CR2_MOUSE
ID CR2_MOUSE Reviewed; 1025 AA.
AC P19070;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Complement receptor type 2;
DE Short=Cr2;
DE AltName: Full=Complement C3d receptor;
DE AltName: CD_antigen=CD21;
DE Flags: Precursor;
GN Name=Cr2;
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].
RC STRAIN=BALB/cJ;
RX PubMed=2139457;
RA Fingeroth J.D.;
RT "Comparative structure and evolution of murine CR2. The homolog of the
RT human C3d/EBV receptor (CD21).";
RL J. Immunol. 144:3458-3467(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-1025.
RX PubMed=2145366;
RA Molina H., Kinoshita T., Inoue K., Carel J.-C., Holers V.M.;
RT "A molecular and immunochemical characterization of mouse CR2. Evidence for
RT a single gene model of mouse complement receptors 1 and 2.";
RL J. Immunol. 145:2974-2983(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 343-401 AND 991-1025.
RX PubMed=2783485; DOI=10.1073/pnas.86.1.242;
RA Fingeroth J.D., Benedict M.A., Levy D.N., Strominger J.L.;
RT "Identification of murine complement receptor type 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:242-246(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 289-1025.
RX PubMed=2528587;
RA Kurtz C.B., Paul M.S., Aegerter M., Weis J.J., Weis J.H.;
RT "Murine complement receptor gene family. II. Identification and
RT characterization of the murine homolog (Cr2) to human CR2 and its molecular
RT linkage to Crry.";
RL J. Immunol. 143:2058-2067(1989).
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 -!- FUNCTION: Receptor for complement C3d and for HNRNPU. Participates in B
CC lymphocytes activation. {ECO:0000250|UniProtKB:P20023}.
CC -!- SUBUNIT: Interacts (via Sushi domain 1 and 2) with C3. Interacts with
CC CD19. Part of a complex composed of CD19, CR2/CD21, CD81 and
CC IFITM1/CD225 in the membrane of mature B-cells.
CC {ECO:0000250|UniProtKB:P20023}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20023};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P20023}.
CC -!- TISSUE SPECIFICITY: B-lymphocytes.
CC -!- SIMILARITY: Belongs to the receptors of complement activation (RCA)
CC family. {ECO:0000305}.
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DR EMBL; M81083; AAA37451.1; -; mRNA.
DR EMBL; M35684; AAA37448.1; -; mRNA.
DR EMBL; M61132; AAA63295.1; -; mRNA.
DR EMBL; M35685; AAA37450.1; ALT_SEQ; mRNA.
DR EMBL; M29281; AAA37447.1; -; mRNA.
DR PIR; A43526; A43526.
DR AlphaFoldDB; P19070; -.
DR SMR; P19070; -.
DR STRING; 10090.ENSMUSP00000080938; -.
DR GlyGen; P19070; 17 sites.
DR PhosphoSitePlus; P19070; -.
DR MaxQB; P19070; -.
DR PaxDb; P19070; -.
DR PeptideAtlas; P19070; -.
DR PRIDE; P19070; -.
DR ProteomicsDB; 278028; -.
DR ABCD; P19070; 1 sequenced antibody.
DR UCSC; uc007eey.1; mouse.
DR MGI; MGI:88489; Cr2.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P19070; -.
DR PhylomeDB; P19070; -.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR PRO; PR:P19070; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P19070; protein.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0001848; F:complement binding; ISO:MGI.
DR GO; GO:0004875; F:complement receptor activity; IMP:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0030183; P:B cell differentiation; ISO:MGI.
DR GO; GO:0042100; P:B cell proliferation; ISO:MGI.
DR GO; GO:0006957; P:complement activation, alternative pathway; ISO:MGI.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IBA:GO_Central.
DR CDD; cd00033; CCP; 13.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 13.
DR SMART; SM00032; CCP; 14.
DR SUPFAM; SSF57535; SSF57535; 15.
DR PROSITE; PS50923; SUSHI; 15.
PE 1: Evidence at protein level;
KW Cell membrane; Complement pathway; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW Sushi; Transmembrane; Transmembrane helix.
