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Database: UniProt
Entry: A0A3Q2WSA3_HAPBU
LinkDB: A0A3Q2WSA3_HAPBU
Original site: A0A3Q2WSA3_HAPBU 
ID   A0A3Q2WSA3_HAPBU        Unreviewed;       930 AA.
AC   A0A3Q2WSA3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Complement component C6 {ECO:0000256|ARBA:ARBA00018265};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000028640.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000028640.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; A0A3Q2WSA3; -.
DR   STRING; 8153.ENSHBUP00000028640; -.
DR   Ensembl; ENSHBUT00000017991.1; ENSHBUP00000028640.1; ENSHBUG00000012538.1.
DR   GeneTree; ENSGT00940000156804; -.
DR   Proteomes; UP000264840; 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:0048856; P:anatomical structure development; IEA:UniProt.
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; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 2.
DR   InterPro; IPR048825; C7_KAZAL.
DR   InterPro; IPR048831; C8A_B_C6_EGF-like.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR003884; FacI_MAC.
DR   InterPro; IPR040729; Kazal_3.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR001862; MAC_perforin.
DR   InterPro; IPR020864; MACPF.
DR   InterPro; IPR020863; MACPF_CS.
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:SF2; COMPLEMENT COMPONENT C7; 1.
DR   Pfam; PF21330; C7_KAZAL; 1.
DR   Pfam; PF21195; C8A_B_C6_EGF-like; 1.
DR   Pfam; PF18434; Kazal_3; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF01823; MACPF; 1.
DR   Pfam; PF00084; Sushi; 2.
DR   Pfam; PF00090; TSP_1; 2.
DR   PRINTS; PR00764; COMPLEMENTC9.
DR   PRINTS; PR01705; TSP1REPEAT.
DR   SMART; SM00032; CCP; 2.
DR   SMART; SM00057; FIMAC; 2.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00457; MACPF; 1.
DR   SMART; SM00209; TSP1; 2.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 2.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS00279; MACPF_1; 1.
DR   PROSITE; PS51412; MACPF_2; 1.
DR   PROSITE; PS50923; SUSHI; 2.
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:PRU00302}; 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|SAM:Phobius};
KW   Membrane attack complex {ECO:0000256|ARBA:ARBA00023058};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW   ProRule:PRU00302}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          225..544
FT                   /note="MACPF"
FT                   /evidence="ECO:0000259|PROSITE:PS51412"
FT   DOMAIN          657..716
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          717..779
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          879..930
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DISULFID        193..211
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        205..220
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        687..714
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        719..762
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   930 AA;  103057 MW;  49D358AEF151F626 CRC64;
     MTSGLSLLRA VMVFMLLLFL YLFTECGMSW QRCRRTPRCV SVGSSCDVFT LWRSKEWRHL
     PVESENSRKT VRRRLPDTLL AGYMSLSAIV LVQRRRLNSE EHIMKLNLAA ALALSLAFIS
     PVCCQQPVNC RWGPYGDWSE CDGCTSTKVR TRHVEVFAQF GGVPCSGEAT QTQTCVPQKR
     CPLEAGCGDR FRCTSGQCIS QSLVCNGDQD CEDGLDERNC GEDNSLATCD LDKTPPNSDF
     TGRGYDVLTG KLRAGVINTR SFGGQCRKVF SGDHKVLYRL PHNILRYNFE VTVDNDESDE
     SYESSWSYMQ HIQSNAFLVH DRRTFHKEVT NNKAYRLIIL KNKVELAQFQ NSAPQYLTLA
     EGFWKALSLL PLTYDYSAYH QVLQKYGTHY LSEGSLGGEY QALLELDRQA LASTSTTDID
     YQRCWRKVKR RFFRKKVKTV CEKLTKSVSS SHGSSVNKMP IKVNVFGGDI GLIGALSVLD
     LENPEANGEV YDNWASSVKD FPEVINQKLR PLYELVKEVQ CAGLKKLHLK RATEEYLAEE
     HPCHCQPCQN NGQPLLTGSE CRCVCRPGTS GRACENGAVI GEQPGVIHGS WSCWSSWGSC
     SGGQRSRTRS CNNPAPSRGG QHCTGLQVEQ KPCDDPDIQY LQMMEPQCFS LSVTPPKTCG
     PPPNLRNGFV QNPRDFYLVG NTVEYSCVDW YYLSGNAVAT CAENQKWTTG TRVCKSSTCG
     IPSLNNLVVA TPTKQAYEIG DSVSLSCPEG SVIDREVSEI ICTPSLQWSP SPAVAHCTAA
     PTAPSPPSGL TCKLWETLGK NECVCKMPNQ CTTSLQLCAT LRANRNMVLD VCKLGALRCM
     GRNFVLTSDS DCRWPEKKFT SCEDCQPGTI CQEAERKCVC RNASECPKDS TPLCVSSGDG
     STHVTTTECE AGARRCAGEQ VNVISIDPCQ
//
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