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FLASH GENE

Symbol

C1S

contributors: mct - updated : 29-11-2016

HGNC name	complement component 1, s subcomponent
HGNC id	1247

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

Corresponding disease	C1S complement component 1S deficiency
Location	12p13.31      Physical location : 7.167.979 - 7.178.333
Synonym name	C1 esterase
EC.number	3.4.21.42

DNA

TYPE	functioning gene
STRUCTURE	10.36 kb     12 Exon(s)

10 Kb 5' upstream gene genomic sequence study

MAPPING

cloned

Y

linked

Y

status

confirmed

RNA

TRANSCRIPTS	type	messenger

identification nb exons type bp product Protein kDa AA specific expression Year Pubmed NM_201442 12 - 2850 NP_958850 76.7 688 - 2013 23592783 NM_001734 12 - 2763 NP_001725 - 688 - 2013 23592783 NM_001346850 - - 2648 NP_001333779 - 521 - 2013 23592783

EXPRESSION

Type

widely

expressed in	(based on citations)
organ(s)	System Organ level 1 Organ level 2 Organ level 3 Organ level 4 Level Pubmed Species Stage Rna symbol Digestive liver           mouth tongue       Respiratory lung       highly   respiratory tract larynx

cell lineage
cell lines
fluid/secretion	plasma

at STAGE

PROTEIN

PHYSICAL PROPERTIES

STRUCTURE

motifs/domains	two short consensus repeats, sushi structure
	one EGF-like domain
	two CUB domains, complement control domain
	serine protease domain in the C terminal region

mono polymer

dimer

isoforms

Precursor

HOMOLOGY

interspecies

ortholog to murine C1s

Homologene

FAMILY

serine protease/trypsin family

CATEGORY

enzyme , immunity/defense

SUBCELLULAR LOCALIZATION

extracellular

basic FUNCTION	complement component, s subcomponent, activating C2 and C4 after cleavage
	classical pathway of C3 activation
	C1R specificity is well suited to its cleavage targets and efficient cleavage of C1S is achieved through both active site and exosite contributions
	C1QA binds to the nucleolus in advanced apoptotic cells, and the C1QA-associated C1R/C1S proteases degrade nucleolar proteins
	complementary role of C1S in apoptotic cells clearance through the proteolytic cleavage of intracellular alarmins and autoantigens

CELLULAR PROCESS

PHYSIOLOGICAL PROCESS

PATHWAY

metabolism

signaling

a component	dimerizing after activation
	two C1S complexing with one C1Q,two C12
	C1, the first component of the complement system, is a Ca(2+)-dependent heteropentamer complex of C1QA and two modular serine proteases, C1R and C1S

INTERACTION

DNA

RNA

small molecule	metal binding,
	calcium Ca2+
	like heparin, Polyphosphate (polyP) is a naturally occurring cofactor for the C1s: SERPING1 interaction and thus an important regulator of complement activation

protein	activating C2 and C4
	C1S cleaves complement component C4 and then C2 to cause full activation of the system
	C1R both autoactivates and subsequently cleaves and activates C1S
	active C1S propagates the immune response through its ability to bind and cleave the effector molecule complement Component 4 (C4)
	C1QA recruits C1R/C1S to specific structures in dead cells, leading to cellular antigen degradation
	serpin, C1-esterase inhibitor (SERPING1), is the only known plasma inhibitor of C1s, the initiating serine protease of the classical pathway of complement

cell & other

REGULATION

activated by

C1q

inhibited by

C1 inhibitor (SERPING1)

ASSOCIATED DISORDERS

corresponding disease(s)

C1S , EDSPD2

related resource

CISbase - Mutation registry for C1s deficiency

Other morbid association(s)

Type Gene Modification Chromosome rearrangement Protein expression Protein Function constitutional     --low   strong association of congenital C1S deficiency with Systemic Lupus Erythematosus

Susceptibility

Variant & Polymorphism

Candidate gene

Marker

Therapy target

ANIMAL & CELL MODELS