CR1L_RAT
ID CR1L_RAT Reviewed; 559 AA.
AC Q63135; Q63612;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Complement component receptor 1-like protein;
DE AltName: Full=Antigen 5I2;
DE AltName: Full=Complement regulatory protein Crry;
DE Flags: Precursor;
GN Name=Cr1l; Synonyms=Crry;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Liver;
RX PubMed=8117286; DOI=10.1006/bbrc.1994.1117;
RA Sakurada C., Seno H., Dohi N., Takizawa H., Nonaka M., Okada N., Okada H.;
RT "Molecular cloning of the rat complement regulatory protein, 5I2 antigen.";
RL Biochem. Biophys. Res. Commun. 198:819-826(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley;
RX PubMed=7590969; DOI=10.1007/bf00179397;
RA Quigg R.J., Lo C.F., Alexander J.J., Sneed A.E. III, Moxley G.;
RT "Molecular characterization of rat Crry: widespread distribution of two
RT alternative forms of Crry mRNA.";
RL Immunogenetics 42:362-367(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
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).
RN [4]
RP PROTEIN SEQUENCE OF 39-53; 66-74; 369-373 AND 520-528 (ISOFORM 1),
RP INTERACTION WITH C3B, AND FUNCTION.
RX PubMed=8144902;
RA Takizawa H., Okada N., Okada H.;
RT "Complement inhibitor of rat cell membrane resembling mouse Crry/p65.";
RL J. Immunol. 152:3032-3038(1994).
RN [5]
RP FUNCTION.
RX PubMed=7534798;
RA Quigg R.J., Holers V.M., Morgan B.P., Sneed A.E. III;
RT "Crry and CD59 regulate complement in rat glomerular epithelial cells and
RT are inhibited by the nephritogenic antibody of passive Heymann nephritis.";
RL J. Immunol. 154:3437-3443(1995).
RN [6]
RP FUNCTION.
RX PubMed=15474557; DOI=10.1016/j.lfs.2004.06.007;
RA Antic Stankovic J., Vucevic D., Majstorovic I., Vasilijic S., Colic M.;
RT "The role of rat Crry, a complement regulatory protein, in proliferation of
RT thymocytes.";
RL Life Sci. 75:3053-3062(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-554, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [8]
RP 3D-STRUCTURE MODELING OF 34-353.
RX PubMed=12767833; DOI=10.1016/s0022-2836(03)00492-3;
RA Aslam M., Guthridge J.M., Hack B.K., Quigg R.J., Holers V.M., Perkins S.J.;
RT "The extended multidomain solution structures of the complement protein
RT Crry and its chimeric conjugate Crry-Ig by scattering, analytical
RT ultracentrifugation and constrained modelling: implications for function
RT and therapy.";
RL J. Mol. Biol. 329:525-550(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-288, AND DISULFIDE BONDS.
RX PubMed=21795784; DOI=10.1107/s1744309111016551;
RA Roversi P., Johnson S., Caesar J.J., McLean F., Leath K.J.,
RA Tsiftsoglou S.A., Morgan B.P., Harris C.L., Sim R.B., Lea S.M.;
RT "Structures of the rat complement regulator CrrY.";
RL Acta Crystallogr. F 67:739-743(2011).
CC -!- FUNCTION: Acts as a cofactor for complement factor I, a serine protease
CC which protects autologous cells against complement-mediated injury by
CC cleaving C3b and C4b deposited on host tissue. Also acts as a decay-
CC accelerating factor, preventing the formation of C4b2a and C3bBb, the
CC amplification convertases of the complement cascade. Seems to act as a
CC costimulatory factor for T-cells. May play a crucial role in early
CC embryonic development by maintaining fetomaternal tolerance.
CC {ECO:0000269|PubMed:15474557, ECO:0000269|PubMed:7534798,
CC ECO:0000269|PubMed:8144902}.
CC -!- SUBUNIT: Interacts with C3b. {ECO:0000269|PubMed:8144902}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q63135-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63135-2; Sequence=VSP_019051;
CC -!- SIMILARITY: Belongs to the receptors of complement activation (RCA)
CC family. {ECO:0000305}.
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DR EMBL; D42114; BAA07698.1; -; mRNA.
DR EMBL; D42115; BAA22548.1; -; mRNA.
DR EMBL; L36532; AAA91821.1; -; mRNA.
DR EMBL; BC061736; AAH61736.1; -; mRNA.
DR PIR; JC2054; JC2054.
DR RefSeq; NP_001005265.1; NM_001005265.1. [Q63135-2]
DR RefSeq; NP_001005330.1; NM_001005330.1.
DR RefSeq; NP_062174.1; NM_019301.2. [Q63135-1]
DR PDB; 1NTJ; X-ray; 30.00 A; A=34-353.
