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complement C1r subcomponent-like protein (C1r-like protein, C1r-LP, C1r-like serine protease analog protein, CLSPa, C1RL, C1RL1, C1RLP, CLSPA)
Function:
- mediates proteolytic cleavage of HP/haptoglobin in the endoplasmic reticulum
- does not associate with the C1 complex
- does not cleave the proform of complement C1s [2]
Structure:
- belongs to the peptidase S1 family
- contains 1 CUB domain
- contains 1 peptidase S1 domain
Compartment: secreted
Expression:
- expressed in placenta, liver, kidney, pancreas > lung, spleen, prostate, ovary, colon, peripheral blood leukacytes > heart, skeletal muscle, thymus, testis, & small intestine
- expressed mainly in liver & in serum (at protein level)
- up-regulated in monocytes & dendritic cells undergoing maturation or activation
Pathology:
- expressed in PC-3 (prostate adenocarcinoma) & SK-OV-3 (ovary adenocarcinoma) cells, but not in LoVo & HT-29 (colon adenocarcinoma), SMMC7721 (hepatocellular carcinoma), CaoV-3 (ovary adenocarcinoma), HeLa (cervix epithelioid carcinoma), MCF-7 (breast adenocarcinoma), U251 (glioma) or A549 (lung carcinoma) cells
- widely expressed in myeloid leukemia cell lines, including K-562 (chronic myelogenous leukemia), THP-1 (myelomonocytic leukemia), HL-60 & NB4 (promyelocytic leukemia), & KG-1 (acute myelogenous leukemia) cells
General
glycoprotein
protease; proteinase; endopeptidase
secreted protein
Properties
SIZE: entity length = 487 aa
MW = 53 kD
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-35}
CUB domain {39-163}
MOTIF: cysteine residue {C94}
MODIFICATION: cysteine residue {C112}
cysteine residue {C112}
MODIFICATION: cysteine residue {C94}
N-glycosylation site {N166}
N-glycosylation site {N242}
S1 domain {245-484}
MOTIF: histidine residue {H283}
N-glycosylation site {N296}
aspartate residue {D339}
N-glycosylation site {N363}
cysteine residue {C402}
MODIFICATION: cysteine residue {C421}
cysteine residue {C421}
MODIFICATION: cysteine residue {C402}
cysteine residue {C432}
MODIFICATION: cysteine residue {C462}
serine residue {S436}
cysteine residue {C462}
MODIFICATION: cysteine residue {C432}
Database Correlations
UniProt Q9NZP8
PFAM correlations
Kegg hsa:5127
References
- UniProt :accession Q9NZP8
- Wicher KB, Fries E.
Prohaptoglobin is proteolytically cleaved in the endoplasmic
reticulum by the complement C1r-like protein.
Proc Natl Acad Sci U S A. 2004 Oct 5;101(40):14390-5.
Epub 2004 Sep 22.
PMID: 15385675