CO8B_PAROL
ID CO8B_PAROL Reviewed; 588 AA.
AC Q9PVW7;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Complement component C8 beta chain;
DE AltName: Full=Complement component 8 subunit beta;
DE Flags: Precursor;
GN Name=c8b;
OS Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Paralichthyidae;
OC Paralichthys.
OX NCBI_TaxID=8255;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10541805; DOI=10.1007/s002510050684;
RA Katagiri T., Hirono I., Aoki T.;
RT "Molecular analysis of complement component C8beta and C9 cDNAs of Japanese
RT flounder, Paralichthys olivaceus.";
RL Immunogenetics 50:43-48(1999).
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; AB020962; BAA86877.1; -; mRNA.
DR AlphaFoldDB; Q9PVW7; -.
DR SMR; Q9PVW7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005579; C:membrane attack complex; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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 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; Repeat; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..46
FT /evidence="ECO:0000250"
FT /id="PRO_0000023599"
FT CHAIN 47..588
FT /note="Complement component C8 beta chain"
FT /id="PRO_0000023600"
FT DOMAIN 58..113
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 115..152
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 542..588
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT CARBOHYD 64
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 67
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 548
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 551
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT DISULFID 59..94
FT /evidence="ECO:0000250"
FT DISULFID 70..73
FT /evidence="ECO:0000250"
FT DISULFID 104..112
FT /evidence="ECO:0000250"
FT DISULFID 118..129
FT /evidence="ECO:0000250"
FT DISULFID 123..142
FT /evidence="ECO:0000250"
FT DISULFID 136..151
FT /evidence="ECO:0000250"
FT DISULFID 374..399
FT /evidence="ECO:0000250"
SQ SEQUENCE 588 AA; 65872 MW; 0C525BB95E7AC2AF CRC64;
MFRVAIPRSA LNLHSCLLHV TLSLVLISKA AITTAGNEDS DVREARSVSD QQVVHPVDCV
ISDWSAWSRC DTCQKKRYRY AKLDQPSQFG GEPCHFHDME DEACDVPDRY TCDSIPLCEG
FLCTQTGRCI HRTLQCNGED DCGDMSDEVG CKKVPKPCRQ EAEEYWGIEN LAKGINILNS
NLEGLVLDNR YYAGSCLPQY IQDVRFRKPH NLQQYTLETK GSYDFNVQSF ESYSDYMDYS
MRERMTQTIV SIGFAIPGIA EFGFNYNNAK VTRSIQKIRR ASSKINSFVS AKAELELAQY
MLRSDDLMLH PEFLQRLRSL PQAYVYGEYR QIYRDYGTHY ITEAALGGEY EHTIILDKEK
LAKTDYSLED YKSCTQAGLK IGANIYGVYV SAGIEGGSCN GLLNEMGEDT AIGSSVEDFV
AVVRGGSSES ITGLVSKKLP TPQLMRLWGE GVRFNPDFIR KTTRPLYELV TSKDFSHDAT
LKRNLKRALS EYLAESSSCR CAPCHNNGVA VLRGTRCDCV CPTGYTGRGC EITQRKKQIA
TDGSWSCWGA WSSCSGRKMS RSRQCNNPVP SDGGLACRGL QQESTDCF
