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FCRL1_MOUSE
ID   FCRL1_MOUSE             Reviewed;         343 AA.
AC   Q8R4Y0; Q68SP0; Q7TMH2; Q80WN3; Q8BYS4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Fc receptor-like protein 1;
DE            Short=FcR-like protein 1;
DE            Short=FcRL1;
DE   AltName: Full=BXMAS1-like protein 1;
DE            Short=mBXMH1;
DE   AltName: Full=Fc receptor homolog 1;
DE            Short=FcRH1;
DE            Short=moFcRH1;
DE   AltName: Full=IFGP family protein 1;
DE            Short=mIFGP1;
DE   AltName: CD_antigen=CD307a;
DE   Flags: Precursor;
GN   Name=Fcrl1; Synonyms=Fcrh1, Ifgp1;
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=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=12037601; DOI=10.1007/s00251-002-0436-x;
RA   Guselnikov S.V., Ershova S.A., Mechetina L.V., Najakshin A.M.,
RA   Volkova O.Y., Alabyev B.Y., Taranin A.V.;
RT   "A family of highly diverse human and mouse genes structurally links
RT   leukocyte FcR, gp42 and PECAM-1.";
RL   Immunogenetics 54:87-95(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), 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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus, and 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May function as an activating coreceptor in B-cells. May
CC       function in B-cells activation and differentiation (By similarity).
CC       {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=4;
CC       Name=1; Synonyms=a, long;
CC         IsoId=Q8R4Y0-1; Sequence=Displayed;
CC       Name=2; Synonyms=short;
CC         IsoId=Q8R4Y0-2; Sequence=VSP_033296;
CC       Name=3;
CC         IsoId=Q8R4Y0-3; Sequence=VSP_033299;
CC       Name=4; Synonyms=b;
CC         IsoId=Q8R4Y0-4; Sequence=VSP_033297, VSP_033298;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in B-cells at the
CC       various stages of differentiation. {ECO:0000269|PubMed:12037601,
CC       ECO:0000269|PubMed:15302849}.
CC   -!- PTM: Phosphorylated on tyrosines upon activation. {ECO:0000250}.
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DR   EMBL; AF329485; AAM11542.1; -; mRNA.
DR   EMBL; AY506554; AAS91574.1; -; mRNA.
DR   EMBL; AY506555; AAS91575.1; -; mRNA.
DR   EMBL; AY158088; AAO20871.1; -; mRNA.
DR   EMBL; AY158089; AAO20872.1; -; mRNA.
DR   EMBL; AK038494; BAC30017.1; -; mRNA.
DR   EMBL; AK156985; BAE33923.1; -; mRNA.
DR   EMBL; BC055830; AAH55830.1; -; mRNA.
DR   CCDS; CCDS17452.1; -. [Q8R4Y0-1]
DR   CCDS; CCDS50942.1; -. [Q8R4Y0-2]
DR   CCDS; CCDS79937.1; -. [Q8R4Y0-3]
DR   RefSeq; NP_001129708.1; NM_001136236.1.
DR   RefSeq; NP_001297474.1; NM_001310545.1.
DR   RefSeq; NP_694730.2; NM_153090.2.
DR   RefSeq; NP_835459.1; NM_178165.4.
DR   AlphaFoldDB; Q8R4Y0; -.
DR   SMR; Q8R4Y0; -.
DR   STRING; 10090.ENSMUSP00000130936; -.
DR   GlyGen; Q8R4Y0; 2 sites.
DR   iPTMnet; Q8R4Y0; -.
DR   PhosphoSitePlus; Q8R4Y0; -.
DR   MaxQB; Q8R4Y0; -.
DR   PRIDE; Q8R4Y0; -.
DR   ProteomicsDB; 272978; -. [Q8R4Y0-1]
DR   ProteomicsDB; 272979; -. [Q8R4Y0-2]
DR   ProteomicsDB; 272980; -. [Q8R4Y0-3]
DR   ProteomicsDB; 272981; -. [Q8R4Y0-4]
DR   ABCD; Q8R4Y0; 35 sequenced antibodies.
DR   DNASU; 229499; -.
DR   GeneID; 229499; -.
DR   KEGG; mmu:229499; -.
DR   CTD; 115350; -.
DR   MGI; MGI:2442862; Fcrl1.
DR   eggNOG; ENOG502S65W; Eukaryota.
DR   InParanoid; Q8R4Y0; -.
DR   OrthoDB; 53940at2759; -.
DR   PhylomeDB; Q8R4Y0; -.
DR   BioGRID-ORCS; 229499; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Fcrla; mouse.
DR   PRO; PR:Q8R4Y0; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8R4Y0; protein.
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:0015026; F:coreceptor activity; ISO:MGI.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0042113; P:B cell activation; ISO:MGI.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 2.
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   Pfam; PF13895; Ig_2; 1.
DR   SMART; SM00409; IG; 2.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   2: Evidence at transcript 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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..343
FT                   /note="Fc receptor-like protein 1"
FT                   /id="PRO_0000331639"
FT   TOPO_DOM        17..219
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          17..109
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          117..200
FT                   /note="Ig-like C2-type 2"
FT   REGION          251..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           266..271
FT                   /note="ITIM motif 1"
FT   MOTIF           279..284
FT                   /note="ITIM motif 2"
FT   MOTIF           291..296
FT                   /note="ITIM motif 3"
FT   MOTIF           325..330
FT                   /note="ITIM motif 4"
FT   MOTIF           337..342
FT                   /note="ITIM motif 5"
FT   COMPBIAS        254..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        138..185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         205..247
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15302849,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_033296"
FT   VAR_SEQ         206..208
FT                   /note="LSL -> KPT (in isoform 4)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_033297"
FT   VAR_SEQ         209..343
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_033298"
FT   VAR_SEQ         319..343
FT                   /note="SFQVSSGLYSKPRINIAHMDYEDAM -> VQGGIA (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033299"
FT   CONFLICT        102
FT                   /note="A -> P (in Ref. 4; BAC30017)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232
FT                   /note="P -> L (in Ref. 4; BAC30017)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="S -> P (in Ref. 4; BAC30017)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   343 AA;  37277 MW;  F4F235954A907B6C CRC64;
     MLPWLLLLIC ALPCEPAGIS DVSLKTRPPG GWVMEGDKLV LICSVDRVTG NITYFWYRGA
     LGFQLETKTQ PSLTAEFEIS DMKQSDADQY YCAANDGHDP IASELVSIHV RVPVSRPVLT
     FGDSGTQAVL GDLVELHCKA LRGSPPIFYQ FYHESIILGN SSAPSGGGAS FNFSLTAEHS
     GNFSCEASNG QGAQRSEVVA LNLTGLSLVP TENGISHLSL GLTGWLLGCL SPITMALIFC
     YWLKRKIGRQ SEDPVRSPPQ TVLQGSTYPK SPDSRQPEPL YENVNVVSGN EVYSLVYHTP
     QVLEPAAAQH VRTHGVSESF QVSSGLYSKP RINIAHMDYE DAM
 
 
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