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   25-MAY-2022, entry version 115.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; 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 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. C8A inserts into the target
CC       membrane, but does not form pores by itself (By similarity).
CC       {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:0000269|PubMed:7510745}. Cell
CC       membrane {ECO:0000269|PubMed:7510745}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:7510745}. Note=Secreted as soluble protein. Inserts
CC       into the cell membrane of target cells.
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC       {ECO:0000305}.
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DR   EMBL; L26981; AAA31191.1; -; mRNA.
DR   PIR; I46686; I46686.
DR   RefSeq; NP_001075724.1; NM_001082255.1.
DR   AlphaFoldDB; P98136; -.
DR   SMR; P98136; -.
DR   CORUM; P98136; -.
DR   STRING; 9986.ENSOCUP00000014764; -.
DR   GeneID; 100009076; -.
DR   KEGG; ocu:100009076; -.
DR   CTD; 731; -.
DR   eggNOG; ENOG502QT87; Eukaryota.
DR   InParanoid; P98136; -.
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; 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; PTHR45742:SF1; PTHR45742:SF1; 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; Cytolysis;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Immunity; Innate immunity; Membrane; Membrane attack complex;
KW   Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane beta strand.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..30
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000023589"
FT   CHAIN           31..585
FT                   /note="Complement component C8 alpha chain"
FT                   /id="PRO_0000023590"
FT   DOMAIN          38..91
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          94..132
FT                   /note="LDL-receptor class A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          136..499
FT                   /note="MACPF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT   DOMAIN          499..530
FT                   /note="EGF-like"
FT   DOMAIN          540..584
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   CARBOHYD        44
FT                   /note="C-linked (Man) tryptophan"
FT                   /evidence="ECO:0000250|UniProtKB:P07357"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        543
FT                   /note="C-linked (Man) tryptophan"
FT                   /evidence="ECO:0000250|UniProtKB:P07357"
FT   CARBOHYD        546
FT                   /note="C-linked (Man) tryptophan"
FT                   /evidence="ECO:0000250|UniProtKB:P07357"
FT   CARBOHYD        549
FT                   /note="C-linked (Man) tryptophan"
FT                   /evidence="ECO:0000250|UniProtKB:P07357"
FT   DISULFID        39..74
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..53
FT                   /evidence="ECO:0000250"
FT   DISULFID        84..90
FT                   /evidence="ECO:0000250"
FT   DISULFID        96..108
FT                   /evidence="ECO:0000250"
FT   DISULFID        102..121
FT                   /evidence="ECO:0000250"
FT   DISULFID        115..130
FT                   /evidence="ECO:0000250"
FT   DISULFID        140..177
FT                   /evidence="ECO:0000250"
FT   DISULFID        194
FT                   /note="Interchain (with C-60 in C8-gamma chain)"
FT                   /evidence="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