CD180_MOUSE
ID CD180_MOUSE Reviewed; 661 AA.
AC Q62192; Q8C251;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=CD180 antigen;
DE AltName: Full=Lymphocyte antigen 78;
DE Short=Ly-78;
DE AltName: Full=Radioprotective 105 kDa protein;
DE AltName: CD_antigen=CD180;
DE Flags: Precursor;
GN Name=Cd180; Synonyms=Ly78, Rp105;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 21-43.
RC STRAIN=BALB/cJ; TISSUE=B-cell lymphoma;
RX PubMed=7897216;
RA Miyake K., Yamashita Y., Ogata M., Sudo T., Kimoto M.;
RT "RP105, a novel B cell surface molecule implicated in B cell activation, is
RT a member of the leucine-rich repeat protein family.";
RL J. Immunol. 154:3333-3340(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP INTERACTION WITH LY86.
RX PubMed=9686597;
RA Miyake K., Shimazu R., Kondo J., Niki T., Akashi S., Ogata H.,
RA Yamashita Y., Miura Y., Kimoto M.;
RT "Mouse MD-1, a molecule that is physically associated with RP105 and
RT positively regulates its expression.";
RL J. Immunol. 161:1348-1353(1998).
RN [4]
RP FUNCTION.
RX PubMed=10880523; DOI=10.1084/jem.192.1.23;
RA Ogata H., Su I., Miyake K., Nagai Y., Akashi S., Mecklenbraeuker I.,
RA Rajewsky K., Kimoto M., Tarakhovsky A.;
RT "The Toll-like receptor protein RP105 regulates lipopolysaccharide
RT signaling in B cells.";
RL J. Exp. Med. 192:23-29(2000).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 21-626 IN COMPLEX WITH LY86,
RP SUBUNIT, AND GLYCOSYLATION AT ASN-34; ASN-53; ASN-70; ASN-244; ASN-394;
RP ASN-402 AND ASN-451.
RX PubMed=21959264; DOI=10.1016/j.jmb.2011.09.020;
RA Ohto U., Miyake K., Shimizu T.;
RT "Crystal structures of mouse and human RP105/MD-1 complexes reveal unique
RT dimer organization of the toll-like receptor family.";
RL J. Mol. Biol. 413:815-825(2011).
CC -!- FUNCTION: May cooperate with MD-1 and TLR4 to mediate the innate immune
CC response to bacterial lipopolysaccharide (LPS) in B-cells. Leads to NF-
CC kappa-B activation. Also involved in the life/death decision of B-
CC cells. {ECO:0000269|PubMed:10880523}.
CC -!- SUBUNIT: M-shaped tetramer of two CD180-LY86 heterodimers.
CC {ECO:0000269|PubMed:21959264}.
CC -!- INTERACTION:
CC Q62192; O88188: Ly86; NbExp=5; IntAct=EBI-79487, EBI-79494;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: B-lymphocytes and spleen. Not detected in thymus,
CC kidney, muscle, heart, brain or liver.
CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D37797; BAA07043.1; -; mRNA.
DR EMBL; AK089255; BAC40816.1; -; mRNA.
DR CCDS; CCDS26741.1; -.
DR PIR; I56258; I56258.
DR RefSeq; NP_032559.2; NM_008533.2.
DR PDB; 3T6Q; X-ray; 1.90 A; A/B=21-626.
DR PDBsum; 3T6Q; -.
DR AlphaFoldDB; Q62192; -.
DR SMR; Q62192; -.
DR DIP; DIP-30961N; -.
DR IntAct; Q62192; 1.
DR STRING; 10090.ENSMUSP00000022124; -.
DR GlyConnect; 2197; 1 N-Linked glycan (1 site).
DR GlyGen; Q62192; 10 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q62192; -.
DR PhosphoSitePlus; Q62192; -.
DR SwissPalm; Q62192; -.
DR EPD; Q62192; -.
DR MaxQB; Q62192; -.
DR PaxDb; Q62192; -.
DR PRIDE; Q62192; -.
DR ProteomicsDB; 281134; -.
DR Antibodypedia; 1122; 436 antibodies from 38 providers.
DR DNASU; 17079; -.
DR Ensembl; ENSMUST00000022124; ENSMUSP00000022124; ENSMUSG00000021624.
DR GeneID; 17079; -.
DR KEGG; mmu:17079; -.
DR UCSC; uc007rry.1; mouse.
DR CTD; 4064; -.
DR MGI; MGI:1194924; Cd180.
DR VEuPathDB; HostDB:ENSMUSG00000021624; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000161183; -.
DR HOGENOM; CLU_006000_5_1_1; -.
DR InParanoid; Q62192; -.
DR OMA; MCTEKEA; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q62192; -.
DR TreeFam; TF351113; -.
DR Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR BioGRID-ORCS; 17079; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Cd180; mouse.
DR PRO; PR:Q62192; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q62192; protein.
