FCRL5_MOUSE
ID FCRL5_MOUSE Reviewed; 596 AA.
AC Q68SN8; E9QLI5; Q80WN2; Q8BJA5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Fc receptor-like protein 5;
DE Short=FcR-like protein 5;
DE Short=FcRL5;
DE AltName: Full=BXMAS1-like protein 2;
DE Short=mBXMH2;
DE AltName: Full=Fc receptor homolog 3;
DE Short=FcRH3;
DE Short=moFcRH3;
DE AltName: CD_antigen=CD307e;
DE Flags: Precursor;
GN Name=Fcrl5; Synonyms=Fcrh3;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=15302849; DOI=10.1093/intimm/dxh137;
RA Davis R.S., Stephan R.P., Chen C.-C., Dennis G. Jr., Cooper M.D.;
RT "Differential B cell expression of mouse Fc receptor homologs.";
RL Int. Immunol. 16:1343-1353(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Nakayama Y., Maher S.E., Weissman S.M., Bothwell A.L.M.;
RT "Molecular cloning of mouse BXMAS1 homologs; homologous to IgFc receptor.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=NOD; TISSUE=Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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).
CC -!- SUBUNIT: Interacts with PTPN6, PTPN11, SYK and ZAP70. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q68SN8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68SN8-2; Sequence=VSP_033309;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in marginal zone B cells.
CC {ECO:0000269|PubMed:15302849}.
CC -!- PTM: Phosphorylated on cytoplasmic tyrosines; required for interaction
CC with protein tyrosine phosphatases and protein tyrosine kinases.
CC {ECO:0000250}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-14 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO20873.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY506558; AAS91578.1; -; mRNA.
DR EMBL; AY158090; AAO20873.1; ALT_INIT; mRNA.
DR EMBL; AK089756; BAC40954.1; -; mRNA.
DR EMBL; AC163618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS50943.1; -. [Q68SN8-1]
DR CCDS; CCDS50944.1; -. [Q68SN8-2]
DR RefSeq; NP_001106709.1; NM_001113238.1. [Q68SN8-2]
DR RefSeq; NP_899045.3; NM_183222.3. [Q68SN8-1]
DR AlphaFoldDB; Q68SN8; -.
DR SMR; Q68SN8; -.
DR DIP; DIP-60955N; -.
DR IntAct; Q68SN8; 1.
DR STRING; 10090.ENSMUSP00000050151; -.
DR GlyGen; Q68SN8; 2 sites.
DR PhosphoSitePlus; Q68SN8; -.
DR PaxDb; Q68SN8; -.
DR PRIDE; Q68SN8; -.
DR ProteomicsDB; 271685; -. [Q68SN8-1]
DR ProteomicsDB; 271686; -. [Q68SN8-2]
DR Antibodypedia; 47044; 223 antibodies from 30 providers.
DR DNASU; 329693; -.
DR Ensembl; ENSMUST00000049926; ENSMUSP00000050151; ENSMUSG00000048031. [Q68SN8-1]
DR Ensembl; ENSMUST00000166297; ENSMUSP00000131176; ENSMUSG00000048031. [Q68SN8-2]
DR Ensembl; ENSMUST00000193229; ENSMUSP00000141311; ENSMUSG00000048031. [Q68SN8-2]
DR Ensembl; ENSMUST00000194102; ENSMUSP00000142210; ENSMUSG00000048031. [Q68SN8-1]
DR GeneID; 329693; -.
DR KEGG; mmu:329693; -.
DR UCSC; uc008psf.1; mouse. [Q68SN8-2]
DR UCSC; uc012crg.1; mouse. [Q68SN8-1]
DR CTD; 83416; -.
DR MGI; MGI:3053558; Fcrl5.
DR VEuPathDB; HostDB:ENSMUSG00000048031; -.
DR eggNOG; ENOG502S65W; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_023383_6_1_1; -.
DR InParanoid; Q68SN8; -.
DR OMA; LPQKTKW; -.
DR OrthoDB; 53940at2759; -.
DR BioGRID-ORCS; 329693; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q68SN8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q68SN8; protein.
DR Bgee; ENSMUSG00000048031; Expressed in spleen and 5 other tissues.
DR ExpressionAtlas; Q68SN8; baseline and differential.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
DR GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; IDA:MGI.
DR GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; IDA:MGI.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:MGI.
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 Pfam; PF13895; Ig_2; 3.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..596
FT /note="Fc receptor-like protein 5"
FT /id="PRO_0000331641"
FT TOPO_DOM 27..496
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..115
FT /note="Ig-like C2-type 1"
FT DOMAIN 106..199
FT /note="Ig-like C2-type 2"
FT DOMAIN 207..294
FT /note="Ig-like C2-type 3"
FT DOMAIN 296..384
FT /note="Ig-like C2-type 4"
FT DOMAIN 398..483
FT /note="Ig-like C2-type 5"
FT REGION 522..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 137..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 228..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 325..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 419..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 29..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033309"
FT CONFLICT 161..163
FT /note="PQS -> HQ (in Ref. 1; AAS91578 and 2; AAO20873)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="F -> L (in Ref. 3; BAC40954)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="Y -> S (in Ref. 1; AAS91578 and 2; AAO20873)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="R -> H (in Ref. 3; BAC40954)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="V -> R (in Ref. 1; AAS91578 and 2; AAO20873)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="K -> R (in Ref. 1; AAS91578 and 2; AAO20873)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="S -> R (in Ref. 1; AAS91578, 2; AAO20873 and 3;
FT BAC40954)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="K -> E (in Ref. 1; AAS91578 and 2; AAO20873)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="Y -> H (in Ref. 1; AAS91578 and 2; AAO20873)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="C -> R (in Ref. 3; BAC40954)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="N -> T (in Ref. 1; AAS91578, 2; AAO20873 and 3;
FT BAC40954)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 66779 MW; 3EF9C7E4728461B4 CRC64;
MSGSFSPCVV FTQMWLTLLV VTPVNGQHEA AQQSVVSLQP PWTTFFRGEV VTLTCYRFGF
SVPQKTKWYQ KRKTVKQTPG ALVIKAHTLK VHESGEYWCQ ADSLLPSMHV NVEFSEDFLV
LQAPPAVFEG DSVVLRCYAK KGIEAETLTF YKDGKALTLH PQSSEFYIHR ANLKDNGQYK
CTSKKKWSFG SLYTSNTVVV QVQELFPRPV LRARPSHPID GSPVTLTCQT QLSAQKSDAR
LQFCFFRNLQ LLGSGCSRSS EFHIPAIWTE ESKRYQCKAE TVNSQVSKQS TAFIIPVQRA
SARFQTHIIP ASKLVFEGQL LLLNCSVKGV PGPLKFSWYK KDMLNKETKI LKSSNAEFKI
SQVNISDAGE YYCEANNSRR SFVSRAFPIT IKVPVSQPVL TLSTGKTQAL EGDLMTLHCQ
SQRGSPCILY EFFYENVSLG NSSILSGGGA YFNFSMSTER SGNYYCTADN GLGAQCSEAI
RISIFDMTKN RSVPMAAGIT VGLLIMAVGV FLFYCWFSRK AGGKPTSDDS RNPSDSEPQE
PTYYNVPACI ELQPVYSNEP EENVIYTEVR RTQPRQKHAD QESESPRSRC QMAEKK
