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Protein

Complement component C6

Gene

C6

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells.By similarity

GO - Biological processi

  • complement activation, classical pathway Source: UniProtKB-KW
  • cytolysis Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • positive regulation of apoptotic process Source: RGD
Complete GO annotation...

Keywords - Biological processi

Complement pathway, Cytolysis, Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Complement component C6
Gene namesi
Name:C6
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2238. C6.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: RGD
  • membrane attack complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane attack complex, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21By similarityAdd BLAST21
ChainiPRO_000002358222 – 934Complement component C6Add BLAST913

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi22 ↔ 61By similarity
Disulfide bondi24 ↔ 65By similarity
Glycosylationi29C-linked (Man)By similarity1
Glycosylationi32C-linked (Man)By similarity1
Disulfide bondi35 ↔ 73By similarity
Glycosylationi38O-linked (Fuc...)By similarity1
Disulfide bondi39 ↔ 78By similarity
Disulfide bondi82 ↔ 117By similarity
Glycosylationi90C-linked (Man)By similarity1
Disulfide bondi93 ↔ 127By similarity
Disulfide bondi96 ↔ 133By similarity
Disulfide bondi140 ↔ 151By similarity
Disulfide bondi146 ↔ 164By similarity
Disulfide bondi158 ↔ 173By similarity
Disulfide bondi180 ↔ 218By similarity
Glycosylationi324N-linked (GlcNAc...)Sequence analysis1
Glycosylationi392O-linked (Fuc...)By similarity1
Disulfide bondi399 ↔ 420By similarity
Disulfide bondi499 ↔ 623By similarity
Disulfide bondi521 ↔ 570By similarity
Disulfide bondi523 ↔ 539By similarity
Disulfide bondi526 ↔ 541By similarity
Disulfide bondi543 ↔ 552By similarity
Glycosylationi568C-linked (Man)By similarity1
Glycosylationi571C-linked (Man)By similarity1
Glycosylationi574C-linked (Man)By similarity1
Disulfide bondi577 ↔ 611By similarity
Disulfide bondi589 ↔ 601By similarity
Disulfide bondi644 ↔ 686By similarity
Disulfide bondi672 ↔ 699By similarity
Disulfide bondi704 ↔ 746By similarity
Disulfide bondi732 ↔ 761By similarity
Disulfide bondi773 ↔ 823By similarity
Disulfide bondi784 ↔ 801By similarity
Disulfide bondi786 ↔ 837By similarity
Disulfide bondi793 ↔ 816By similarity
Disulfide bondi862 ↔ 873By similarity
Disulfide bondi867 ↔ 919By similarity
Disulfide bondi880 ↔ 897By similarity
Disulfide bondi882 ↔ 932By similarity
Disulfide bondi888 ↔ 912By similarity

Post-translational modificationi

All cysteine residues are assumed to be cross-linked to one another. Individual modules containing an even number of conserved cysteine residues are supposed to have disulfide linkages only within the same module (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ811M5.

Interactioni

Subunit structurei

Component of the membrane attack complex (MAC). MAC assembly is initiated by proteolytic cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8 and 12-14 copies of the pore-forming subunit C9 (By similarity).By similarity

Protein-protein interaction databases

BioGridi246424. 1 interactor.

Structurei

3D structure databases

ProteinModelPortaliQ811M5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 79TSP type-1 1PROSITE-ProRule annotationAdd BLAST58
Domaini81 – 134TSP type-1 2PROSITE-ProRule annotationAdd BLAST54
Domaini138 – 175LDL-receptor class APROSITE-ProRule annotationAdd BLAST38
Domaini176 – 522MACPFPROSITE-ProRule annotationAdd BLAST347
Domaini523 – 553EGF-likeAdd BLAST31
Domaini565 – 612TSP type-1 3PROSITE-ProRule annotationAdd BLAST48
Domaini642 – 701Sushi 1PROSITE-ProRule annotationAdd BLAST60
Domaini702 – 763Sushi 2PROSITE-ProRule annotationAdd BLAST62
Domaini780 – 839Kazal-like 1PROSITE-ProRule annotationAdd BLAST60
Domaini876 – 934Kazal-like 2PROSITE-ProRule annotationAdd BLAST59

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni611 – 688CCP 1Add BLAST78
Regioni642 – 934C5B-binding domainAdd BLAST293
Regioni689 – 765CCP 2Add BLAST77
Regioni766 – 840Factor I module (FIM) 1Add BLAST75
Regioni858 – 934Factor I module (FIM) 2Add BLAST77

Sequence similaritiesi

Belongs to the complement C6/C7/C8/C9 family.Curated
Contains 1 EGF-like domain.Curated
Contains 2 Kazal-like domains.PROSITE-ProRule annotation
Contains 1 LDL-receptor class A domain.PROSITE-ProRule annotation
Contains 1 MACPF domain.PROSITE-ProRule annotation
Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation
Contains 3 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Sushi

Phylogenomic databases

HOGENOMiHOG000111865.
HOVERGENiHBG005366.
InParanoidiQ811M5.
KOiK03995.
PhylomeDBiQ811M5.

