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Database: UniProt
Entry: P98137
LinkDB: P98137
Original site: P98137 
ID   CO8B_RABIT              Reviewed;         590 AA.
AC   P98137;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   10-APR-2019, entry version 109.
DE   RecName: Full=Complement component C8 beta chain;
DE   AltName: Full=Complement component 8 subunit beta;
DE   Flags: Precursor;
GN   Name=C8B;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=New Zealand white; TISSUE=Liver;
RX   PubMed=7510745;
RA   White R.V., Kaufman K.M., Letson C.S., Platteborze P.L., Sodetz J.M.;
RT   "Characterization of rabbit complement component C8. Functional
RT   evidence for the species-selective recognition of C8 alpha by
RT   homologous restriction factor (CD59).";
RL   J. Immunol. 152:2501-2508(1994).
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:0000269|PubMed:7510745}.
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:0000269|PubMed:7510745}.
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC       {ECO:0000305}.
DR   EMBL; L26980; AAA31192.1; -; mRNA.
DR   PIR; I46687; I46687.
DR   RefSeq; NP_001076137.1; NM_001082668.1.
DR   UniGene; Ocu.1991; -.
DR   ProteinModelPortal; P98137; -.
DR   SMR; P98137; -.
DR   STRING; 9986.ENSOCUP00000025903; -.
DR   PRIDE; P98137; -.
DR   GeneID; 100009385; -.
DR   KEGG; ocu:100009385; -.
DR   CTD; 732; -.
DR   HOVERGEN; HBG106489; -.
DR   InParanoid; P98137; -.
DR   KO; K03998; -.
DR   OrthoDB; 787014at2759; -.
DR   Proteomes; UP000001811; Unplaced.
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; 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   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; PS51412; MACPF_2; 1.
DR   PROSITE; PS50092; TSP1; 2.
PE   1: Evidence at protein 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     32       {ECO:0000255}.
FT   PROPEP       33     54       {ECO:0000255}.
FT                                /FTId=PRO_0000023595.
FT   CHAIN        55    590       Complement component C8 beta chain.
FT                                /FTId=PRO_0000023596.
FT   DOMAIN       64    117       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      120    157       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      158    504       MACPF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00745}.
FT   DOMAIN      505    535       EGF-like.
FT   DOMAIN      545    588       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   MOD_RES     418    418       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   CARBOHYD     44     44       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     70     70       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   CARBOHYD     73     73       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   CARBOHYD    101    101       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    551    551       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   CARBOHYD    554    554       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07358}.
FT   DISULFID     65    100       {ECO:0000250}.
FT   DISULFID     76     79       {ECO:0000250}.
FT   DISULFID    110    116       {ECO:0000250}.
FT   DISULFID    122    133       {ECO:0000250}.
FT   DISULFID    127    146       {ECO:0000250}.
FT   DISULFID    140    155       {ECO:0000250}.
FT   DISULFID    378    403       {ECO:0000250}.
FT   DISULFID    503    550       {ECO:0000250}.
FT   DISULFID    505    521       {ECO:0000250}.
FT   DISULFID    508    523       {ECO:0000250}.
FT   DISULFID    525    534       {ECO:0000250}.
FT   DISULFID    557    590       {ECO:0000250}.
SQ   SEQUENCE   590 AA;  66858 MW;  54ED81B15F2CCC2C CRC64;
     MKKSWTWTWR VPAELLLLCA ALGCLCVPGS RSERPRSLEP TVVNRSLAKS RHSRSVDATP
     MPIDCELSSW SSWTMCDPCQ KKRYRHAYLL RPSQFNGEPC NFSDKEVEDC ATSRPCRSQV
     RCEGFVCAQT GRCVNRRLLC NGDNDCGDQS DEANCRKIYK KCHHEMEQYW AIGSLASGIN
     LFTNSLEGPV LDHRYYAGGC NPHYILDMRF RKPYNVESYT PQTQGKYKFA LAEYESYSDF
     ERNVMEKTYS KSTFNLGFKI PSIFEFGINT ESDQLMNYIS RTKRFSHTKS KFLHARSALE
     VAHYKLKPRN LMLHYDFLQR VQRVPLEYSY GEYRDLFRDF GHHFITEAVL GGIYEYTLIM
     NKEAMERADY SLNDVQACAK NDFKLGAAIE EVYVSLGVST SKCRGILNEI KDRNKRDTMV
     QDLVVLVRGG ASEHITALAY SDLPTADLMQ EWGDAVQYNP AIIKIKVEPL YELVTATDVA
     YSSTVKQNMR QALEEFQGEV SPCRCAPCQG NGVPVQKGSR CDCICPVGFQ GSACEITSRK
     NVPIDGRWSC WSRWSSCSGG QKTRRRQCNN PAPQDGGSPC SGPASETLAC
//
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