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Database: UniProt
Entry: Q9PVW7
LinkDB: Q9PVW7
Original site: Q9PVW7 
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   20-JUN-2018, entry version 98.
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
RT   Japanese flounder, Paralichthys olivaceus.";
RL   Immunogenetics 50:43-48(1999).
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}.
DR   EMBL; AB020962; BAA86877.1; -; mRNA.
DR   ProteinModelPortal; Q9PVW7; -.
DR   SMR; Q9PVW7; -.
DR   PRIDE; Q9PVW7; -.
DR   HOVERGEN; HBG106489; -.
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   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; PTHR19325:SF401; PTHR19325:SF401; 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;
KW   Innate immunity; Membrane attack complex; Repeat; Secreted; Signal.
FT   SIGNAL        1     30       {ECO:0000255}.
FT   PROPEP       31     46       {ECO:0000250}.
FT                                /FTId=PRO_0000023599.
FT   CHAIN        47    588       Complement component C8 beta chain.
FT                                /FTId=PRO_0000023600.
FT   DOMAIN       58    113       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      115    152       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      154    500       MACPF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00745}.
FT   DOMAIN      501    531       EGF-like.
FT   DOMAIN      542    588       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   CARBOHYD     64     64       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   CARBOHYD     67     67       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   CARBOHYD    548    548       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   CARBOHYD    551    551       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   DISULFID     59     94       {ECO:0000250}.
FT   DISULFID     70     73       {ECO:0000250}.
FT   DISULFID    104    112       {ECO:0000250}.
FT   DISULFID    118    129       {ECO:0000250}.
FT   DISULFID    123    142       {ECO:0000250}.
FT   DISULFID    136    151       {ECO:0000250}.
FT   DISULFID    374    399       {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
//
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