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Database: UniProt
Entry: P55314
LinkDB: P55314
Original site: P55314 
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   08-MAY-2019, entry version 145.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   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.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   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.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian 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
RT   project: 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
CC       plays a key role in the innate and adaptive immune response by
CC       forming pores in the plasma membrane of target cells.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterotrimer of 3 chains: alpha, beta and gamma. The
CC       alpha and gamma chains are disulfide bonded. Component of the
CC       membrane attack complex (MAC). MAC assembly is initiated by
CC       proteolytic cleavage of C5 into C5a and C5b. C5b sequentially
CC       binds C6, C7, C8 and multiple copies of the pore-forming subunit
CC       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; Positions=248, 256; Evidence={ECO:0000305};
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   SMR; P55314; -.
DR   STRING; 10116.ENSRNOP00000010100; -.
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; ENOG410IE7H; Eukaryota.
DR   eggNOG; ENOG410Y2J1; LUCA.
DR   GeneTree; ENSGT00940000160247; -.
DR   HOGENOM; HOG000231146; -.
DR   InParanoid; P55314; -.
DR   KO; K03998; -.
DR   OMA; YSDFEHN; -.
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 2 organ(s), highest expression level in liver.
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; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
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; IPR013032; EGF-like_CS.
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; Complete proteome;
KW   Cytolysis; Disulfide bond; EGF-like domain; Glycoprotein; Immunity;
KW   Innate immunity; Membrane attack complex; Phosphoprotein;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   PROPEP       32     53       {ECO:0000250}.
FT                                /FTId=PRO_0000291305.
FT   CHAIN        54    589       Complement component C8 beta chain.
FT                                /FTId=PRO_0000162509.
FT   DOMAIN       63    116       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      120    155       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      157    503       MACPF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00745}.
FT   DOMAIN      504    534       EGF-like.
FT   DOMAIN      544    587       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   MOD_RES     417    417       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   CARBOHYD     43     43       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     69     69       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   CARBOHYD     72     72       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   CARBOHYD    242    242       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    550    550       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   CARBOHYD    553    553       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   DISULFID     64     99       {ECO:0000250}.
FT   DISULFID     75     78       {ECO:0000250}.
FT   DISULFID    109    115       {ECO:0000250}.
FT   DISULFID    121    132       {ECO:0000250}.
FT   DISULFID    126    145       {ECO:0000250}.
FT   DISULFID    139    154       {ECO:0000250}.
FT   DISULFID    502    549       {ECO:0000250}.
FT   DISULFID    504    520       {ECO:0000250}.
FT   DISULFID    507    522       {ECO:0000250}.
FT   DISULFID    524    533       {ECO:0000250}.
FT   DISULFID    556    589       {ECO:0000250}.
FT   CONFLICT    451    451       W -> R (in Ref. 3; AAA82890).
FT                                {ECO:0000305}.
FT   CONFLICT    458    458       N -> I (in Ref. 3; AAA82890).
FT                                {ECO:0000305}.
FT   CONFLICT    464    464       L -> S (in Ref. 3; AAA82890).
FT                                {ECO:0000305}.
FT   CONFLICT    497    497       M -> K (in Ref. 3; AAA82890).
FT                                {ECO:0000305}.
FT   CONFLICT    526    528       AGF -> VGL (in Ref. 3; AAA82890).
FT                                {ECO:0000305}.
FT   CONFLICT    588    588       D -> N (in Ref. 3; AAA82890).
FT                                {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
//
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