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Database: UniProt
Entry: P98136
LinkDB: P98136
Original site: P98136 
ID   CO8A_RABIT              Reviewed;         585 AA.
AC   P98136;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-JAN-2019, entry version 109.
DE   RecName: Full=Complement component C8 alpha chain;
DE   AltName: Full=Complement component 8 subunit alpha;
DE   Flags: Precursor;
GN   Name=C8A;
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], PROTEIN SEQUENCE OF 31-40, SUBUNIT, AND
RP   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
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. C8A inserts
CC       into the target membrane, but does not form pores by itself (By
CC       similarity). {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:0000269|PubMed:7510745}. Cell
CC       membrane {ECO:0000269|PubMed:7510745}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:7510745}. Note=Secreted as soluble protein.
CC       Inserts into the cell membrane of target cells.
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC       {ECO:0000305}.
DR   EMBL; L26981; AAA31191.1; -; mRNA.
DR   PIR; I46686; I46686.
DR   RefSeq; NP_001075724.1; NM_001082255.1.
DR   UniGene; Ocu.1990; -.
DR   ProteinModelPortal; P98136; -.
DR   SMR; P98136; -.
DR   CORUM; P98136; -.
DR   STRING; 9986.ENSOCUP00000014764; -.
DR   PRIDE; P98136; -.
DR   GeneID; 100009076; -.
DR   KEGG; ocu:100009076; -.
DR   CTD; 731; -.
DR   eggNOG; ENOG410IE8U; Eukaryota.
DR   eggNOG; ENOG410Y5MF; LUCA.
DR   HOGENOM; HOG000231146; -.
DR   HOVERGEN; HBG005368; -.
DR   InParanoid; P98136; -.
DR   KO; K03997; -.
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; IPR037565; Complement_C8_alpha.
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:SF385; PTHR19325:SF385; 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; 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   1: Evidence at protein level;
KW   Cell membrane; Complement alternate pathway; Complement pathway;
KW   Complete proteome; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Immunity;
KW   Innate immunity; Membrane; Membrane attack complex;
KW   Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane beta strand.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   PROPEP       21     30       {ECO:0000255}.
FT                                /FTId=PRO_0000023589.
FT   CHAIN        31    585       Complement component C8 alpha chain.
FT                                /FTId=PRO_0000023590.
FT   DOMAIN       38     91       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN       94    132       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      136    499       MACPF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00745}.
FT   DOMAIN      499    530       EGF-like.
FT   DOMAIN      540    584       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   CARBOHYD     44     44       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07357}.
FT   CARBOHYD    438    438       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    543    543       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07357}.
FT   CARBOHYD    546    546       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07357}.
FT   CARBOHYD    549    549       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P07357}.
FT   DISULFID     39     74       {ECO:0000250}.
FT   DISULFID     50     53       {ECO:0000250}.
FT   DISULFID     84     90       {ECO:0000250}.
FT   DISULFID     96    108       {ECO:0000250}.
FT   DISULFID    102    121       {ECO:0000250}.
FT   DISULFID    115    130       {ECO:0000250}.
FT   DISULFID    140    177       {ECO:0000250}.
FT   DISULFID    194    194       Interchain (with C-60 in C8-gamma chain).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000255|PROSITE-ProRule:PRU00210}.
SQ   SEQUENCE   585 AA;  65306 MW;  2FFD3241B0310048 CRC64;
     MLVAAFFTLF LVTCQPAVTA QEKVNQRVNR AATPRAFDCQ LSSWSEWTDC FPCQDTKYRH
     RSLLQPNKFG GTICSGDIWD RASCYSPTAC LRPAQCGQDF QCKETGRCLK RHLVCNGEND
     CLDGSDEDNC EDIRATESDC AQYDPIPGSE KAALGYNILT QEEAQSVYDA RYYGGRCETV
     YNGEWRHVRY DPVCERLHHG EDDKYFRKPY NFLKYHFEAR ADTGISFELY VDGNDLFSKV
     KNDKSHSAGV TISAGLTGSP LLGTVGVSGS EDASFLNKLS QYNEKKYNFM RIFTKVQTAH
     FKMRRDDIVL DEGMLQALVE LPEQYNYGMY SKFINDYGTH YITSGSMGGT YEYILVLNTE
     KMESLGVTSE DISSCFGGFG EIQYEKGKIN AQGILSGKHC KKSGSGDKEA DKMGQAVKDI
     ISRVRGGSSG WGGGLSQNGS ATTYRFWGRS LKYNPVVIDF EMQPIHEVLL HTNLGHVEAK
     RQNLRRALDQ YLMEFNACRC GPCFNNGKPI LEGTSCRCQC SLGLQGPACE QTEQQGAKAD
     GHWSCWGSWS PCTAGTRERR RECNNPAPQN GGAPCPGWRV QTQAC
//
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