ID C3YIK1_BRAFL Unreviewed; 949 AA.
AC C3YIK1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=MACPF domain-containing protein {ECO:0000259|PROSITE:PS51412};
GN ORFNames=BRAFLDRAFT_105963 {ECO:0000313|EMBL:EEN59934.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN59934.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN59934.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN59934.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC {ECO:0000256|ARBA:ARBA00009214}.
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DR EMBL; GG666515; EEN59934.1; -; Genomic_DNA.
DR RefSeq; XP_002603923.1; XM_002603877.1.
DR AlphaFoldDB; C3YIK1; -.
DR STRING; 7739.C3YIK1; -.
DR eggNOG; ENOG502QPIM; Eukaryota.
DR InParanoid; C3YIK1; -.
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: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; 3.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
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 InterPro; IPR044004; TSP1_spondin_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR45742; COMPLEMENT COMPONENT C6; 1.
DR PANTHER; PTHR45742:SF8; MACPF DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF21195; C8A_B_C6_EGF-like; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF01823; MACPF; 1.
DR Pfam; PF19028; TSP1_spondin; 1.
DR Pfam; PF00090; TSP_1; 2.
DR PRINTS; PR00764; COMPLEMENTC9.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00457; MACPF; 1.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
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; 3.
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 {ECO:0000256|SAM:Phobius};
KW Membrane attack complex {ECO:0000256|ARBA:ARBA00023058};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..554
FT /note="MACPF"
FT /evidence="ECO:0000259|PROSITE:PS51412"
FT REGION 713..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..896
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 175..187
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 182..200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 194..209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 949 AA; 104434 MW; 3F20DA69241735EA CRC64;
MSIVSKNRLL CCYEEFEKHQ DMRCMFRLLV LAAVIAVLTV PSDGWRRRRR RRAPPPPPPP
VHCQVGGWSP WSTCSRSCEG GNQARTRAIT RHPAHGGRAC PTLRQSRACN LQTCPIDCIV
GTFGNWTRCD PCERKEERDR LVLRPTQFKG HGCPADLHET RPCVTNEPCP PKDSCRENEF
TCQNMRCIPQ LQTCNGDNDC GDFSDERQCD RIFDVCDGQD FDAIPNIAFA GSGYNILSGE
VAGKVLENRL YGGTCNTVYS GDHGKSFRLP ENLQNYRFQV LADNSFAATA YNSAEEYYRE
TRSNSQRNVK VGGSGSFFVI KASGGVSHSQ SRMTHEVIES AQKIDSKYFK VVNTVELAQF
KMRRNGLNPS DIFLRRMKDL PVYYNYLDYS FLIEDFGTHY FSSGSLGGQY EYVYRYSRAD
LSHSGLTEEE QKSCLSAEAK ASFFSFSGSS SGSRCKENAL SQRNSGSFTL SASESFSHVK
GGSSESAGQL AFANGPNPQK YEAWIQDVKR NPAIISYEIT PISELLVGIP YADIKRRNME
KALVEYLHFY HSCKCNSCQN NGQAIMIGTE CVCVCKAGTY GISCELGTQV DNVGTAVHGN
WACWGSWAPC SKSCGSGQRV RRRTCSNPTP RNNGQTCPGQ DSETETCNSQ PCLTQCQPGY
YSRTGYAPCR ACPAGAFQTL PGQKSCLDCP RGTTTGRSAS VLFEHCVEDD ESEDTHSVGV
HGSRGSHGHA GSAEGSRPGS RPGSRPDRTG GFGSRGTNAS YSDGASAVSS GSAGRGVVET
DRVRDTVRIP EEEDEETVRI PDEDRVRDTV RIPEEDEDTV RISDEDRVRD TVRIPGEDRV
RDTVRIPYEE EDDPTEPPST NPRRHHHGSS SASSGGGRQH AEEDPEPADG NERSTESPTE
SESAAAALPA RPGAETSSTD ADTSPADPDD VISSVLDTWR NNDDDYYDY
//