Family and domain databases

CDDicd00033. CCP. 2 hits.
InterProiIPR003884. FacI_MAC.
IPR002350. Kazal_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001862. MAC_perforin.
IPR020864. MACPF.
IPR020863. MACPF_CS.
IPR000436. Sushi_SCR_CCP_dom.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF00057. Ldl_recept_a. 1 hit.
PF01823. MACPF. 1 hit.
PF00084. Sushi. 2 hits.
PF00090. TSP_1. 2 hits.
[Graphical view]
PRINTSiPR00764. COMPLEMENTC9.
SMARTiSM00032. CCP. 2 hits.
SM00057. FIMAC. 2 hits.
SM00192. LDLa. 1 hit.
SM00457. MACPF. 1 hit.
SM00209. TSP1. 3 hits.
[Graphical view]
SUPFAMiSSF57424. SSF57424. 1 hit.
SSF57535. SSF57535. 2 hits.
SSF82895. SSF82895. 3 hits.
PROSITEiPS00022. EGF_1. 1 hit.
PS51465. KAZAL_2. 2 hits.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 1 hit.
PS00279. MACPF_1. 1 hit.
PS51412. MACPF_2. 1 hit.
PS50923. SUSHI. 2 hits.
PS50092. TSP1. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q811M5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRHLTLCFI LLIILIDKSE ACFCDHYPWT HWSSCSKSCN SGTQSRQRQI
60 70 80 90 100
VVNDYYRDNS CDQLCTKQET RQCNVETCPI NCVLGDYGTW SDCDPCIRKQ
110 120 130 140 150
VKVRSVLRPS QFGGQPCTEP LVTFQPCVPS ELCKIEETDC KNKFLCDSGR
160 170 180 190 200
CIPSKLKCNG ENDCGDNSDE RNCGRTKPVC SRTYTPIPSV QLMGAGFHFL
210 220 230 240 250
AGEPRGDVPD NSFTGGICKS VRSSRTSNPH RVPANLENVN FEVQTIEDDL
260 270 280 290 300
KTDFYKDLAT IGKNKNEDRS LSGEKKDSFY VPIFYSSKKS ENFQRNSGFK
310 320 330 340 350
NAIEASHKKD SSFVRIHKVI KVLNFTMKTT DLQLSDVFLK ALIHLPLEYN
360 370 380 390 400
FALYSRIFDD FGTHYFTSGS LGGKYDLLYQ FSRQELQNSG LTEEETRNCV
410 420 430 440 450
RYETKKRFLF FTKTYKEDRC TTNRLSEKYK GSFLQGSEKS ISLVQGGRSQ
460 470 480 490 500
QAAALAWEKG SSGPEANVFS EWLESVKENP AVVDYELAPI IDLVRNIPCA
510 520 530 540 550
VTKRNNLRKA LQEYAAKFDP CQCAPCPNNG RPRLSGTECL CVCQSGTYGE
560 570 580 590 600
NCEKRSPDYK SNAVDGNWGC WSSWSACNAA YRRSRSRECN NPEPQRGGQR
610 620 630 640 650
CEGKHWQEED CTFSIMEKVG QPCISDDEEI KEVDLAEPEA DSGCPQPPLP
660 670 680 690 700
ENAFVWNEKK LYSVGEEVEI SCLTGFKAVG YQYFRCLPDR TWRQGDVECQ
710 720 730 740 750
RTECLKPVVQ DVLTISPFQS VYKIGESIEL TCPRGFVVAG PSRYTCKGDS
760 770 780 790 800
WTPPIPNSLS CEKDILTKSK GLCQPGQKQS GSECVCMSPE EDCSSYSEDL
810 820 830 840 850
CIFDEGSSQY FTSSACKFLA EKCLNSNQFH FVHAGSCQEG PQLEWGLERL
860 870 880 890 900
KLAMKSTKRV PCGYDTCYDW EKCSAHTSNC VCLLPPQCPK DENQLHCVKM
910 920 930
GSSMRGKTVN ICTLGAVRCA NRKVEILNPG RCLD
Length:934
Mass (Da):105,114
Last modified:June 1, 2003 - v1
Checksum:i90C219EEFF03AE15
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY230250 mRNA. Translation: AAO40768.1.
RefSeqiNP_788263.1. NM_176074.3.
UniGeneiRn.16145.

Genome annotation databases

GeneIDi24237.
KEGGirno:24237.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY230250 mRNA. Translation: AAO40768.1.
RefSeqiNP_788263.1. NM_176074.3.
UniGeneiRn.16145.

3D structure databases

ProteinModelPortaliQ811M5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246424. 1 interactor.

Proteomic databases

PRIDEiQ811M5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24237.
KEGGirno:24237.

Organism-specific databases

CTDi729.
RGDi2238. C6.

Phylogenomic databases

HOGENOMiHOG000111865.
HOVERGENiHBG005366.
InParanoidiQ811M5.
KOiK03995.
PhylomeDBiQ811M5.

Miscellaneous databases

PROiQ811M5.

Family and domain databases

CDDicd00033. CCP. 2 hits.
InterProiIPR003884. FacI_MAC.
IPR002350. Kazal_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001862. MAC_perforin.
IPR020864. MACPF.
IPR020863. MACPF_CS.
IPR000436. Sushi_SCR_CCP_dom.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF00057. Ldl_recept_a. 1 hit.
PF01823. MACPF. 1 hit.
PF00084. Sushi. 2 hits.
PF00090. TSP_1. 2 hits.
[Graphical view]
PRINTSiPR00764. COMPLEMENTC9.
SMARTiSM00032. CCP. 2 hits.
SM00057. FIMAC. 2 hits.
SM00192. LDLa. 1 hit.
SM00457. MACPF. 1 hit.
SM00209. TSP1. 3 hits.
[Graphical view]
SUPFAMiSSF57424. SSF57424. 1 hit.
SSF57535. SSF57535. 2 hits.
SSF82895. SSF82895. 3 hits.
PROSITEiPS00022. EGF_1. 1 hit.
PS51465. KAZAL_2. 2 hits.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 1 hit.
PS00279. MACPF_1. 1 hit.
PS51412. MACPF_2. 1 hit.
PS50923. SUSHI. 2 hits.
PS50092. TSP1. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO6_RAT
AccessioniPrimary (citable) accession number: Q811M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: June 1, 2003
Last modified: November 30, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.