CO8B_RABIT
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 25-MAY-2022, entry version 119.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR 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 evidence
RT for the species-selective recognition of C8 alpha by homologous restriction
RT factor (CD59).";
RL J. Immunol. 152:2501-2508(1994).
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:0000269|PubMed:7510745}.
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:0000269|PubMed:7510745}.
CC -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC {ECO:0000305}.
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DR EMBL; L26980; AAA31192.1; -; mRNA.
DR PIR; I46687; I46687.
DR RefSeq; NP_001076137.1; NM_001082668.1.
DR AlphaFoldDB; P98137; -.
DR SMR; P98137; -.
DR STRING; 9986.ENSOCUP00000025903; -.
DR PRIDE; P98137; -.
DR GeneID; 100009385; -.
DR KEGG; ocu:100009385; -.
DR CTD; 732; -.
DR eggNOG; KOG3535; Eukaryota.
DR InParanoid; P98137; -.
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 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; 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; PS51412; MACPF_2; 1.
DR PROSITE; PS50092; TSP1; 2.
PE 1: Evidence at protein level;
KW Complement alternate pathway; Complement pathway; Cytolysis;
KW Disulfide bond; EGF-like domain; Glycoprotein; Immunity; Innate immunity;
KW Membrane attack complex; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT PROPEP 33..54
FT /evidence="ECO:0000255"
FT /id="PRO_0000023595"
FT CHAIN 55..590
FT /note="Complement component C8 beta chain"
FT /id="PRO_0000023596"
FT DOMAIN 64..117
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 120..157
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 158..504
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 505..535
FT /note="EGF-like"
FT DOMAIN 545..588
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 557..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 418
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 73
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT CARBOHYD 554
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P07358"
FT DISULFID 65..100
FT /evidence="ECO:0000250"
FT DISULFID 76..79
FT /evidence="ECO:0000250"
FT DISULFID 110..116
FT /evidence="ECO:0000250"
FT DISULFID 122..133
FT /evidence="ECO:0000250"
FT DISULFID 127..146
FT /evidence="ECO:0000250"
FT DISULFID 140..155
FT /evidence="ECO:0000250"
FT DISULFID 378..403
FT /evidence="ECO:0000250"
FT DISULFID 503..550
FT /evidence="ECO:0000250"
FT DISULFID 505..521
FT /evidence="ECO:0000250"
FT DISULFID 508..523
FT /evidence="ECO:0000250"
FT DISULFID 525..534
FT /evidence="ECO:0000250"
FT DISULFID 557..590
FT /evidence="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
