A0A4W4EEX1 · A0A4W4EEX1_ELEEL

Function

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Features

Showing features for binding site, active site.

167350100150200250300350400450500550600650
Type
IDPosition(s)Description
Binding site60Ca2+ 1 (UniProtKB | ChEBI)
Binding site68Ca2+ 1 (UniProtKB | ChEBI)
Binding site114Ca2+ 1 (UniProtKB | ChEBI)
Binding site116Ca2+ 1 (UniProtKB | ChEBI)
Binding site132Ca2+ 2 (UniProtKB | ChEBI)
Binding site133Ca2+ 2 (UniProtKB | ChEBI)
Binding site135Ca2+ 2 (UniProtKB | ChEBI)
Binding site149Ca2+ 2 (UniProtKB | ChEBI)
Binding site150Ca2+ 2 (UniProtKB | ChEBI)
Binding site153Ca2+ 2 (UniProtKB | ChEBI)
Binding site223Ca2+ 3 (UniProtKB | ChEBI)
Binding site231Ca2+ 3 (UniProtKB | ChEBI)
Binding site268Ca2+ 3 (UniProtKB | ChEBI)
Active site462Charge relay system
Active site515Charge relay system
Active site616Charge relay system

GO annotations

AspectTerm
Cellular Componentblood microparticle
Molecular Functioncalcium ion binding
Molecular Functionserine-type endopeptidase activity
Biological Processcomplement activation, classical pathway
Biological Processinnate immune response
Biological Processzymogen activation

Keywords

Names & Taxonomy

Protein names

  • Submitted names
    • Complement component 1, s subcomponent.1

Gene names

    • Name
      c1s.2

Organism names

Accessions

  • Primary accession
    A0A4W4EEX1

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, modified residue.

Type
IDPosition(s)Description
Signal1-16
ChainPRO_502121269517-673
Disulfide bond65↔83
Disulfide bond136↔147
Disulfide bond143↔156
Modified residue149(3R)-3-hydroxyasparagine
Disulfide bond158↔171
Disulfide bond175↔200
Disulfide bond229↔246
Disulfide bond287↔332
Disulfide bond314↔344
Disulfide bond349↔392
Disulfide bond377↔409
Disulfide bond413↔535Interchain (between heavy and light chains)
Disulfide bond588↔601
Disulfide bond612↔647

Post-translational modification

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-131CUB
Domain132-172EGF-like
Domain171-283CUB
Domain285-346Sushi
Domain347-411Sushi
Domain424-671Peptidase S1

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    673
  • Mass (Da)
    73,906
  • Last updated
    2019-09-18 v1
  • MD5 Checksum
    3DEEFF30D6CB2233C175C02A7CA04057
MIVIFVCVLLVQVCGSVPLAGWVQSPGYPFGYDPHATLTWKHCAAPGHTLMLSFFHLDLEDSEQCENDVVKVFAGNVLLTKLCGRMSAQHLLSSVNPLLRSSSGGCLSLSFEADFSNPERHTGFRAFYKEQDVDECWDHEPECSHFCHNYIGGYTCSCKPGYYLSEDQHTCSANCTEELFGEGVLTPVGSPGPYLENSFCTYTLAVQEGQQLVLSFVGEFDVESRDGQCIDTLTIKTDSAVFGPFCGQTAPPKISTGAQRVQIFFHTDQGGTNTGFTLSYRAKPMQCPGNVTANSILAPQRSQYTPGDTVTVQCVTGHSLESTLQQTFESTCQKSGRWSPVRYCEPIDCGPPNFSDLIVLTEEDPVTTYNHNISVKCLSEYYELIGDANFICDASGTWVSEKAQTKPLCLPVCGKNTAFSSGRIFGGRKAQPEELPWHLLIKEPQRGGASLISDQWAVTAAHVVDRYESDTLIFYGGITDGMDRNAVLMESEKIIIHPGFEKRKPEQDHTNYDNDIALVKMSARVSLGPNIRPVCLPNKTNSLPEQTARLSMEGKMGTISGFGGRSETLTKARYLQYGHVIEYSEVPCFPNNLKVTDNMFCAGGKSKEVDSCKGDSGGPLVVPAVGSGSPNTRHQLKGIVSWGPSICGNEHNKGYYTKVENYLDWIMETMQKN

Keywords

Genome annotation databases

Similar Proteins

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