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Database: UniProt
Entry: A0A093SVJ2_PHACA
LinkDB: A0A093SVJ2_PHACA
Original site: A0A093SVJ2_PHACA 
ID   A0A093SVJ2_PHACA        Unreviewed;       588 AA.
AC   A0A093SVJ2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Complement component C8 beta chain {ECO:0000256|ARBA:ARBA00013949};
DE   AltName: Full=Complement component 8 subunit beta {ECO:0000256|ARBA:ARBA00031383};
GN   ORFNames=N336_07291 {ECO:0000313|EMBL:KFW86564.1};
OS   Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC   Phalacrocorax.
OX   NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW86564.1, ECO:0000313|Proteomes:UP000053238};
RN   [1] {ECO:0000313|EMBL:KFW86564.1, ECO:0000313|Proteomes:UP000053238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW86564.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002409}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC       {ECO:0000256|ARBA:ARBA00009214}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR   EMBL; KL418482; KFW86564.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093SVJ2; -.
DR   Proteomes; UP000053238; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005579; C:membrane attack complex; IEA:UniProtKB-KW.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 2.
DR   InterPro; IPR048831; C8A_B_C6_EGF-like.
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; COMPLEMENT COMPONENT C6; 1.
DR   PANTHER; PTHR45742:SF5; COMPLEMENT COMPONENT C8 BETA CHAIN; 1.
DR   Pfam; PF21195; C8A_B_C6_EGF-like; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF01823; MACPF; 1.
DR   Pfam; PF00090; TSP_1; 2.
DR   PRINTS; PR00764; COMPLEMENTC9.
DR   PRINTS; PR01705; TSP1REPEAT.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00457; MACPF; 1.
DR   SMART; SM00209; TSP1; 2.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
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   3: Inferred from homology;
KW   Complement pathway {ECO:0000256|ARBA:ARBA00022875};
KW   Cytolysis {ECO:0000256|ARBA:ARBA00022852};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Membrane attack complex {ECO:0000256|ARBA:ARBA00023058};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053238};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          157..502
FT                   /note="MACPF"
FT                   /evidence="ECO:0000259|PROSITE:PS51412"
FT   REGION          566..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        139..154
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   588 AA;  66244 MW;  48D89DF6719481D1 CRC64;
     MSTTCTAFAL YPVKLLLLYA VFGILTIHCF GGEKESLDLS GTNRSVANSR WARSVSNLPQ
     PRDCTLSAWS SWSKCDPCQK KRYRFAHLEQ PSQFNGDPCD YSDKETEDCV TNNPCRNKVR
     CEGFLCAVTG RCITRRLLCN GDDDCGDQSD EKNCKKVFKK CDQKMEQYWG IENLAKGLNI
     FTNNLEGLVL DHRYYAGGCS PHYIMDTRFR KPYNVESYTP ETKGKYEFTM TEYDSYSNYE
     SSVLEAKASQ SSFSFGIKIP RVFELGYSSN DNRFKKFIQR MKRFSSTSSK FIHARSELAV
     AIYKLKPRGL MLHYEFLQRL HQLPLEYSYG EYRELYRDYG THYITEATVG GIYEYTLVMN
     SNELQKAGYS LSDVQKCAQY SFNIGASIVV SLKLGITEAG CKSLLKEIGD STSKKQYVED
     FIVLVRGGAS EHITALAYKD LPTAALMQEW GDAVQYNPEI IKLKAEPLYQ LVTPTDFANA
     MAIKENLRRA LDEFQLETSS CRCAPCHSNG IPFLQGTKCE CLCPLGYSGT ACEISKRKDA
     AVNGNWGCWA SWSPCSGGQR TRRRQCNNPS PQNGGSLCSG PDAETVTC
//
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