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CD180 antigen (Lymphocyte antigen 78) (Ly-78) (Radioprotective 105 kDa protein) (CD antigen CD180)

 CD180_MOUSE             Reviewed;         661 AA.
Q62192; Q8C251;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
23-MAY-2018, entry version 140.
RecName: Full=CD180 antigen;
AltName: Full=Lymphocyte antigen 78;
Short=Ly-78;
AltName: Full=Radioprotective 105 kDa protein;
AltName: CD_antigen=CD180;
Flags: Precursor;
Name=Cd180; Synonyms=Ly78, Rp105;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 21-43.
STRAIN=BALB/cJ; TISSUE=B-cell lymphoma;
PubMed=7897216;
Miyake K., Yamashita Y., Ogata M., Sudo T., Kimoto M.;
"RP105, a novel B cell surface molecule implicated in B cell
activation, is a member of the leucine-rich repeat protein family.";
J. Immunol. 154:3333-3340(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
INTERACTION WITH LY86.
PubMed=9686597;
Miyake K., Shimazu R., Kondo J., Niki T., Akashi S., Ogata H.,
Yamashita Y., Miura Y., Kimoto M.;
"Mouse MD-1, a molecule that is physically associated with RP105 and
positively regulates its expression.";
J. Immunol. 161:1348-1353(1998).
[4]
FUNCTION.
PubMed=10880523; DOI=10.1084/jem.192.1.23;
Ogata H., Su I., Miyake K., Nagai Y., Akashi S., Mecklenbraeuker I.,
Rajewsky K., Kimoto M., Tarakhovsky A.;
"The Toll-like receptor protein RP105 regulates lipopolysaccharide
signaling in B cells.";
J. Exp. Med. 192:23-29(2000).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 21-626 IN COMPLEX WITH LY86,
SUBUNIT, AND GLYCOSYLATION AT ASN-34; ASN-53; ASN-70; ASN-244;
ASN-394; ASN-402 AND ASN-451.
PubMed=21959264; DOI=10.1016/j.jmb.2011.09.020;
Ohto U., Miyake K., Shimizu T.;
"Crystal structures of mouse and human RP105/MD-1 complexes reveal
unique dimer organization of the toll-like receptor family.";
J. Mol. Biol. 413:815-825(2011).
-!- 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. {ECO:0000269|PubMed:10880523}.
-!- SUBUNIT: M-shaped tetramer of two CD180-LY86 heterodimers.
{ECO:0000269|PubMed:21959264}.
-!- INTERACTION:
O88188:Ly86; NbExp=5; IntAct=EBI-79487, EBI-79494;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: B-lymphocytes and spleen. Not detected in
thymus, kidney, muscle, heart, brain or liver.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D37797; BAA07043.1; -; mRNA.
EMBL; AK089255; BAC40816.1; -; mRNA.
CCDS; CCDS26741.1; -.
PIR; I56258; I56258.
RefSeq; NP_032559.2; NM_008533.2.
UniGene; Mm.373974; -.
PDB; 3T6Q; X-ray; 1.90 A; A/B=21-626.
PDBsum; 3T6Q; -.
ProteinModelPortal; Q62192; -.
SMR; Q62192; -.
DIP; DIP-30961N; -.
IntAct; Q62192; 1.
STRING; 10090.ENSMUSP00000022124; -.
iPTMnet; Q62192; -.
PhosphoSitePlus; Q62192; -.
SwissPalm; Q62192; -.
MaxQB; Q62192; -.
PaxDb; Q62192; -.
PRIDE; Q62192; -.
DNASU; 17079; -.
Ensembl; ENSMUST00000022124; ENSMUSP00000022124; ENSMUSG00000021624.
GeneID; 17079; -.
KEGG; mmu:17079; -.
UCSC; uc007rry.1; mouse.
CTD; 4064; -.
MGI; MGI:1194924; Cd180.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000119006; -.
HOGENOM; HOG000146395; -.
HOVERGEN; HBG050848; -.
InParanoid; Q62192; -.
KO; K06555; -.
OMA; PLDCTCS; -.
OrthoDB; EOG091G01RC; -.
TreeFam; TF351113; -.
Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
PRO; PR:Q62192; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021624; -.
CleanEx; MM_CD180; -.
ExpressionAtlas; Q62192; baseline and differential.
Genevisible; Q62192; MM.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0002322; P:B cell proliferation involved in immune response; IMP:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IGI:MGI.
GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
Pfam; PF13855; LRR_8; 3.
SMART; SM00369; LRR_TYP; 7.
SMART; SM00082; LRRCT; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Glycoprotein; Immunity;
Inflammatory response; Innate immunity; Leucine-rich repeat; Membrane;
Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 20 {ECO:0000269|PubMed:7897216}.
CHAIN 21 661 CD180 antigen.
/FTId=PRO_0000034742.
TOPO_DOM 21 626 Extracellular.
TRANSMEM 627 650 Helical. {ECO:0000255}.
TOPO_DOM 651 661 Cytoplasmic.
DOMAIN 33 53 LRRNT.
REPEAT 54 75 LRR 1.
REPEAT 78 99 LRR 2.
REPEAT 102 123 LRR 3.
REPEAT 126 147 LRR 4.
REPEAT 150 171 LRR 5.
REPEAT 174 195 LRR 6.
REPEAT 201 221 LRR 7.
REPEAT 275 296 LRR 8.
REPEAT 299 321 LRR 9.
