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Protein

Complement component C8 beta chain

Gene

C8b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 - Molecular functioni

  • protein complex binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Complement alternate pathway, Complement pathway, Cytolysis, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiR-RNO-166665. Terminal pathway of complement.
R-RNO-977606. Regulation of Complement cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement component C8 beta chain
Alternative name(s):
Complement component 8 subunit beta
Gene namesi
Name:C8b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi2239. C8b.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: Ensembl
  • extracellular region Source: RGD
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence analysisAdd
BLAST
Propeptidei32 – 5322By similarityPRO_0000291305Add
BLAST
Chaini54 – 589536Complement component C8 beta chainPRO_0000162509Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...)Sequence analysis
Disulfide bondi64 ↔ 99By similarity
Glycosylationi69 – 691C-linked (Man)By similarity
Glycosylationi72 – 721C-linked (Man)By similarity
Disulfide bondi75 ↔ 78By similarity
Disulfide bondi109 ↔ 115By similarity
Disulfide bondi121 ↔ 132By similarity
Disulfide bondi126 ↔ 145By similarity
Disulfide bondi139 ↔ 154By similarity
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence analysis
Modified residuei417 – 4171PhosphothreonineBy similarity
Disulfide bondi502 ↔ 549By similarity
Disulfide bondi504 ↔ 520By similarity
Disulfide bondi507 ↔ 522By similarity
Disulfide bondi524 ↔ 533By similarity
Glycosylationi550 – 5501C-linked (Man)By similarity
Glycosylationi553 – 5531C-linked (Man)By similarity
Disulfide bondi556 ↔ 589By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP55314.
PRIDEiP55314.

Expressioni

Gene expression databases

GenevisibleiP55314. RN.

Interactioni

Subunit structurei

Heterotrimer of 3 chains: alpha, beta and gamma. The alpha and gamma chains are disulfide bonded. Component of the membrane attack complex (MAC). MAC assembly is initiated by protelytic cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8 and multiple copies of the pore-forming subunit C9 (By similarity).By similarity

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010100.

Structurei

3D structure databases

ProteinModelPortaliP55314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 11654TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini120 – 15536LDL-receptor class APROSITE-ProRule annotationAdd
BLAST
Domaini157 – 503347MACPFPROSITE-ProRule annotationAdd
BLAST
Domaini504 – 53431EGF-likeAdd
BLAST
Domaini544 – 58744TSP type-1 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IE7H. Eukaryota.
ENOG410Y2J1. LUCA.
GeneTreeiENSGT00550000074478.
HOGENOMiHOG000231146.
HOVERGENiHBG106489.
InParanoidiP55314.
KOiK03998.
OMAiGIYEYTL.
OrthoDBiEOG7QK0BJ.
PhylomeDBiP55314.
TreeFamiTF330498.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001862. MAC_perforin.
IPR020864. MACPF.
IPR020863. MACPF_CS.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF00057. Ldl_recept_a. 1 hit.
PF01823. MACPF. 1 hit.
PF00090. TSP_1. 2 hits.
[Graphical view]
PRINTSiPR00764. COMPLEMENTC9.
SMARTiSM00192. LDLa. 1 hit.
SM00457. MACPF. 1 hit.
SM00209. TSP1. 2 hits.
[Graphical view]
SUPFAMiSSF57424. SSF57424. 1 hit.
SSF82895. SSF82895. 2 hits.
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 1 hit.
PS00279. MACPF_1. 1 hit.
PS51412. MACPF_2. 1 hit.
PS50092. TSP1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P55314-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTGAQVWRA LAKSCLLCAA LGCLHLPGAR GEKPDFFETN AVNGSLVRSR
60 70 80 90 100
PVRSVDVTPA PTDCQLSTWS SWTACDPCQK KRYRHTYLLR PSQFYGELCD
110 120 130 140 150
FSDKEVEDCV TNRACRSQVR CEGFVCAQTG RCVNRRLLCN GDNDCGDQSD
160 170 180 190 200
EANCRRIYKK CSQDMEQYWA IGNLASGINL FTNTFEGPVL DHRYYAGACS
210 220 230 240 250
PHYILNTNFR KPYNVESYTP QTQGKYEFAL TEYESYFDFE HNVTEKATSK
260 270 280 290 300
SSFKFGFKLD GLVEFGVRKE SNEGRHYISR TKRFSHTKSK FLHARSVLEV
310 320 330 340 350
AHYKLKSRQL MLHYEFLQRV KSLPLEYSYG EYRDLLRDFG THFITEAVLG
360 370 380 390 400
GIYEYTLIMN KDAMERGDYT LDHVSACAGG GFQIGGNVYK VYLKLGVSEK
410 420 430 440 450
KCSDILNEIK DRNKRRTMVE DLVVLVRGGT SEYITSLAYK DLPTAELMKE
460 470 480 490 500
WGDAVQYNPA IIKLKAEPLY ELVTATDFAY SSTVKQNMKK ALEEFQMEVS
510 520 530 540 550
SCRCAPCRNN GVPILKESRC ECICPAGFQG VACEVTNRKD IPIDGKWSCW
560 570 580
SDWSPCSGGR KTRQRQCNNP APQRGGSPCS GPASETLDC
Length:589
Mass (Da):66,667
Last modified:June 12, 2007 - v2
Checksum:i1F0143FE1BFA2EB3
GO

