells."
    Ogata H., Su I., Miyake K., Nagai Y., Akashi S., Mecklenbraeuker I., Rajewsky K., Kimoto M., Tarakhovsky A.
    J. Exp. Med. 192:23-29(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.
  6. "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 (1.9 ANGSTROMS) OF 21-626 IN COMPLEX WITH LY86, SUBUNIT, GLYCOSYLATION AT ASN-34; ASN-53; ASN-70; ASN-244; ASN-394; ASN-402 AND ASN-451.

Entry informationi

Entry nameiCD180_MOUSE
AccessioniPrimary (citable) accession number: Q62192
Secondary accession number(s): Q8C251
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.