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Database: UniProt
Entry: F1SMI8_PIG
LinkDB: F1SMI8_PIG
Original site: F1SMI8_PIG 
ID   F1SMI8_PIG              Unreviewed;       880 AA.
AC   F1SMI8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 4.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=Complement component C6 {ECO:0000256|ARBA:ARBA00018265};
GN   Name=C6 {ECO:0000313|Ensembl:ENSSSCP00000017868.4,
GN   ECO:0000313|VGNC:VGNC:86050};
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:ENSSSCP00000017868.4, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000017868.4, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000017868.4,
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:ENSSSCP00000017868.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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   -!- SUBUNIT: Component of the membrane attack complex (MAC). MAC assembly
CC       is initiated by proteolytic cleavage of C5 into C5a and C5b. C5b binds
CC       sequentially C6, C7, C8 and 12-14 copies of the pore-forming subunit
CC       C9. {ECO:0000256|ARBA:ARBA00025836}.
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:PRU00302}.
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DR   AlphaFoldDB; F1SMI8; -.
DR   PeptideAtlas; F1SMI8; -.
DR   Ensembl; ENSSSCT00000018364.5; ENSSSCP00000017868.4; ENSSSCG00000016861.5.
DR   VGNC; VGNC:86050; C6.
DR   eggNOG; ENOG502QPIM; Eukaryota.
DR   GeneTree; ENSGT00940000156814; -.
DR   HOGENOM; CLU_014082_0_0_1; -.
DR   TreeFam; TF330498; -.
DR   ChiTaRS; C6; pig.
DR   Proteomes; UP000008227; Chromosome 16.
DR   Bgee; ENSSSCG00000016861; Expressed in liver and 21 other cell types or tissues.
DR   ExpressionAtlas; F1SMI8; baseline and differential.
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; cd00033; CCP; 2.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 3.30.60.30; -; 2.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR   InterPro; IPR048828; C6_KAZAL.
DR   InterPro; IPR048831; C8A_B_C6_EGF-like.
DR   InterPro; IPR003884; FacI_MAC.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR001862; MAC_perforin.
DR   InterPro; IPR020864; MACPF.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR45742; COMPLEMENT COMPONENT C6; 1.
DR   PANTHER; PTHR45742:SF4; COMPLEMENT COMPONENT C6; 1.
DR   Pfam; PF21288; C6_KAZAL; 1.
DR   Pfam; PF21195; C8A_B_C6_EGF-like; 1.
DR   Pfam; PF01823; MACPF; 1.
DR   Pfam; PF00084; Sushi; 2.
DR   Pfam; PF00090; TSP_1; 2.
DR   PRINTS; PR00764; COMPLEMENTC9.
DR   SMART; SM00032; CCP; 2.
DR   SMART; SM00057; FIMAC; 2.
DR   SMART; SM00457; MACPF; 1.
DR   SMART; SM00209; TSP1; 3.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 2.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS51412; MACPF_2; 1.
DR   PROSITE; PS50923; SUSHI; 2.
DR   PROSITE; PS50092; TSP1; 3.
PE   1: Evidence at protein level;
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:PRU00302}; 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   Proteomics identification {ECO:0007829|PeptideAtlas:F1SMI8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW   ProRule:PRU00302}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..880
FT                   /note="Complement component C6"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5023895665"
FT   DOMAIN          161..478
FT                   /note="MACPF"
FT                   /evidence="ECO:0000259|PROSITE:PS51412"
FT   DOMAIN          587..646
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          647..708
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          730..784
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   REGION          543..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        617..644
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   880 AA;  99193 MW;  62808FEE41EF94DC CRC64;
     MDIWVVSMFW LFGLIDKSQA CFCDHYPWTQ WSSCSKTCNS GTQTRQRQIT INQYYLDNFC
     DRLCTKQETR ECNWQTCPIN CLLGDYGPWS DCDPCVEKQF KVRSILHPNQ FGGQPCTEPL
     MTFRPCIPSK LCKIEEVDCK NKFRCDSGRC IASKLECNGE NDSVCSRKYN PIPSVQLMGA
     GFHILAGEPR GEVLGNSFTG GICKTVKSSK ASNPFRVPAN LENVQTKEDD FETDFYEDLI
     PLENSKDQQA TGFGQEKSSF HVPIFYSSKK SQTSSHNSAF KQAIQASHKK DSSFIRIHKV
     IKVLNFTMKT KDLHRIFDDF GTHYFTSGSL GGVYDLLYQF SNEELKNSGL TQEEAKNCIR
     IETKKRYFIV TKTKVEHRCT TNRMSEKYEG SFLQGSEKSI SLVKGGRSEY AAALAWEKGS
     SGPGEKTYSE WLESVKENPA VIDFEVRLLV RNIPCAVTRR NNLRRAFREY AAKFDPCQCA
     PCPNNGRPVL SGTECLCVCQ SGTYGDNCER RAPDYKSNAV DGNWGCWSSW STCDATYKRS
     RTRECNNPAP RQGGKPCEGR GGRRNTPCIG DDEDMKEIDL PEIESDSGCP QPVPPENGFI
     RNEKTLYSVG EDVEIVCLTG FKTVGYQYFR CLPDRTWRRG DVECQRTDCL LPVVPEVLKL
     SPFQRLYKIG DSIELSCPKG FVIAGPSRYT CSGDSWTPPI SSSLTCEQDF LTRLKGHCQP
     GQKQLGSECV CLSPEEDCSH HSEDLCVLDT DSNHYFTSSA CKFLAEKCLN NQQLQFLHIG
     SCQDGPQLEW GLERIKLSSS STKNESCGYD TCYSWEKCSA TTSKCICLLP FQCLKGGYQH
     YCVKMGSSTT TRTMNICEVG AIRCALRKME ILYPGRCRSN
//
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