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Complement component receptor 1-like protein (Complement regulatory protein Crry) (Protein p65)

 CR1L_MOUSE              Reviewed;         483 AA.
Q64735; E9QL18; Q3TV30; Q58E68; Q61447; Q61449; Q8CF59; Q8K328;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 135.
RecName: Full=Complement component receptor 1-like protein;
AltName: Full=Complement regulatory protein Crry;
AltName: Full=Protein p65;
Flags: Precursor;
Name=Cr1l; Synonyms=Crry, Cry;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
1 AND 2).
STRAIN=BALB/cJ;
PubMed=2307848;
Paul M.S., Aegerter-Shaw M., Cepek K., Miller M.D., Weis J.H.;
"The murine complement receptor gene family: III. The genomic and
transcriptional complexity of the Crry and Crry-ps genes.";
J. Immunol. 144:1988-1996(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 64-437 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Pancreas;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=Czech II; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-477 (ISOFORM 2), NUCLEOTIDE SEQUENCE
[MRNA] OF 12-167 (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Liver, and Spleen;
PubMed=2911011;
Paul M.S., Aegerter-Shaw M., O'Brien S.E., Kurtz C.B., Weis J.H.;
"The murine complement receptor gene family analysis of mCRY gene
products and their homology to human CR1.";
J. Immunol. 142:582-589(1989).
[6]
FUNCTION.
PubMed=1730912; DOI=10.1084/jem.175.1.121;
Molina H., Wong W., Kinoshita T., Brenner C., Foley S., Holers V.M.;
"Distinct receptor and regulatory properties of recombinant mouse
complement receptor 1 (CR1) and Crry, the two genetic homologues of
human CR1.";
J. Exp. Med. 175:121-129(1992).
[7]
TISSUE SPECIFICITY.
PubMed=7691944;
Li B., Sallee C., Dehoff M., Foley S., Molina H., Holers V.M.;
"Mouse Crry/p65. Characterization of monoclonal antibodies and the
tissue distribution of a functional homologue of human MCP and DAF.";
J. Immunol. 151:4295-4305(1993).
[8]
FUNCTION.
PubMed=7528766; DOI=10.1084/jem.181.1.151;
Kim Y.-U., Kinoshita T., Molina H., Hourcade D., Seya T., Wagner L.M.,
Holers V.M.;
"Mouse complement regulatory protein Crry/p65 uses the specific
mechanisms of both human decay-accelerating factor and membrane
cofactor protein.";
J. Exp. Med. 181:151-159(1995).
[9]
FUNCTION.
PubMed=10779754; DOI=10.4049/jimmunol.164.9.4533;
Fernandez-Centeno E., de Ojeda G., Rojo J.M., Portoles P.;
"Crry/p65, a membrane complement regulatory protein, has costimulatory
properties on mouse T cells.";
J. Immunol. 164:4533-4542(2000).
[10]
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=10642554; DOI=10.1126/science.287.5452.498;
Xu C., Mao D., Holers V.M., Palanca B., Cheng A.M., Molina H.;
"A critical role for murine complement regulator crry in fetomaternal
tolerance.";
Science 287:498-501(2000).
[11]
FUNCTION.
PubMed=11986227; DOI=10.1182/blood.V99.10.3707;
Miwa T., Zhou L., Hilliard B., Molina H., Song W.-C.;
"Crry, but not CD59 and DAF, is indispensable for murine erythrocyte
protection in vivo from spontaneous complement attack.";
Blood 99:3707-3716(2002).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460; THR-463 AND
SER-477, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454; SER-460; SER-468
AND SER-477, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Liver, Lung, Pancreas, and 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).
[15]
3D-STRUCTURE MODELING OF 84-401.
PubMed=12767833; DOI=10.1016/S0022-2836(03)00492-3;
Aslam M., Guthridge J.M., Hack B.K., Quigg R.J., Holers V.M.,
Perkins S.J.;
"The extended multidomain solution structures of the complement
protein Crry and its chimeric conjugate Crry-Ig by scattering,
analytical ultracentrifugation and constrained modelling: implications
for function and therapy.";
J. Mol. Biol. 329:525-550(2003).
-!- FUNCTION: Acts as a cofactor for complement factor I, a serine
protease which protects autologous cells against complement-
mediated injury by cleaving C3b and C4b deposited on host tissue.
Also acts as a decay-accelerating factor, preventing the formation
of C4b2a and C3bBb, the amplification convertases of the
complement cascade. Plays a crucial role in early embryonic
development by maintaining fetomaternal tolerance. Also acts as a
costimulatory factor for T-cells which favors IL-4 secretion.
