CO8B_MOUSE
ID CO8B_MOUSE Reviewed; 589 AA.
AC Q8BH35; Q4VAH1; Q8CHJ5; Q8CHJ6; Q8VC14;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Complement component C8 beta chain;
DE AltName: Full=Complement component 8 subunit beta;
DE Flags: Precursor;
GN Name=C8b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=DBA/2J, Mae/Stm, and MSM/Ms; TISSUE=Liver;
RA Tanaka S., Kikkawa Y., Hosonuma M.I., Koike S., Yonekawa H.;
RT "Two mouse strains with complementary mutations on the 8th complement.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; 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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-43 AND ASN-252.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BH35-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BH35-2; Sequence=VSP_016666;
CC -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC {ECO:0000305}.
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DR EMBL; AB077304; BAC41369.1; -; mRNA.
DR EMBL; AB077305; BAC41370.1; -; mRNA.
DR EMBL; AB077306; BAC41371.1; -; mRNA.
DR EMBL; AK050313; BAC34183.1; -; mRNA.
DR EMBL; BC022129; AAH22129.1; -; mRNA.
DR EMBL; BC096382; AAH96382.1; -; mRNA.
DR CCDS; CCDS18414.1; -. [Q8BH35-1]
DR CCDS; CCDS84762.1; -. [Q8BH35-2]
DR RefSeq; NP_001303600.1; NM_001316671.1. [Q8BH35-2]
DR RefSeq; NP_598643.1; NM_133882.2. [Q8BH35-1]
DR AlphaFoldDB; Q8BH35; -.
DR SMR; Q8BH35; -.
DR BioGRID; 225551; 3.
DR ComplexPortal; CPX-6202; Membrane attack complex.
DR STRING; 10090.ENSMUSP00000031663; -.
DR GlyGen; Q8BH35; 6 sites.
DR iPTMnet; Q8BH35; -.
DR PhosphoSitePlus; Q8BH35; -.
DR CPTAC; non-CPTAC-3535; -.
DR CPTAC; non-CPTAC-5590; -.
DR jPOST; Q8BH35; -.
DR MaxQB; Q8BH35; -.
DR PaxDb; Q8BH35; -.
DR PeptideAtlas; Q8BH35; -.
DR PRIDE; Q8BH35; -.
DR ProteomicsDB; 283548; -. [Q8BH35-1]
DR ProteomicsDB; 283549; -. [Q8BH35-2]
DR Antibodypedia; 19370; 211 antibodies from 27 providers.
DR DNASU; 110382; -.
DR Ensembl; ENSMUST00000031663; ENSMUSP00000031663; ENSMUSG00000029656. [Q8BH35-1]
DR Ensembl; ENSMUST00000065072; ENSMUSP00000066940; ENSMUSG00000029656. [Q8BH35-2]
DR GeneID; 110382; -.
DR KEGG; mmu:110382; -.
DR UCSC; uc008txy.1; mouse. [Q8BH35-1]
DR UCSC; uc012dhv.1; mouse. [Q8BH35-2]
DR CTD; 732; -.
DR MGI; MGI:88236; C8b.
DR VEuPathDB; HostDB:ENSMUSG00000029656; -.
DR eggNOG; KOG3535; Eukaryota.
DR GeneTree; ENSGT00940000160247; -.
DR HOGENOM; CLU_032453_1_0_1; -.
DR InParanoid; Q8BH35; -.
DR OMA; CEGFLCA; -.
DR OrthoDB; 787014at2759; -.
DR PhylomeDB; Q8BH35; -.
DR TreeFam; TF330498; -.
DR Reactome; R-MMU-166665; Terminal pathway of complement.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 110382; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q8BH35; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BH35; protein.
DR Bgee; ENSMUSG00000029656; Expressed in left lobe of liver and 25 other tissues.
DR Genevisible; Q8BH35; MM.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005579; C:membrane attack complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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 GO; GO:0050778; P:positive regulation of immune response; IC:ComplexPortal.
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; 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 1: Evidence at protein level;
KW Alternative splicing; Complement alternate pathway; Complement pathway;
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
FT /evidence="ECO:0000255"
FT PROPEP 32..53
FT /evidence="ECO:0000250"
FT /id="PRO_0000023593"
FT CHAIN 54..589
FT /note="Complement component C8 beta chain"
FT /id="PRO_0000023594"
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 404..534
FT /note="EGF-like"
FT DOMAIN 544..587
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 570..589
FT /note="Disordered"
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:0000269|PubMed:16944957"
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 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
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 377..402
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 VAR_SEQ 222..287
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_016666"
FT VARIANT 14
FT /note="S -> W (in strain: Mae/Stm)"
FT VARIANT 19
FT /note="A -> T (in strain: MSM/Ms)"
FT VARIANT 60
FT /note="A -> E (in strain: Mae/Stm)"
FT VARIANT 118
FT /note="Q -> R (in strain: MSM/Ms)"
FT VARIANT 160
FT /note="N -> K (in strain: Mae/Stm)"
FT VARIANT 449
FT /note="E -> K (in strain: Mae/Stm and MSM/Ms)"
FT VARIANT 497
FT /note="S -> R (in strain: Mae/Stm and MSM/Ms)"
FT VARIANT 503
FT /note="R -> H (in strain: Mae/Stm and MSM/Ms)"
FT VARIANT 564
FT /note="H -> Q (in strain: Mae/Stm)"
FT VARIANT 569
FT /note="N -> S (in strain: MSM/Ms)"
FT VARIANT 577
FT /note="S -> N (in strain: Mae/Stm and MSM/Ms)"
SQ SEQUENCE 589 AA; 66229 MW; 540B299AFBC408A0 CRC64;
MKIGAQVWRA LAKSCLLCAT LGCLHFPGSR GGKPDFFETK AVNGSLVKSR PVRSVAEAPA
PIDCELSTWS SWTACDPCQK KRYRHTYLLR PSQFYGELCD LSDKEVEDCV TNQPCRSQVR
CEGFVCAQTG RCVNRRLLCN GDNDCGDQSD EANCRRIYKN CQREMEQYWA IDRLASGINL
FTNTFEGPVL DHRYYAGGCS PHYILDTNFR KPYNVESYTP QTKCEYEFTL TEYESYSDFE
RLVIEKKTHM FNFTSGFKVD GVMDLGIKVE SNEGKNYVTR TKRFAHTQSK FLHARSVLEV
AHYKLKSRSL MLHYEFLQRV KSLPLEYSYG EYRDLLRDFG THFITEAVLG GIYEYTLIMN
KDAMEQGDYT LSHVTACAGG SFGIGGMVYK VYVKVGVSAK KCSDIMKEIN ERNKRSTMVE
DLVVLVRGGT SEDITALAYK ELPTPELMEA WGDAVKYNPA IIKIKAEPLY ELVTATDFAY
SSTVKQNLKK ALEEFQSEVS SCRCAPCRGN GVPVLKGSRC ECICPGGFQG TACEVTYRKD
IPIDGKWSCW SDWSACSGGH KTRHRQCNNP APHKGGSPCS GPASETLNC
