CO8B_RAT
ID CO8B_RAT Reviewed; 589 AA.
AC P55314; Q5EB58;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Complement component C8 beta chain;
DE AltName: Full=Complement component 8 subunit beta;
DE Flags: Precursor;
GN Name=C8b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-259 AND 160-589.
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 450-589.
RC STRAIN=Brown Norway/Crl; TISSUE=Liver;
RX PubMed=7665162; DOI=10.1006/geno.1995.1017;
RA Kershaw E.E., Chua S.C., Williams J.A., Murphy E.M., Leibel R.L.;
RT "Molecular mapping of SSRs for Pgm1 and C8b in the vicinity of the rat
RT fatty locus.";
RL Genomics 27:149-154(1995).
CC -!- FUNCTION: Constituent of the membrane attack complex (MAC) that plays a
CC key role in the innate and adaptive immune response by forming pores in
CC the plasma membrane of target cells. {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer of 3 chains: alpha, beta and gamma. The alpha and
CC gamma chains are disulfide bonded. Component of the membrane attack
CC complex (MAC). MAC assembly is initiated by proteolytic cleavage of C5
CC into C5a and C5b. C5b sequentially binds C6, C7, C8 and multiple copies
CC of the pore-forming subunit C9 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CO561829; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AABR03041555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03042213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CO561829; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC090023; AAH90023.1; -; mRNA.
DR EMBL; U20194; AAA82890.1; -; mRNA.
DR RefSeq; NP_001178688.1; NM_001191759.1.
DR RefSeq; XP_006238557.1; XM_006238495.3.
DR AlphaFoldDB; P55314; -.
DR SMR; P55314; -.
DR STRING; 10116.ENSRNOP00000010100; -.
DR GlyGen; P55314; 6 sites.
DR PaxDb; P55314; -.
DR PRIDE; P55314; -.
DR Ensembl; ENSRNOT00000010100; ENSRNOP00000010100; ENSRNOG00000007639.
DR GeneID; 313421; -.
DR KEGG; rno:313421; -.
DR UCSC; RGD:2239; rat.
DR CTD; 732; -.
DR RGD; 2239; C8b.
DR eggNOG; KOG3535; Eukaryota.
DR GeneTree; ENSGT00940000160247; -.
DR HOGENOM; CLU_032453_1_0_1; -.
DR InParanoid; P55314; -.
DR OMA; CEGFLCA; -.
DR OrthoDB; 787014at2759; -.
DR PhylomeDB; P55314; -.
DR TreeFam; TF330498; -.
DR Reactome; R-RNO-166665; Terminal pathway of complement.
DR Reactome; R-RNO-977606; Regulation of Complement cascade.
DR PRO; PR:P55314; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007639; Expressed in liver and 2 other tissues.
DR Genevisible; P55314; RN.
DR GO; GO:0005576; C:extracellular region; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005579; C:membrane attack complex; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0006956; P:complement activation; IBA:GO_Central.
DR GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.20.100.10; -; 2.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR037566; Complement_C8_beta.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR001862; MAC_perforin.
DR InterPro; IPR020864; MACPF.
DR InterPro; IPR020863; MACPF_CS.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR45742:SF5; PTHR45742:SF5; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF01823; MACPF; 1.
DR Pfam; PF00090; TSP_1; 2.
DR PRINTS; PR00764; COMPLEMENTC9.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00457; MACPF; 1.
DR SMART; SM00209; TSP1; 2.
DR SUPFAM; SSF57424; SSF57424; 1.
DR SUPFAM; SSF82895; SSF82895; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS00279; MACPF_1; 1.
DR PROSITE; PS51412; MACPF_2; 1.
DR PROSITE; PS50092; TSP1; 2.
PE 2: Evidence at transcript level;
KW Complement alternate pathway; Complement pathway; Cytolysis;
KW Disulfide bond; EGF-like domain; Glycoprotein; Immunity; Innate immunity;
KW Membrane attack complex; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT PROPEP 32..53
FT /evidence="ECO:0000250"
FT /id="PRO_0000291305"
FT CHAIN 54..589
FT /note="Complement component C8 beta chain"
FT /id="PRO_0000162509"
FT DOMAIN 63..116
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 120..155
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 157..503
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 504..534
FT /note="EGF-like"
FT DOMAIN 544..587
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 556..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 417
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 72
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 553
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT DISULFID 64..99
FT /evidence="ECO:0000250"
FT DISULFID 75..78
FT /evidence="ECO:0000250"
FT DISULFID 109..115
FT /evidence="ECO:0000250"
FT DISULFID 121..132
FT /evidence="ECO:0000250"
FT DISULFID 126..145
FT /evidence="ECO:0000250"
FT DISULFID 139..154
FT /evidence="ECO:0000250"
FT DISULFID 502..549
FT /evidence="ECO:0000250"
FT DISULFID 504..520
FT /evidence="ECO:0000250"
FT DISULFID 507..522
FT /evidence="ECO:0000250"
FT DISULFID 524..533
FT /evidence="ECO:0000250"
FT DISULFID 556..589
FT /evidence="ECO:0000250"
FT CONFLICT 451
FT /note="W -> R (in Ref. 3; AAA82890)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="N -> I (in Ref. 3; AAA82890)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="L -> S (in Ref. 3; AAA82890)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="M -> K (in Ref. 3; AAA82890)"
FT /evidence="ECO:0000305"
FT CONFLICT 526..528
FT /note="AGF -> VGL (in Ref. 3; AAA82890)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="D -> N (in Ref. 3; AAA82890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 66667 MW; 1F0143FE1BFA2EB3 CRC64;
MKTGAQVWRA LAKSCLLCAA LGCLHLPGAR GEKPDFFETN AVNGSLVRSR PVRSVDVTPA
PTDCQLSTWS SWTACDPCQK KRYRHTYLLR PSQFYGELCD FSDKEVEDCV TNRACRSQVR
CEGFVCAQTG RCVNRRLLCN GDNDCGDQSD EANCRRIYKK CSQDMEQYWA IGNLASGINL
FTNTFEGPVL DHRYYAGACS PHYILNTNFR KPYNVESYTP QTQGKYEFAL TEYESYFDFE
HNVTEKATSK SSFKFGFKLD GLVEFGVRKE SNEGRHYISR TKRFSHTKSK FLHARSVLEV
AHYKLKSRQL MLHYEFLQRV KSLPLEYSYG EYRDLLRDFG THFITEAVLG GIYEYTLIMN
KDAMERGDYT LDHVSACAGG GFQIGGNVYK VYLKLGVSEK KCSDILNEIK DRNKRRTMVE
DLVVLVRGGT SEYITSLAYK DLPTAELMKE WGDAVQYNPA IIKLKAEPLY ELVTATDFAY
SSTVKQNMKK ALEEFQMEVS SCRCAPCRNN GVPILKESRC ECICPAGFQG VACEVTNRKD
IPIDGKWSCW SDWSPCSGGR KTRQRQCNNP APQRGGSPCS GPASETLDC
