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Q9NZP8

- C1RL_HUMAN

UniProt

Q9NZP8 - C1RL_HUMAN

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Protein

Complement C1r subcomponent-like protein

Gene

C1RL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Mediates the proteolytic cleavage of HP/haptoglobin in the endoplasmic reticulum.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei283 – 2831Charge relay systemBy similarity
Active sitei339 – 3391Charge relay systemBy similarity
Active sitei436 – 4361Charge relay systemBy similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. complement activation, classical pathway Source: UniProtKB-KW
  2. innate immune response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Complement pathway, Immunity, Innate immunity

Protein family/group databases

MEROPSiS01.189.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C1r subcomponent-like protein (EC:3.4.21.-)
Short name:
C1r-LP
Short name:
C1r-like protein
Alternative name(s):
C1r-like serine protease analog protein
Short name:
CLSPa
Gene namesi
Name:C1RL
Synonyms:C1RL1, C1RLP, CLSPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:21265. C1RL.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular space Source: UniProt
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi436 – 4361S → A: Unable to cleave HP. 1 Publication

Organism-specific databases

PharmGKBiPA134957759.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence AnalysisAdd
BLAST
Chaini36 – 487452Complement C1r subcomponent-like proteinPRO_0000318678Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi94 ↔ 112By similarity
Glycosylationi147 – 1471N-linked (GlcNAc...)1 Publication
Glycosylationi166 – 1661N-linked (GlcNAc...)1 Publication
Glycosylationi242 – 2421N-linked (GlcNAc...) (complex)3 Publications
Glycosylationi296 – 2961N-linked (GlcNAc...)2 Publications
Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi402 ↔ 421By similarity
Disulfide bondi432 ↔ 462By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9NZP8.
PRIDEiQ9NZP8.

PTM databases

PhosphoSiteiQ9NZP8.

Expressioni

Tissue specificityi

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).2 Publications

Inductioni

Up-regulated in monocytes and dendritic cells (DC) undergoing maturation or activation.1 Publication

Gene expression databases

BgeeiQ9NZP8.
CleanExiHS_C1RL.
ExpressionAtlasiQ9NZP8. baseline and differential.
GenevestigatoriQ9NZP8.

Organism-specific databases

HPAiHPA011338.

Interactioni

Protein-protein interaction databases

BioGridi119431. 2 interactions.
STRINGi9606.ENSP00000266542.

Structurei

3D structure databases

ProteinModelPortaliQ9NZP8.
SMRiQ9NZP8. Positions 51-483.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 163125CUBPROSITE-ProRule annotationAdd
BLAST
Domaini245 – 484240Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 CUB domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000237311.
HOVERGENiHBG000559.
InParanoidiQ9NZP8.
OMAiWQAFTSI.
PhylomeDBiQ9NZP8.
TreeFamiTF330373.

Family and domain databases

Gene3Di2.60.120.290. 1 hit.
InterProiIPR000859. CUB_dom.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00431. CUB. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00042. CUB. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 1 hit.
PROSITEiPS01180. CUB. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NZP8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPGPRVWGKY LWRSPHSKGC PGAMWWLLLW GVLQACPTRG SVLLAQELPQ
60 70 80 90 100
QLTSPGYPEP YGKGQESSTD IKAPEGFAVR LVFQDFDLEP SQDCAGDSVT
110 120 130 140 150
ISFVGSDPSQ FCGQQGSPLG RPPGQREFVS SGRSLRLTFR TQPSSENKTA
160 170 180 190 200
HLHKGFLALY QTVAVNYSQP ISEASRGSEA INAPGDNPAK VQNHCQEPYY
210 220 230 240 250
QAAAAGALTC ATPGTWKDRQ DGEEVLQCMP VCGRPVTPIA QNQTTLGSSR
260 270 280 290 300
AKLGNFPWQA FTSIHGRGGG ALLGDRWILT AAHTIYPKDS VSLRKNQSVN
310 320 330 340 350
VFLGHTAIDE MLKLGNHPVH RVVVHPDYRQ NESHNFSGDI ALLELQHSIP
360 370 380 390 400
LGPNVLPVCL PDNETLYRSG LLGYVSGFGM EMGWLTTELK YSRLPVAPRE
410 420 430 440 450
ACNAWLQKRQ RPEVFSDNMF CVGDETQRHS VCQGDSGSVY VVWDNHAHHW
460 470 480
VATGIVSWGI GCGEGYDFYT KVLSYVDWIK GVMNGKN
Length:487
Mass (Da):53,498
Last modified:February 26, 2008 - v2
Checksum:i6DE7CE9EA08C7990
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941C → R in BAD96522. 1 PublicationCurated
Sequence conflicti99 – 991V → A in BAD96522. 1 PublicationCurated
Sequence conflicti349 – 3491I → M in BAD96522. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti285 – 2851I → V.1 Publication
Corresponds to variant rs3742089 [ dbSNP | Ensembl ].
VAR_038852

