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Complement C1r subcomponent-like protein (C1r-LP) (C1r-like protein) (EC 3.4.21.-) (C1r-like serine protease analog protein) (CLSPa)

 C1RL_HUMAN              Reviewed;         487 AA.
Q9NZP8; Q53GX9;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 2.
27-SEP-2017, entry version 134.
RecName: Full=Complement C1r subcomponent-like protein;
Short=C1r-LP;
Short=C1r-like protein;
EC=3.4.21.-;
AltName: Full=C1r-like serine protease analog protein;
Short=CLSPa;
Flags: Precursor;
Name=C1RL; Synonyms=C1RL1, C1RLP, CLSPA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, INDUCTION, AND VARIANT VAL-285.
TISSUE=Dendritic cell;
PubMed=15358180; DOI=10.1016/j.bbrc.2004.06.127;
Lin N., Liu S., Li N., Wu P., An H., Yu Y., Wan T., Cao X.;
"A novel human dendritic cell-derived C1r-like serine protease analog
inhibits complement-mediated cytotoxicity.";
Biochem. Biophys. Res. Commun. 321:329-336(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15527420; DOI=10.1042/BJ20041196;
Ligoudistianou C., Xu Y., Garnier G., Circolo A., Volanakis J.E.;
"A novel human complement-related protein, C1r-like protease (C1r-LP),
specifically cleaves pro-C1s.";
Biochem. J. 387:165-173(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
FUNCTION, AND MUTAGENESIS OF SER-436.
PubMed=15385675; DOI=10.1073/pnas.0405692101;
Wicher K.B., Fries E.;
"Prohaptoglobin is proteolytically cleaved in the endoplasmic
reticulum by the complement C1r-like protein.";
Proc. Natl. Acad. Sci. U.S.A. 101:14390-14395(2004).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-242 AND ASN-296.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-147; ASN-242 AND ASN-296.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[8]
GLYCOSYLATION AT ASN-242.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
-!- FUNCTION: Mediates the proteolytic cleavage of HP/haptoglobin in
the endoplasmic reticulum. {ECO:0000269|PubMed:15358180,
ECO:0000269|PubMed:15385675, ECO:0000269|PubMed:15527420}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15358180}.
-!- TISSUE SPECIFICITY: Highly expressed in placenta, liver, kidney,
pancreas, moderately in lung, spleen, prostate, ovary, colon, and
PBL, and weakly in heart, skeletal muscle, thymus, testis, and
small intestine. Expressed in PC-3 (prostate adenocarcinoma) and
SK-OV-3 (ovary adenocarcinoma) cells, but not in LoVo and HT-29
(colon adenocarcinoma), SMMC7721 (hepatocellular carcinoma), CaoV-
3 (ovary adenocarcinoma), HeLa (cervix epithelioid carcinoma),
MCF-7 (breast adenocarcinoma), U-251MG (glioma) or A-549 (lung
carcinoma) cells. Widely expressed in myeloid leukemia cell lines,
including K-562 (chronic myelogenous leukemia), THP-1
(myelomonocytic leukemia), HL-60 and NB4 (promyelocytic leukemia),
and KG-1 (acute myelogenous leukemia) cells. Expressed mainly in
the liver and in serum (at protein level).
{ECO:0000269|PubMed:15358180, ECO:0000269|PubMed:15527420}.
-!- INDUCTION: Up-regulated in monocytes and dendritic cells (DC)
undergoing maturation or activation.
{ECO:0000269|PubMed:15358180}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- CAUTION: Does not associate with the C1 complex. According to
PubMed:15385675, doesn't cleave the proform of complement C1s.
{ECO:0000305}.
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EMBL; AF178985; AAF44349.1; -; mRNA.
EMBL; AK222802; BAD96522.1; -; mRNA.
EMBL; AC018653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC094008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC233309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS8573.1; -.
RefSeq; NP_001284569.1; NM_001297640.1.
RefSeq; NP_057630.2; NM_016546.3.
UniGene; Hs.631730; -.
ProteinModelPortal; Q9NZP8; -.
SMR; Q9NZP8; -.
BioGrid; 119431; 3.
STRING; 9606.ENSP00000266542; -.
MEROPS; S01.189; -.
iPTMnet; Q9NZP8; -.
PhosphoSitePlus; Q9NZP8; -.
BioMuta; C1RL; -.
DMDM; 182705204; -.