Sequence cautioni

The sequence CO561829 differs from that shown. Reason: Frameshift at positions 248 and 256. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti451 – 4511W → R in AAA82890 (PubMed:7665162).Curated
Sequence conflicti458 – 4581N → I in AAA82890 (PubMed:7665162).Curated
Sequence conflicti464 – 4641L → S in AAA82890 (PubMed:7665162).Curated
Sequence conflicti497 – 4971M → K in AAA82890 (PubMed:7665162).Curated
Sequence conflicti526 – 5283AGF → VGL in AAA82890 (PubMed:7665162).Curated
Sequence conflicti588 – 5881D → N in AAA82890 (PubMed:7665162).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03041555 Genomic DNA. No translation available.
AABR03042213 Genomic DNA. No translation available.
CO561829 mRNA. No translation available.
BC090023 mRNA. Translation: AAH90023.1.
U20194 mRNA. Translation: AAA82890.1.
RefSeqiNP_001178688.1. NM_001191759.1.
XP_006238557.1. XM_006238495.2.
UniGeneiRn.110603.

Genome annotation databases

EnsembliENSRNOT00000010100; ENSRNOP00000010100; ENSRNOG00000007639.
GeneIDi313421.
KEGGirno:313421.
UCSCiRGD:2239. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03041555 Genomic DNA. No translation available.
AABR03042213 Genomic DNA. No translation available.
CO561829 mRNA. No translation available.
BC090023 mRNA. Translation: AAH90023.1.
U20194 mRNA. Translation: AAA82890.1.
RefSeqiNP_001178688.1. NM_001191759.1.
XP_006238557.1. XM_006238495.2.
UniGeneiRn.110603.

3D structure databases

ProteinModelPortaliP55314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010100.

Proteomic databases

PaxDbiP55314.
PRIDEiP55314.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010100; ENSRNOP00000010100; ENSRNOG00000007639.
GeneIDi313421.
KEGGirno:313421.
UCSCiRGD:2239. rat.

Organism-specific databases

CTDi732.
RGDi2239. C8b.

Phylogenomic databases

eggNOGiENOG410IE7H. Eukaryota.
ENOG410Y2J1. LUCA.
GeneTreeiENSGT00550000074478.
HOGENOMiHOG000231146.
HOVERGENiHBG106489.
InParanoidiP55314.
KOiK03998.
OMAiGIYEYTL.
OrthoDBiEOG7QK0BJ.
PhylomeDBiP55314.
TreeFamiTF330498.

Enzyme and pathway databases

ReactomeiR-RNO-166665. Terminal pathway of complement.
R-RNO-977606. Regulation of Complement cascade.

Miscellaneous databases

PROiP55314.

Gene expression databases

GenevisibleiP55314. RN.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001862. MAC_perforin.
IPR020864. MACPF.
IPR020863. MACPF_CS.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF00057. Ldl_recept_a. 1 hit.
PF01823. MACPF. 1 hit.
PF00090. TSP_1. 2 hits.
[Graphical view]
PRINTSiPR00764. COMPLEMENTC9.
SMARTiSM00192. LDLa. 1 hit.
SM00457. MACPF. 1 hit.
SM00209. TSP1. 2 hits.
[Graphical view]
SUPFAMiSSF57424. SSF57424. 1 hit.
SSF82895. SSF82895. 2 hits.
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 1 hit.
PS00279. MACPF_1. 1 hit.
PS51412. MACPF_2. 1 hit.
PS50092. TSP1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-259 AND 160-589.
    Tissue: Liver.
  3. "Molecular mapping of SSRs for Pgm1 and C8b in the vicinity of the rat fatty locus."
    Kershaw E.E., Chua S.C., Williams J.A., Murphy E.M., Leibel R.L.
    Genomics 27:149-154(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 450-589.
    Strain: Brown Norway/Crl.
    Tissue: Liver.

Entry informationi

Entry nameiCO8B_RAT
AccessioniPrimary (citable) accession number: P55314
Secondary accession number(s): Q5EB58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 12, 2007
Last modified: June 8, 2016
This is version 124 of the entry and version 2 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.