LRB3B_RAT
ID LRB3B_RAT Reviewed; 744 AA.
AC C0HJX3;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 3B {ECO:0000312|RGD:1589827};
DE Flags: Precursor;
GN Name=Lilrb3b {ECO:0000312|RGD:1589827};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000303|PubMed:15057822};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000303|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
CC -!- FUNCTION: May act as receptor for class I MHC antigens. Becomes
CC activated upon coligation of LILRB3 and immune receptors, such as
CC FCGR2B and the B-cell receptor. Down-regulates antigen-induced B-cell
CC activation by recruiting phosphatases to its immunoreceptor tyrosine-
CC based inhibitor motifs (ITIM). {ECO:0000250|UniProtKB:P97484}.
CC -!- SUBUNIT: Interacts with LYN, PTPN6/SHP-1 and PTPN11/SHP-2.
CC {ECO:0000250|UniProtKB:P97484}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P97484};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: Contains 3 copies of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases,
CC including PTPN6/SHP-1, resulting in the dephosphorylation of the
CC downstream protein kinases SYK and BTK. {ECO:0000250|UniProtKB:P97484}.
CC -!- PTM: Phosphorylated on tyrosine residues by LYN. Phosphorylation at
CC Tyr-697 and Tyr-727 is important for interaction with PTPN6/SHP-1 and
CC PTPN11/SHP-2. {ECO:0000250|UniProtKB:P97484}.
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DR EMBL; AABR07071870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001300853.1; NM_001313924.1.
DR RefSeq; NP_001300877.1; NM_001313948.1.
DR AlphaFoldDB; C0HJX3; -.
DR SMR; C0HJX3; -.
DR GlyGen; C0HJX3; 3 sites.
DR Ensembl; ENSRNOT00000077327; ENSRNOP00000071172; ENSRNOG00000058422.
DR GeneID; 683463; -.
DR GeneID; 690955; -.
DR KEGG; rno:683463; -.
DR CTD; 18733; -.
DR CTD; 683463; -.
DR RGD; 1589827; Lilrb3b.
DR OrthoDB; 1000446at2759; -.
DR PRO; PR:C0HJX3; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR GO; GO:0032396; F:inhibitory MHC class I receptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0001782; P:B cell homeostasis; ISO:RGD.
DR GO; GO:0019724; P:B cell mediated immunity; ISO:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; ISO:RGD.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISO:RGD.
DR GO; GO:0051248; P:negative regulation of protein metabolic process; ISO:RGD.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; ISO:RGD.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:RGD.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 2.
DR Pfam; PF13895; Ig_2; 2.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 3: Inferred from homology;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..744
FT /note="Leukocyte immunoglobulin-like receptor subfamily B
FT member 3B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435466"
FT TOPO_DOM 25..543
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..744
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..119
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 121..221
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 223..316
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 320..419
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 426..520
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255"
FT REGION 572..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 615..620
FT /note="ITIM motif 1"
FT /evidence="ECO:0000305"
FT MOTIF 695..700
FT /note="ITIM motif 2"
FT /evidence="ECO:0000305"
FT MOTIF 725..730
FT /note="ITIM motif 3"
FT /evidence="ECO:0000305"
FT COMPBIAS 689..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 697
FT /note="Phosphotyrosine; by LYN"
FT /evidence="ECO:0000250|UniProtKB:P97484"
FT MOD_RES 727
FT /note="Phosphotyrosine; by LYN"
FT /evidence="ECO:0000250|UniProtKB:P97484"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..98
FT /evidence="ECO:0000305"
FT DISULFID 144..197
FT /evidence="ECO:0000305"
FT DISULFID 246..295
FT /evidence="ECO:0000305"
FT DISULFID 343..395
FT /evidence="ECO:0000305"
FT DISULFID 445..496
FT /evidence="ECO:0000305"
SQ SEQUENCE 744 AA; 82704 MW; BDD6C8DF455D1F26 CRC64;
MTFTFTALLC LGLTLGLWIP VLTGSLPKPI LRVQPDSVVS MGTTVTFICE ETIGAKQSYL
YRNGNLQRRV PKNNQKPTNK TEFLFLNVGH QNAGQYHCSY KSQGKSSDYS EPLELVVTGA
YSKPSLSAQT NPVVTSGGYV TLKCEPSHYG HTLILTVEGP QKLSWRQDPQ CNYYTENCHV
LFYVGPLTSN QRWIFRCYSY ETNTPQVWSA PSEPVEILVS GKLQKPTIKA EPGSVIHSGK
AMIIWCQGDL DAEIYFLHKE GSHNTQSTQT LQQPGNKAKL FIRPVTQGHA GDYRCYYYSS
AGWSEPSDTL ELVVTGIYNY HPLMLSGPPS PVVPEGGNVT LHCTSHRYYD KFILIKEDQK
FSSSLDTKYI SSTGQHQALF VMGPMTPNYS GTFRCYGYYK HTPQLWSEPS NLLKILITGQ
LHHVLFLSVM PNSTVHSGEN VTLMCWSTYS VDTFILSKEG SGQPPLRLKS KIQDQQYQSE
FSMSGVTSKL SGTYRCYGSH DSSLYLLSFA SAPVELIVSG PIRTSDLPPT MSIPPDGLQR
YLKALIGVSV AFLLFLFILI FILLRRRHQE KFRKDDEDAQ KGKELQLSTG AAEPVTRDRG
HQKRSNPAAA TQEESLYASV EDMETKDGVE LDTWKPPEGD PQGETYAQVE PSRLRRAGAI
SPVVSREQLN TKYEQAEEGQ EVDSQATESE EPQDVTYAQL CSRTLRQGTA APPLSQAGEA
PEEPSVYAAL ATARPGAVPK NKKQ