FT SIGNAL 1..11
FT CHAIN 12..1025
FT /note="Complement receptor type 2"
FT /id="PRO_0000006011"
FT TOPO_DOM 12..963
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 964..990
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 991..1025
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 12..75
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 80..140
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 144..204
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 205..265
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 266..336
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 341..400
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 401..460
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 461..516
FT /note="Sushi 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 517..587
FT /note="Sushi 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 592..651
FT /note="Sushi 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 652..706
FT /note="Sushi 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 707..771
FT /note="Sushi 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 776..835
FT /note="Sushi 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 839..899
FT /note="Sushi 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 900..960
FT /note="Sushi 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 694
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 851
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 901
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 14..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 42..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 82..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 110..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 146..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 175..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 207..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 234..263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 268..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 297..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 343..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 371..398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 402..445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 431..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 463..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 487..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 519..568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 548..585
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 594..636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 622..649
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 654..689
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 675..704
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 709..752
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 738..769
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 778..820
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 806..833
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 841..884
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 870..897
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 902..945
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 931..958
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CONFLICT 289..291
FT /note="YGS -> EFR (in Ref. 4; AAA37447)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="S -> T (in Ref. 2; AAA63295)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="P -> A (in Ref. 2; AAA63295)"
FT /evidence="ECO:0000305"
FT CONFLICT 962..963
FT /note="Missing (in Ref. 4; AAA37447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1025 AA; 112995 MW; 19E518B9A0273694 CRC64;
MLTWFLFYFS EISCDPPPEV KNARKPYYSL PIVPGTVLRY TCSPSYRLIG EKAIFCISEN
QVHATWDKAP PICESVNKTI SCSDPIVPGG FMNKGSKAPF RHGDSVTFTC KANFTMKGSK
TVWCQANEMW GPTALPVCES DFPLECPSLP TIHNGHHTGQ HVDQFVAGLS VTYSCEPGYL
LTGKKTIKCL SSGDWDGVIP TCKEAQCEHP GKFPNGQVKE PLSLQVGTTV YFSCNEGYQL
QGQPSSQCVI VEQKAIWTKK PVCKEILCPP PPPVRNGSHT GSFSENVPYG STVTYTCDPS
PEKGVSFTLI GEKTINCTTG SQKTGIWSGP APYCVLSTSA VLCLQPKIKR GQILSILKDS
YSYNDTVAFS CEPGFTLKGN RSIRCNAHGT WEPPVPVCEK GCQAPPKIIN GQKEDSYLLN
FDPGTSIRYS CDPGYLLVGE DTIHCTPEGK WTPITPQCTV AECKPVGPHL FKRPQNQFIR
TAVNSSCDEG FQLSESAYQL CQGTIPWFIE IRLCKEITCP PPPVIHNGTH TWSSSEDVPY
GTVVTYMCYP GPEEGVKFKL IGEQTIHCTS DSRGRGSWSS PAPLCKLSLP AVQCTDVHVE
NGVKLTDNKA PYFYNDSVMF KCDDGYILSG SSQIRCKANN TWDPEKPLCK KEGCEPMRVH
GLPDDSHIKL VKRTCQNGYQ LTGYTYEKCQ NAENGTWFKK IEVCTVILCQ PPPKIANGGH
TGMMAKHFLY GNEVSYECDE GFYLLGEKSL QCVNDSKGHG SWSGPPPQCL QSSPLTHCPD
PEVKHGYKLN KTHSAFSHND IVHFVCNQGF IMNGSHLIRC HTNNTWLPGV PTCIRKASLG
CQSPSTIPNG NHTGGSIARF PPGMSVMYSC YQGFLMAGEA RLICTHEGTW SQPPPFCKEV
NCSFPEDTNG IQKGFQPGKT YRFGATVTLE CEDGYTLEGS PQSQCQDDSQ WNPPLALCKY
RRWSTIPLIC GISVGSALII LMSVGFCMIL KHRESNYYTK TRPKEGALHL ETREVYSIDP
YNPAS