EPD; Q9NZP8; -.
PaxDb; Q9NZP8; -.
PeptideAtlas; Q9NZP8; -.
PRIDE; Q9NZP8; -.
DNASU; 51279; -.
Ensembl; ENST00000266542; ENSP00000266542; ENSG00000139178.
GeneID; 51279; -.
KEGG; hsa:51279; -.
UCSC; uc001qsn.4; human.
CTD; 51279; -.
DisGeNET; 51279; -.
EuPathDB; HostDB:ENSG00000139178.10; -.
GeneCards; C1RL; -.
H-InvDB; HIX0010393; -.
HGNC; HGNC:21265; C1RL.
HPA; CAB026172; -.
HPA; HPA011338; -.
MIM; 608974; gene.
neXtProt; NX_Q9NZP8; -.
OpenTargets; ENSG00000139178; -.
PharmGKB; PA134957759; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118890; -.
HOGENOM; HOG000237311; -.
HOVERGEN; HBG000559; -.
InParanoid; Q9NZP8; -.
OMA; PWQAFTS; -.
OrthoDB; EOG091G05VY; -.
PhylomeDB; Q9NZP8; -.
TreeFam; TF330373; -.
ChiTaRS; C1RL; human.
GenomeRNAi; 51279; -.
PRO; PR:Q9NZP8; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139178; -.
CleanEx; HS_C1RL; -.
ExpressionAtlas; Q9NZP8; baseline and differential.
Genevisible; Q9NZP8; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
CDD; cd00041; CUB; 1.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.60.120.290; -; 1.
InterPro; IPR000859; CUB_dom.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00431; CUB; 1.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00042; CUB; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF49854; SSF49854; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57535; SSF57535; 1.
PROSITE; PS01180; CUB; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Complement pathway; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Immunity; Innate immunity; Polymorphism; Protease;
Reference proteome; Secreted; Serine protease; Signal.
SIGNAL 1 35 {ECO:0000255}.
CHAIN 36 487 Complement C1r subcomponent-like protein.
/FTId=PRO_0000318678.
DOMAIN 39 163 CUB. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 245 484 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 283 283 Charge relay system. {ECO:0000250}.
ACT_SITE 339 339 Charge relay system. {ECO:0000250}.
ACT_SITE 436 436 Charge relay system. {ECO:0000250}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 242 242 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 94 112 {ECO:0000250}.
DISULFID 402 421 {ECO:0000250}.
DISULFID 432 462 {ECO:0000250}.
VARIANT 285 285 I -> V (in dbSNP:rs3742089).
{ECO:0000269|PubMed:15358180}.
/FTId=VAR_038852.
MUTAGEN 436 436 S->A: Unable to cleave HP.
{ECO:0000269|PubMed:15385675}.
CONFLICT 94 94 C -> R (in Ref. 3; BAD96522).
{ECO:0000305}.
CONFLICT 99 99 V -> A (in Ref. 3; BAD96522).
{ECO:0000305}.
CONFLICT 349 349 I -> M (in Ref. 3; BAD96522).
{ECO:0000305}.
SEQUENCE 487 AA; 53498 MW; 6DE7CE9EA08C7990 CRC64;
MPGPRVWGKY LWRSPHSKGC PGAMWWLLLW GVLQACPTRG SVLLAQELPQ QLTSPGYPEP
YGKGQESSTD IKAPEGFAVR LVFQDFDLEP SQDCAGDSVT ISFVGSDPSQ FCGQQGSPLG
RPPGQREFVS SGRSLRLTFR TQPSSENKTA HLHKGFLALY QTVAVNYSQP ISEASRGSEA
INAPGDNPAK VQNHCQEPYY QAAAAGALTC ATPGTWKDRQ DGEEVLQCMP VCGRPVTPIA
QNQTTLGSSR AKLGNFPWQA FTSIHGRGGG ALLGDRWILT AAHTIYPKDS VSLRKNQSVN
VFLGHTAIDE MLKLGNHPVH RVVVHPDYRQ NESHNFSGDI ALLELQHSIP LGPNVLPVCL
PDNETLYRSG LLGYVSGFGM EMGWLTTELK YSRLPVAPRE ACNAWLQKRQ RPEVFSDNMF
CVGDETQRHS VCQGDSGSVY VVWDNHAHHW VATGIVSWGI GCGEGYDFYT KVLSYVDWIK
GVMNGKN


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