REPEAT 322 343 LRR 10.
REPEAT 346 366 LRR 11.
REPEAT 371 391 LRR 12.
REPEAT 397 418 LRR 13.
REPEAT 421 442 LRR 14.
REPEAT 446 466 LRR 15.
REPEAT 470 493 LRR 16.
REPEAT 497 518 LRR 17.
REPEAT 521 544 LRR 18.
REPEAT 546 566 LRR 19.
DOMAIN 577 627 LRRCT.
CARBOHYD 34 34 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21959264}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21959264}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21959264}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 244 244 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21959264}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 394 394 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21959264}.
CARBOHYD 402 402 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21959264}.
CARBOHYD 451 451 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21959264}.
CONFLICT 22 22 T -> D (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 24 24 S -> N (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 28 28 C -> L (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 216 216 L -> P (in Ref. 1; BAA07043).
{ECO:0000305}.
CONFLICT 554 554 R -> H (in Ref. 1; BAA07043).
{ECO:0000305}.
STRAND 29 32 {ECO:0000244|PDB:3T6Q}.
TURN 33 35 {ECO:0000244|PDB:3T6Q}.
STRAND 36 38 {ECO:0000244|PDB:3T6Q}.
STRAND 57 59 {ECO:0000244|PDB:3T6Q}.
STRAND 66 68 {ECO:0000244|PDB:3T6Q}.
STRAND 80 83 {ECO:0000244|PDB:3T6Q}.
TURN 94 99 {ECO:0000244|PDB:3T6Q}.
STRAND 105 107 {ECO:0000244|PDB:3T6Q}.
STRAND 114 116 {ECO:0000244|PDB:3T6Q}.
TURN 118 121 {ECO:0000244|PDB:3T6Q}.
STRAND 129 131 {ECO:0000244|PDB:3T6Q}.
HELIX 140 142 {ECO:0000244|PDB:3T6Q}.
STRAND 153 155 {ECO:0000244|PDB:3T6Q}.
STRAND 177 179 {ECO:0000244|PDB:3T6Q}.
HELIX 190 194 {ECO:0000244|PDB:3T6Q}.
TURN 195 198 {ECO:0000244|PDB:3T6Q}.
STRAND 201 205 {ECO:0000244|PDB:3T6Q}.
TURN 216 221 {ECO:0000244|PDB:3T6Q}.
STRAND 223 228 {ECO:0000244|PDB:3T6Q}.
HELIX 235 241 {ECO:0000244|PDB:3T6Q}.
TURN 242 244 {ECO:0000244|PDB:3T6Q}.
STRAND 246 251 {ECO:0000244|PDB:3T6Q}.
HELIX 265 273 {ECO:0000244|PDB:3T6Q}.
STRAND 274 280 {ECO:0000244|PDB:3T6Q}.
TURN 291 296 {ECO:0000244|PDB:3T6Q}.
STRAND 301 304 {ECO:0000244|PDB:3T6Q}.
STRAND 325 327 {ECO:0000244|PDB:3T6Q}.
HELIX 336 339 {ECO:0000244|PDB:3T6Q}.
HELIX 341 343 {ECO:0000244|PDB:3T6Q}.
STRAND 348 351 {ECO:0000244|PDB:3T6Q}.
TURN 365 368 {ECO:0000244|PDB:3T6Q}.
STRAND 374 376 {ECO:0000244|PDB:3T6Q}.
STRAND 384 388 {ECO:0000244|PDB:3T6Q}.
TURN 389 394 {ECO:0000244|PDB:3T6Q}.
STRAND 400 402 {ECO:0000244|PDB:3T6Q}.
STRAND 409 411 {ECO:0000244|PDB:3T6Q}.
TURN 413 418 {ECO:0000244|PDB:3T6Q}.
STRAND 423 426 {ECO:0000244|PDB:3T6Q}.
TURN 440 443 {ECO:0000244|PDB:3T6Q}.
STRAND 449 451 {ECO:0000244|PDB:3T6Q}.
TURN 462 467 {ECO:0000244|PDB:3T6Q}.
STRAND 473 475 {ECO:0000244|PDB:3T6Q}.
HELIX 482 484 {ECO:0000244|PDB:3T6Q}.
HELIX 491 494 {ECO:0000244|PDB:3T6Q}.
STRAND 500 502 {ECO:0000244|PDB:3T6Q}.
TURN 513 518 {ECO:0000244|PDB:3T6Q}.
STRAND 524 526 {ECO:0000244|PDB:3T6Q}.
HELIX 534 540 {ECO:0000244|PDB:3T6Q}.
STRAND 547 549 {ECO:0000244|PDB:3T6Q}.
HELIX 560 562 {ECO:0000244|PDB:3T6Q}.
HELIX 563 567 {ECO:0000244|PDB:3T6Q}.
STRAND 569 573 {ECO:0000244|PDB:3T6Q}.
HELIX 583 585 {ECO:0000244|PDB:3T6Q}.
HELIX 586 594 {ECO:0000244|PDB:3T6Q}.
HELIX 596 598 {ECO:0000244|PDB:3T6Q}.
HELIX 602 604 {ECO:0000244|PDB:3T6Q}.
STRAND 606 610 {ECO:0000244|PDB:3T6Q}.
HELIX 611 613 {ECO:0000244|PDB:3T6Q}.
HELIX 618 620 {ECO:0000244|PDB:3T6Q}.
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


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