ID CR1L_HUMAN Reviewed; 569 AA. AC Q2VPA4; Q32MC9; Q8NEU7; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 24-JAN-2024, entry version 136. DE RecName: Full=Complement component receptor 1-like protein; DE AltName: Full=Complement C4b-binding protein CR-1-like protein; DE Flags: Precursor; GN Name=CR1L; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1). RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-526 (ISOFORM 1), AND VARIANTS ASP-402 AND VAL-455. 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 57-569 (ISOFORM 3), TISSUE SPECIFICITY, RP INTERACTION WITH IC4, AND SUBCELLULAR LOCATION. RC TISSUE=Bone marrow; RX PubMed=14687939; DOI=10.1016/j.molimm.2003.09.010; RA Logar C.M., Chen W., Schmitt H., Yu C.Y., Birmingham D.J.; RT "A human CR1-like transcript containing sequence for a binding protein for RT iC4 is expressed in hematopoietic and fetal lymphoid tissue."; RL Mol. Immunol. 40:831-840(2004). CC -!- SUBUNIT: Interacts with iC4 (methylamine-treated C4) but not for iC3 CC (methylamine-treated C3). {ECO:0000269|PubMed:14687939}. CC -!- INTERACTION: CC Q2VPA4; Q8NEL9-2: DDHD1; NbExp=3; IntAct=EBI-12330477, EBI-11062258; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14687939}. Membrane CC {ECO:0000269|PubMed:14687939}. Secreted {ECO:0000269|PubMed:14687939}. CC Note=Predominantly found in association with the membrane fraction, but CC also located in the cytoplasm and in the supernatant. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q2VPA4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q2VPA4-2; Sequence=VSP_031151, VSP_031152, VSP_031153; CC Name=3; CC IsoId=Q2VPA4-3; Sequence=VSP_031152, VSP_031153; CC -!- TISSUE SPECIFICITY: Expressed in fetal liver and to a lesser extent in CC fetal spleen and thymus. Expression appears to be limited to CC hematopoietic and fetal lymphoid tissue. {ECO:0000269|PubMed:14687939}. CC -!- SIMILARITY: Belongs to the receptors of complement activation (RCA) CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL137789; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL365178; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC109190; AAI09191.1; -; mRNA. DR EMBL; BC109191; AAI09192.1; -; mRNA. DR EMBL; AY114160; AAM47024.1; -; mRNA. DR CCDS; CCDS44310.1; -. [Q2VPA4-1] DR RefSeq; NP_783641.1; NM_175710.1. [Q2VPA4-1] DR AlphaFoldDB; Q2VPA4; -. DR SMR; Q2VPA4; -. DR BioGRID; 107770; 12. DR IntAct; Q2VPA4; 1. DR STRING; 9606.ENSP00000421736; -. DR GlyCosmos; Q2VPA4; 1 site, No reported glycans. DR GlyGen; Q2VPA4; 1 site. DR iPTMnet; Q2VPA4; -. DR PhosphoSitePlus; Q2VPA4; -. DR BioMuta; CR1L; -. DR DMDM; 296439386; -. DR EPD; Q2VPA4; -. DR jPOST; Q2VPA4; -. DR MassIVE; Q2VPA4; -. DR PaxDb; 9606-ENSP00000421736; -. DR PeptideAtlas; Q2VPA4; -. DR Antibodypedia; 53872; 58 antibodies from 11 providers. DR DNASU; 1379; -. DR Ensembl; ENST00000508064.7; ENSP00000421736.2; ENSG00000197721.17. [Q2VPA4-1] DR GeneID; 1379; -. DR KEGG; hsa:1379; -. DR MANE-Select; ENST00000508064.7; ENSP00000421736.2; NM_175710.2; NP_783641.1. DR UCSC; uc001hga.5; human. [Q2VPA4-1] DR AGR; HGNC:2335; -. DR CTD; 1379; -. DR DisGeNET; 1379; -. DR GeneCards; CR1L; -. DR HGNC; HGNC:2335; CR1L. DR HPA; ENSG00000197721; Tissue enriched (bone). DR MIM; 605886; gene. DR neXtProt; NX_Q2VPA4; -. DR OpenTargets; ENSG00000197721; -. DR PharmGKB; PA26856; -. DR VEuPathDB; HostDB:ENSG00000197721; -. DR eggNOG; KOG4297; Eukaryota. DR GeneTree; ENSGT00940000164130; -. DR InParanoid; Q2VPA4; -. DR OMA; QQIFCPN; -. DR OrthoDB; 5395408at2759; -. DR PhylomeDB; Q2VPA4; -. DR TreeFam; TF334137; -. DR PathwayCommons; Q2VPA4; -. DR SignaLink; Q2VPA4; -. DR BioGRID-ORCS; 1379; 58 hits in 1140 CRISPR screens. DR ChiTaRS; CR1L; human. DR GenomeRNAi; 1379; -. DR Pharos; Q2VPA4; Tdark. DR PRO; PR:Q2VPA4; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q2VPA4; Protein. DR Bgee; ENSG00000197721; Expressed in bone marrow and 103 other cell types or tissues. DR ExpressionAtlas; Q2VPA4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0043235; C:receptor complex; IDA:MGI. DR GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IBA:GO_Central. DR GO; GO:0030449; P:regulation of complement activation; IDA:MGI. DR GO; GO:1903659; P:regulation of complement-dependent cytotoxicity; IDA:MGI. DR GO; GO:0002456; P:T cell mediated immunity; IBA:GO_Central. DR CDD; cd00033; CCP; 8. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 8. DR InterPro; IPR035976; Sushi/SCR/CCP_sf. DR InterPro; IPR000436; Sushi_SCR_CCP_dom. DR PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1. DR PANTHER; PTHR19325:SF545; COMPLEMENT RECEPTOR TYPE 1; 1. DR Pfam; PF00084; Sushi; 8. DR SMART; SM00032; CCP; 8. DR SUPFAM; SSF57535; Complement control module/SCR domain; 8. DR PROSITE; PS50923; SUSHI; 8. DR Genevisible; Q2VPA4; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Disulfide bond; Glycoprotein; Membrane; KW Reference proteome; Repeat; Secreted; Signal; Sushi. FT SIGNAL 1..32 FT /evidence="ECO:0000255" FT CHAIN 33..569 FT /note="Complement component receptor 1-like protein" FT /id="PRO_0000317776" FT DOMAIN 33..93 FT /note="Sushi 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 94..155 FT /note="Sushi 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 156..226 FT /note="Sushi 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 228..287 FT /note="Sushi 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 287..347 FT /note="Sushi 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 348..410 FT /note="Sushi 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 411..472 FT /note="Sushi 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 473..543 FT /note="Sushi 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT CARBOHYD 48 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 35..78 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 65..91 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 96..137 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 123..153 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 158..207 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 187..224 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 230..272 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 258..285 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 289..332 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 318..345 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 350..392 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 378..408 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 413..454 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 440..470 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 504..541 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT VAR_SEQ 1..263 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_031151" FT VAR_SEQ 444 FT /note="H -> F (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14687939, FT ECO:0000303|PubMed:15489334" FT /id="VSP_031152" FT VAR_SEQ 445..569 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14687939, FT ECO:0000303|PubMed:15489334" FT /id="VSP_031153" FT VARIANT 116 FT /note="R -> G (in dbSNP:rs2296158)" FT /id="VAR_038677" FT VARIANT 139 FT /note="I -> V (in dbSNP:rs3085)" FT /id="VAR_038678" FT VARIANT 402 FT /note="N -> D (in dbSNP:rs12729569)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_038679" FT VARIANT 455 FT /note="I -> V (in dbSNP:rs6683902)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_038680" FT VARIANT 491 FT /note="L -> P (in dbSNP:rs2796257)" FT /id="VAR_038681" SQ SEQUENCE 569 AA; 62714 MW; D49F7517E1347A5D CRC64; MAPPVRLERP FPSRRFPGLL LAALVLLLSS FSDQCNVPEW LPFARPTNLT DDFEFPIGTY LNYECRPGYS GRPFSIICLK NSVWTSAKDK CKRKSCRNPP DPVNGMAHVI KDIQFRSQIK YSCPKGYRLI GSSSATCIIS GNTVIWDNKT PVCDRIICGL PPTIANGDFT SISREYFHYG SVVTYHCNLG SRGKKVFELV GEPSIYCTSK DDQVGIWSGP APQCIIPNKC TPPNVENGIL VSDNRSLFSL NEVVEFRCQP GFGMKGPSHV KCQALNKWEP ELPSCSRVCQ PPPDVLHAER TQRDKDNFSP GQEVFYSCEP GYDLRGSTYL HCTPQGDWSP AAPRCEVKSC DDFLGQLPNG HVLFPLNLQL GAKVDFVCDE GFQLKGSSAS YCVLAGMESL WNSSVPVCER KSCETPPVPV NGMVHVITDI HVGSRINYSC TTGHRLIGHS SAECILSGNT AHWSMKPPIC QQIFCPNPPA ILNGRHTGTP LGDIPYGKEV SYTCDPHPDR GMTFNLIGES TIRRTSEPHG NGVWSSPAPR CELPVGAGSH DALIVGKFYE VFAEEFCHL //