{ECO:0000269|PubMed:10642554, ECO:0000269|PubMed:10779754,
ECO:0000269|PubMed:11986227, ECO:0000269|PubMed:1730912,
ECO:0000269|PubMed:7528766}.
-!- SUBUNIT: Interacts with C3b. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q64735-1; Sequence=Displayed;
Name=2;
IsoId=Q64735-2; Sequence=VSP_019050;
-!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
{ECO:0000269|PubMed:2911011, ECO:0000269|PubMed:7691944}.
-!- DEVELOPMENTAL STAGE: Highly expressed in trophoblasts at 7.5 dpc,
and in the maternally derived decidual tissues until 16 dpc.
Expressed only at low levels in the embryo itself.
{ECO:0000269|PubMed:10642554}.
-!- DISRUPTION PHENOTYPE: Death between 9.5 and 13.5 dpc from
developmental arrest. {ECO:0000269|PubMed:10642554}.
-!- SIMILARITY: Belongs to the receptors of complement activation
(RCA) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA37477.1; Type=Frameshift; Positions=200; Evidence={ECO:0000305};
Sequence=BAC25098.1; Type=Frameshift; Positions=152; Evidence={ECO:0000305};
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EMBL; M34173; AAA37467.1; -; Genomic_DNA.
EMBL; M34164; AAA37467.1; JOINED; Genomic_DNA.
EMBL; M34165; AAA37467.1; JOINED; Genomic_DNA.
EMBL; M34166; AAA37467.1; JOINED; Genomic_DNA.
EMBL; M34167; AAA37467.1; JOINED; Genomic_DNA.
EMBL; M34168; AAA37467.1; JOINED; Genomic_DNA.
EMBL; M34169; AAA37467.1; JOINED; Genomic_DNA.
EMBL; M34170; AAA37467.1; JOINED; Genomic_DNA.
EMBL; M34171; AAA37467.1; JOINED; Genomic_DNA.
EMBL; M34172; AAA37467.1; JOINED; Genomic_DNA.
EMBL; M34173; AAA37468.1; -; Genomic_DNA.
EMBL; M34164; AAA37468.1; JOINED; Genomic_DNA.
EMBL; M34165; AAA37468.1; JOINED; Genomic_DNA.
EMBL; M34166; AAA37468.1; JOINED; Genomic_DNA.
EMBL; M34167; AAA37468.1; JOINED; Genomic_DNA.
EMBL; M34168; AAA37468.1; JOINED; Genomic_DNA.
EMBL; M34169; AAA37468.1; JOINED; Genomic_DNA.
EMBL; M34170; AAA37468.1; JOINED; Genomic_DNA.
EMBL; M34171; AAA37468.1; JOINED; Genomic_DNA.
EMBL; M34172; AAA37468.1; JOINED; Genomic_DNA.
EMBL; AK004825; BAC25098.1; ALT_FRAME; mRNA.
EMBL; AK160440; BAE35790.1; -; mRNA.
EMBL; AC139206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC028945; AAH28945.1; -; mRNA.
EMBL; BC092048; AAH92048.1; -; mRNA.
EMBL; M23529; AAA37477.1; ALT_FRAME; mRNA.
EMBL; M23446; AAA37478.1; -; mRNA.
CCDS; CCDS15641.1; -. [Q64735-2]
PIR; A43519; A43519.
PIR; B30550; B30550.
PIR; I55975; I55975.
RefSeq; NP_038527.2; NM_013499.2. [Q64735-2]
UniGene; Mm.301652; -.
PDB; 1NTL; X-ray; 30.00 A; A/B=83-401.
PDBsum; 1NTL; -.
ProteinModelPortal; Q64735; -.
SMR; Q64735; -.
IntAct; Q64735; 1.
MINT; Q64735; -.
iPTMnet; Q64735; -.
PhosphoSitePlus; Q64735; -.
PeptideAtlas; Q64735; -.
PRIDE; Q64735; -.
Ensembl; ENSMUST00000075451; ENSMUSP00000074902; ENSMUSG00000016481. [Q64735-2]
GeneID; 12946; -.
KEGG; mmu:12946; -.
UCSC; uc007eeu.1; mouse. [Q64735-1]
UCSC; uc007eev.1; mouse. [Q64735-2]
CTD; 1379; -.
MGI; MGI:88513; Cr1l.
GeneTree; ENSGT00760000118803; -.