DR PDB; 2XRB; X-ray; 2.50 A; A=1-288.
DR PDB; 2XRD; X-ray; 3.50 A; A=1-288.
DR PDBsum; 1NTJ; -.
DR PDBsum; 2XRB; -.
DR PDBsum; 2XRD; -.
DR AlphaFoldDB; Q63135; -.
DR SMR; Q63135; -.
DR GlyGen; Q63135; 2 sites.
DR iPTMnet; Q63135; -.
DR PhosphoSitePlus; Q63135; -.
DR jPOST; Q63135; -.
DR PaxDb; Q63135; -.
DR PRIDE; Q63135; -.
DR GeneID; 54243; -.
DR KEGG; rno:54243; -.
DR CTD; 1379; -.
DR RGD; 2399; Cr1l.
DR VEuPathDB; HostDB:ENSRNOG00000008193; -.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_020107_5_2_1; -.
DR InParanoid; Q63135; -.
DR OrthoDB; 46968at2759; -.
DR PhylomeDB; Q63135; -.
DR TreeFam; TF334137; -.
DR EvolutionaryTrace; Q63135; -.
DR PRO; PR:Q63135; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000008193; Expressed in lung and 20 other tissues.
DR ExpressionAtlas; Q63135; baseline and differential.
DR Genevisible; Q63135; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
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:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR GO; GO:0006956; P:complement activation; ISO:RGD.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0007565; P:female pregnancy; IEA:UniProtKB-KW.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045916; P:negative regulation of complement activation; IMP:RGD.
DR GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IBA:GO_Central.
DR GO; GO:0030449; P:regulation of complement activation; ISO:RGD.
DR GO; GO:1903659; P:regulation of complement-dependent cytotoxicity; ISO:RGD.
DR GO; GO:0002456; P:T cell mediated immunity; IBA:GO_Central.
DR CDD; cd00033; CCP; 7.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 7.
DR SMART; SM00032; CCP; 7.
DR SUPFAM; SSF57535; SSF57535; 7.
DR PROSITE; PS50923; SUSHI; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complement pathway;
KW Developmental protein; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunity; Innate immunity; Membrane; Phosphoprotein;
KW Pregnancy; Receptor; Reference proteome; Repeat; Signal; Sushi;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..559
FT /note="Complement component receptor 1-like protein"
FT /id="PRO_0000238979"
FT TOPO_DOM 36..482
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..96
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 97..158
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 159..229
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 231..290
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 292..354
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 355..415
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 417..477
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 535..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64735"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64735"
FT MOD_RES 540
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64735"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 53
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:21795784"
FT DISULFID 68..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:21795784"
FT DISULFID 99..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:21795784"
FT DISULFID 126..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:21795784"
FT DISULFID 161..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:21795784"
FT DISULFID 190..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:21795784"
FT DISULFID 233..275
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:21795784"
FT DISULFID 261..288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:21795784"
FT DISULFID 294..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 322..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 357..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 386..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 419..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 448..475
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT VAR_SEQ 354..415
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8117286"
FT /id="VSP_019051"
FT CONFLICT 66
FT /note="Y -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="R -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 206..222
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:2XRB"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:2XRB"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:2XRB"
SQ SEQUENCE 559 AA; 61680 MW; 29E10F6A21DB9B6E CRC64;
MEASSPLDPV GRLVAFCRGG VHLAVLLLFL SPSTLGQCPA PPLFPYAKPI NPTDESTFPV
GTSLKYECRP GYIKRQFSIT CEVNSVWTSP QDVCIRKQCE TPLDPQNGIV HVNTDIRFGS
SITYTCNEGY RLIGSSSAMC IISDQSVAWD AEAPICESIP CEIPPSIPNG DFFSPNREDF
HYGMVVTYQC NTDARGKKLF NLVGEPSIHC TSIDGQVGVW SGPPPQCIEL NKCTPPHVEN
AVIVSKNKSL FSLRDMVEFR CQDGFMMKGD SSVYCRSLNR WEPQLPSCFK VKSCGAFLGE
LPNGHVFVPQ NLQLGAKVTF VCNTGYQLKG NSSSHCVLDG VESIWNSSVP VCEQVICKLP
QDMSGFQKGL QMKKDYYYGD NVALECEDGY TLEGSSQSQC QSDASWDPPL PKCVSQVICK
LPQDMSGFQK GLQMKKDYYY GDNVALECED GYTLEGSSQS QCQSDASWDP PLPKCVSRSN
SGLIAGIFIG IIVLILFIIF SYWMIMKFKK RNSTNEKCKE VGIYLNSKED SCVQPQSLLT
SQENNSTSSP ARNSLTQEV
