ID F1S788_PIG Unreviewed; 589 AA.
AC F1S788;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 3.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Complement C8 alpha chain {ECO:0000313|Ensembl:ENSSSCP00000004152.3};
GN Name=C8A {ECO:0000313|Ensembl:ENSSSCP00000004152.3,
GN ECO:0000313|VGNC:VGNC:86076};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000004152.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000004152.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000004152.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000004152.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Secreted
CC {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 RefSeq; NP_001090919.2; NM_001097450.2.
DR AlphaFoldDB; F1S788; -.
DR SMR; F1S788; -.
DR STRING; 9823.ENSSSCP00000004152; -.
DR PaxDb; 9823-ENSSSCP00000004152; -.
DR PeptideAtlas; F1S788; -.
DR Ensembl; ENSSSCT00000004247.4; ENSSSCP00000004152.3; ENSSSCG00000003835.4.
DR GeneID; 100037953; -.
DR KEGG; ssc:100037953; -.
DR VGNC; VGNC:86076; C8A.
DR eggNOG; ENOG502QT87; Eukaryota.
DR GeneTree; ENSGT00940000160126; -.
DR HOGENOM; CLU_032453_1_0_1; -.
DR InParanoid; F1S788; -.
DR OMA; CQPGVTI; -.
DR OrthoDB; 4572257at2759; -.
DR TreeFam; TF330498; -.
DR Reactome; R-SSC-166665; Terminal pathway of complement.
DR Reactome; R-SSC-977606; Regulation of Complement cascade.
DR Proteomes; UP000008227; Chromosome 6.
DR Bgee; ENSSSCG00000003835; Expressed in liver and 12 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005579; C:membrane attack complex; IBA:GO_Central.
DR GO; GO:0006956; P:complement activation; IBA:GO_Central.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR InterPro; IPR048831; C8A_B_C6_EGF-like.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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:SF1; COMPLEMENT COMPONENT C8 ALPHA 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; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 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; PS00279; MACPF_1; 1.
DR PROSITE; PS51412; MACPF_2; 1.
DR PROSITE; PS50092; TSP1; 2.
PE 1: Evidence at protein level;
KW Complement alternate pathway {ECO:0000256|ARBA:ARBA00023162};
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 {ECO:0000256|ARBA:ARBA00022452};
KW Membrane attack complex {ECO:0000256|ARBA:ARBA00023058};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1S788};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022452};
KW Transmembrane beta strand {ECO:0000256|ARBA:ARBA00022452}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..589
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011682977"
FT DOMAIN 139..503
FT /note="MACPF"
FT /evidence="ECO:0000259|PROSITE:PS51412"
FT DISULFID 99..111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 118..133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 589 AA; 66061 MW; 44F6CA2A0F722C23 CRC64;
MLAVAFFILS LMTCQPGVTI QEKVNRRVSR AVLSSTPTAV SCQLSNWAEW TECFPCQDKK
YRYRSLLQPN KFGGAICSGN VWDQASCHSP TECLRQAQCG QDFQCKETGR CLKRHLVCNG
DRDCLDGSDE DDCEDVRIFE DDCSQYDPIP GSERATLGYN ILTQEETQSV YDARYYGGQC
ETVYNGEWRE LRYDSACERL YYGDDEKYFR KPYNFLKYHF EALADSKFSS ESYDDANDLL
KKVKNEKSVS AGVTVGIGPT GSPFTANVGL SGSRESAFLN KLSKYNEKKY SFIRIFTKVQ
TASFKMRRDN IMLDEVMLQS LMELPEQYNY GMYAKFIDDY GTHYITSGSM GGVYEYILVL
NKENMTKSGV TSDDVTSCFG GSFGIDYDYT DNLQITGSLS GKHCKKLGGG HREDEESNMA
VEDIISRVRG GSSGWGGGLT QNGSIITYRA WGRSLKYNPA VIDFEMKPIY EILRHTNLGP
LEAKCQNLRR ALDQYLMEFN ACRCGPCFNN GEPILVGTSC RCQCPVGYQG LACEQMKSEG
AKADGRWSCW SSWSACRLGT QERRRECNNP APQNGGASCS GHIVQTQAC
//