HOVERGEN; HBG081346; -.
InParanoid; Q64735; -.
KO; K04005; -.
OMA; RITYACG; -.
OrthoDB; EOG091G0A1X; -.
PhylomeDB; Q64735; -.
TreeFam; TF334137; -.
ChiTaRS; Cr1l; mouse.
EvolutionaryTrace; Q64735; -.
PRO; PR:Q64735; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000016481; Expressed in 278 organ(s), highest expression level in aortic valve.
CleanEx; MM_CR1L; -.
ExpressionAtlas; Q64735; baseline and differential.
Genevisible; Q64735; MM.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0007565; P:female pregnancy; IEA:UniProtKB-KW.
GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0045916; P:negative regulation of complement activation; IMP:MGI.
GO; GO:0030449; P:regulation of complement activation; IMP:MGI.
CDD; cd00033; CCP; 5.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00084; Sushi; 5.
SMART; SM00032; CCP; 5.
SUPFAM; SSF57535; SSF57535; 5.
PROSITE; PS50923; SUSHI; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complement pathway;
Complete proteome; Developmental protein; Disulfide bond;
Glycoprotein; Immunity; Innate immunity; Membrane; Phosphoprotein;
Pregnancy; Receptor; Reference proteome; Repeat; Signal; Sushi;
Transmembrane; Transmembrane helix.
SIGNAL 1 40 {ECO:0000255}.
CHAIN 41 483 Complement component receptor 1-like
protein.
/FTId=PRO_0000238978.
TOPO_DOM 41 405 Extracellular. {ECO:0000255}.
TRANSMEM 406 426 Helical. {ECO:0000255}.
TOPO_DOM 427 483 Cytoplasmic. {ECO:0000255}.
DOMAIN 83 143 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 144 205 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 206 276 Sushi 3. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 278 338 Sushi 4. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 340 400 Sushi 5. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 463 463 Phosphothreonine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 468 468 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 477 477 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 85 128 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 115 141 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 146 187 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 173 203 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 208 257 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 237 274 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 280 323 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 309 336 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 342 385 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 371 398 {ECO:0000255|PROSITE-ProRule:PRU00302}.
VAR_SEQ 40 82 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:2911011}.
/FTId=VSP_019050.
CONFLICT 21 21 G -> A (in Ref. 5; AAA37477).
{ECO:0000305}.
CONFLICT 28 28 E -> A (in Ref. 4; AAH92048).
{ECO:0000305}.
CONFLICT 64 67 ADSK -> GRLQ (in Ref. 2; BAE35790).
{ECO:0000305}.
CONFLICT 67 67 Missing (in Ref. 3; AC139206).
{ECO:0000305}.
CONFLICT 112 112 L -> M (in Ref. 4; AAH92048).
{ECO:0000305}.
CONFLICT 164 164 Q -> E (in Ref. 5; AAA37477).
{ECO:0000305}.
CONFLICT 182 182 S -> P (in Ref. 4; AAH92048).
{ECO:0000305}.
CONFLICT 240 240 D -> N (in Ref. 4; AAH92048).
{ECO:0000305}.
CONFLICT 435 437 NTT -> TRF (in Ref. 2; BAE35790).
{ECO:0000305}.
SEQUENCE 483 AA; 53763 MW; 259BFFED4CE547C1 CRC64;
MEVSSRSSEP LDPVWLLVAF GRGGVKLEVL LLFLLPFTLG ELRGGLGKHG HTVHREPAVN
RLCADSKRWS GLPVSAQRPF PMGHCPAPSQ LPSAKPINLT DESMFPIGTY LLYECLPGYI
KRQFSITCKQ DSTWTSAEDK CIRKQCKTPS DPENGLVHVH TGIQFGSRIN YTCNQGYRLI
GSSSAVCVIT DQSVDWDTEA PICEWIPCEI PPGIPNGDFF SSTREDFHYG MVVTYRCNTD
ARGKALFNLV GEPSLYCTSN DGEIGVWSGP PPQCIELNKC TPPPYVENAV MLSENRSLFS
LRDIVEFRCH PGFIMKGASS VHCQSLNKWE PELPSCFKGV ICRLPQEMSG FQKGLGMKKE
YYYGENVTLE CEDGYTLEGS SQSQCQSDGS WNPLLAKCVS RSISGLIVGI FIGIIVFILV
IIVFIWMILK YKKRNTTDEK YKEVGIHLNY KEDSCVRLQS LLTSQENSST TSPARNSLTQ
EVS


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