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF178985 mRNA. Translation: AAF44349.1.
AK222802 mRNA. Translation: BAD96522.1.
AC018653 Genomic DNA. No translation available.
AC094008 Genomic DNA. No translation available.
AC233309 Genomic DNA. No translation available.
CCDSiCCDS8573.1.
RefSeqiNP_057630.2. NM_016546.3.
UniGeneiHs.631730.

Genome annotation databases

EnsembliENST00000266542; ENSP00000266542; ENSG00000139178.
GeneIDi51279.
KEGGihsa:51279.
UCSCiuc001qsn.3. human.

Polymorphism databases

DMDMi182705204.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF178985 mRNA. Translation: AAF44349.1 .
AK222802 mRNA. Translation: BAD96522.1 .
AC018653 Genomic DNA. No translation available.
AC094008 Genomic DNA. No translation available.
AC233309 Genomic DNA. No translation available.
CCDSi CCDS8573.1.
RefSeqi NP_057630.2. NM_016546.3.
UniGenei Hs.631730.

3D structure databases

ProteinModelPortali Q9NZP8.
SMRi Q9NZP8. Positions 51-483.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119431. 2 interactions.
STRINGi 9606.ENSP00000266542.

Protein family/group databases

MEROPSi S01.189.

PTM databases

PhosphoSitei Q9NZP8.

Polymorphism databases

DMDMi 182705204.

Proteomic databases

PaxDbi Q9NZP8.
PRIDEi Q9NZP8.

Protocols and materials databases

DNASUi 51279.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000266542 ; ENSP00000266542 ; ENSG00000139178 .
GeneIDi 51279.
KEGGi hsa:51279.
UCSCi uc001qsn.3. human.

Organism-specific databases

CTDi 51279.
GeneCardsi GC12M007245.
H-InvDB HIX0010393.
HGNCi HGNC:21265. C1RL.
HPAi HPA011338.
MIMi 608974. gene.
neXtProti NX_Q9NZP8.
PharmGKBi PA134957759.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000118890.
HOGENOMi HOG000237311.
HOVERGENi HBG000559.
InParanoidi Q9NZP8.
OMAi WQAFTSI.
PhylomeDBi Q9NZP8.
TreeFami TF330373.

Miscellaneous databases

ChiTaRSi C1RL. human.
GenomeRNAii 51279.
NextBioi 54501.
PROi Q9NZP8.
SOURCEi Search...

Gene expression databases

Bgeei Q9NZP8.
CleanExi HS_C1RL.
ExpressionAtlasi Q9NZP8. baseline and differential.
Genevestigatori Q9NZP8.

Family and domain databases

Gene3Di 2.60.120.290. 1 hit.
InterProi IPR000859. CUB_dom.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00431. CUB. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00042. CUB. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF49854. SSF49854. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 1 hit.
PROSITEi PS01180. CUB. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel human dendritic cell-derived C1r-like serine protease analog inhibits complement-mediated cytotoxicity."
    Lin N., Liu S., Li N., Wu P., An H., Yu Y., Wan T., Cao X.
    Biochem. Biophys. Res. Commun. 321:329-336(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, VARIANT VAL-285.
    Tissue: Dendritic cell.
  2. "A novel human complement-related protein, C1r-like protease (C1r-LP), specifically cleaves pro-C1s."
    Ligoudistianou C., Xu Y., Garnier G., Circolo A., Volanakis J.E.
    Biochem. J. 387:165-173(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  3. 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
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  4. "The finished DNA sequence of human chromosome 12."
    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.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Prohaptoglobin is proteolytically cleaved in the endoplasmic reticulum by the complement C1r-like protein."
    Wicher K.B., Fries E.
    Proc. Natl. Acad. Sci. U.S.A. 101:14390-14395(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF SER-436.
  6. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-242 AND ASN-296.
    Tissue: Plasma.
  7. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-147; ASN-242 AND ASN-296.
    Tissue: Liver.
  8. Cited for: GLYCOSYLATION AT ASN-242.

Entry informationi

Entry nameiC1RL_HUMAN
AccessioniPrimary (citable) accession number: Q9NZP8
Secondary accession number(s): Q53GX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: October 29, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Does not associate with the C1 complex. According to PubMed:15385675, doesn't cleave the proform of complement C1s.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3