CO8B_ONCMY
ID CO8B_ONCMY Reviewed; 587 AA.
AC Q90X85;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Complement component C8 beta chain;
DE AltName: Full=Complement component 8 subunit beta;
DE Flags: Precursor;
GN Name=c8b;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12590968; DOI=10.1016/s0145-305x(02)00092-7;
RA Kazantzi A., Sfyroera G., Holland M.C.H., Lambris J.D., Zarkadis I.K.;
RT "Molecular cloning of the beta subunit of complement component eight of
RT rainbow trout.";
RL Dev. Comp. Immunol. 27:167-174(2003).
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}.
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DR EMBL; AF418597; AAL16647.1; -; mRNA.
DR RefSeq; NP_001118079.1; NM_001124607.1.
DR AlphaFoldDB; Q90X85; -.
DR SMR; Q90X85; -.
DR GeneID; 100136625; -.
DR KEGG; omy:100136625; -.
DR CTD; 732; -.
DR OrthoDB; 787014at2759; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005579; C:membrane attack complex; IEA:UniProtKB-KW.
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; IPR036055; LDL_receptor-like_sf.
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 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; 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; Repeat; Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT PROPEP 32..44
FT /evidence="ECO:0000250"
FT /id="PRO_0000023597"
FT CHAIN 45..587
FT /note="Complement component C8 beta chain"
FT /id="PRO_0000023598"
FT DOMAIN 56..111
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 117..159
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 154..500
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 501..531
FT /note="EGF-like"
FT DOMAIN 541..587
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT CARBOHYD 62
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 65
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 547
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 550
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT DISULFID 57..92
FT /evidence="ECO:0000250"
FT DISULFID 68..71
FT /evidence="ECO:0000250"
FT DISULFID 102..110
FT /evidence="ECO:0000250"
FT DISULFID 118..129
FT /evidence="ECO:0000250"
FT DISULFID 123..142
FT /evidence="ECO:0000250"
FT DISULFID 136..158
FT /evidence="ECO:0000250"
FT DISULFID 374..399
FT /evidence="ECO:0000250"
SQ SEQUENCE 587 AA; 65540 MW; 6D80417659FC879E CRC64;
MNHKLKPTVG LGYCLLCAAL CLLLLRDVAI AGSGEEPSGV REARSVGTQV AVQPVDCVQS
EWSSWTRCDV CRKKRYRYAK LVQPSQFGGE PCHVQGKEVE PCSPPSRYDC THDETPLCEG
FLCTYTGRCV PIDLRCNGDD DCGDWSAEKG SPKVPKACKQ EAQEYHGIEN LAKGINILHS
HLEGSVIDNR YYAGSCLPHY IQDVRFRKPY NLQQYTLETK GTYDFKLQSF ESYSEFVHYT
MTERSSKTTV SIGFALPGVA EFGFNYADSK YSKSEKKIRR ASRKENSFVQ AKAELQLARY
ILKSEDLMLH PEFFLRLRAL PQSYNYGEYR QIYRDYGTHY ITEATLGGDY EYTVILDKEK
LEKTGYSLEA YKNCEQIVLK VGANIKGVYV TVGLEGGGCD GLLNEMGEDT VKGSMVEDYV
AVVSGGDSES ITWLAAKNLP TPPLMRLWGE AVHYNLDFIR SVTRPLYELV TARDFSSANS
LKKNLRRALA EYLEESSSCR CAPCRNNGLA VLKGTRCECV CPSGYSGLGC EITQRPDIGI
DGSWSCWGSW SPCRGRSKTR SRQCNNPAPS SGGIACRGLQ METTDCF