DR Bgee; ENSMUSG00000021624; Expressed in mesenteric lymph node and 73 other tissues.
DR ExpressionAtlas; Q62192; baseline and differential.
DR Genevisible; Q62192; MM.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0002322; P:B cell proliferation involved in immune response; IMP:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IGI:MGI.
DR GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IGI:MGI.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR041281; LRR_11.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR017241; Toll-like_receptor.
DR PANTHER; PTHR24365; PTHR24365; 1.
DR Pfam; PF18831; LRR_11; 1.
DR Pfam; PF13855; LRR_8; 3.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00082; LRRCT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Glycoprotein;
KW Immunity; Inflammatory response; Innate immunity; Leucine-rich repeat;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:7897216"
FT CHAIN 21..661
FT /note="CD180 antigen"
FT /id="PRO_0000034742"
FT TOPO_DOM 21..626
FT /note="Extracellular"
FT TRANSMEM 627..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651..661
FT /note="Cytoplasmic"
FT DOMAIN 33..53
FT /note="LRRNT"
FT REPEAT 54..75
FT /note="LRR 1"
FT REPEAT 78..99
FT /note="LRR 2"
FT REPEAT 102..123
FT /note="LRR 3"
FT REPEAT 126..147
FT /note="LRR 4"
FT REPEAT 150..171
FT /note="LRR 5"
FT REPEAT 174..195
FT /note="LRR 6"
FT REPEAT 201..221
FT /note="LRR 7"
FT REPEAT 275..296
FT /note="LRR 8"
FT REPEAT 299..321
FT /note="LRR 9"
FT REPEAT 322..343
FT /note="LRR 10"
FT REPEAT 346..366
FT /note="LRR 11"
FT REPEAT 371..391
FT /note="LRR 12"
FT REPEAT 397..418
FT /note="LRR 13"
FT REPEAT 421..442
FT /note="LRR 14"
FT REPEAT 446..466
FT /note="LRR 15"
FT REPEAT 470..493
FT /note="LRR 16"
FT REPEAT 497..518
FT /note="LRR 17"
FT REPEAT 521..544
FT /note="LRR 18"
FT REPEAT 546..566
FT /note="LRR 19"
FT DOMAIN 577..627
FT /note="LRRCT"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21959264"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21959264"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21959264"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21959264"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21959264"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21959264"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21959264"
FT CONFLICT 22
FT /note="T -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="S -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="C -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="L -> P (in Ref. 1; BAA07043)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="R -> H (in Ref. 1; BAA07043)"
FT /evidence="ECO:0000305"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:3T6Q"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3T6Q"
FT TURN 94..99
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3T6Q"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:3T6Q"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3T6Q"
FT TURN 216..221
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:3T6Q"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:3T6Q"
FT TURN 291..296
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:3T6Q"
FT TURN 365..368
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:3T6Q"
FT TURN 389..394
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:3T6Q"
FT TURN 413..418
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:3T6Q"
FT TURN 440..443
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:3T6Q"
FT TURN 462..467
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 491..494
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:3T6Q"
FT TURN 513..518
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 534..540
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 563..567
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 583..585
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 586..594
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:3T6Q"
FT STRAND 606..610
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 611..613
FT /evidence="ECO:0007829|PDB:3T6Q"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:3T6Q"
SQ SEQUENCE 661 AA; 74302 MW; 12F91AAB4224602E CRC64;
MAPDISCFFL VALFLASCRA TTSSDQKCIE KEVNKTYNCE NLGLNEIPGT LPNSTECLEF
SFNVLPTIQN TTFSRLINLT FLDLTRCQIY WIHEDTFQSQ HRLDTLVLTA NPLIFMAETA
LSGPKALKHL FFIQTGISSI DFIPLHNQKT LESLYLGSNH ISSIKLPKGF PTEKLKVLDF
QNNAIHYLSK EDMSSLQQAT NLSLNLNGND IAGIELGAFD SAVFQSLNFG GTQNLLVIFK
GLKNSTIQSL WLGTFEDMDD EDISPAVFEG LCEMSVESIN LQKHYFFNIS SNTFHCFSGL
QELDLTATHL SELPSGLVGL STLKKLVLSA NKFENLCQIS ASNFPSLTHL SIKGNTKRLE
LGTGCLENLE NLRELDLSHD DIETSDCCNL QLRNLSHLQS LNLSYNEPLS LKTEAFKECP
QLELLDLAFT RLKVKDAQSP FQNLHLLKVL NLSHSLLDIS SEQLFDGLPA LQHLNLQGNH
FPKGNIQKTN SLQTLGRLEI LVLSFCDLSS IDQHAFTSLK MMNHVDLSHN RLTSSSIEAL
SHLKGIYLNL ASNRISIILP SLLPILSQQR TINLRQNPLD CTCSNIYFLE WYKENMQKLE
DTEDTLCENP PLLRGVRLSD VTLSCSMAAV GIFFLIVFLL VFAILLIFAV KYFLRWKYQH
I
