ID A0A3L8S2M0_CHLGU Unreviewed; 1610 AA.
AC A0A3L8S2M0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Complement C5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=DV515_00013339 {ECO:0000313|EMBL:RLV93890.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV93890.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV93890.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV93890.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV93890.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV93890.1}.
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DR EMBL; QUSF01000088; RLV93890.1; -; Genomic_DNA.
DR STRING; 44316.ENSEGOP00005016045; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00017; ANATO; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.120.1540; -; 2.
DR Gene3D; 2.60.40.1930; -; 3.
DR Gene3D; 2.60.40.1940; -; 1.
DR Gene3D; 6.20.50.160; -; 1.
DR Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR Gene3D; 1.20.91.20; Anaphylotoxins (complement system); 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR InterPro; IPR041425; C3/4/5_MG1.
DR InterPro; IPR048843; C5_CUB.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11412:SF83; COMPLEMENT C5; 1.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF21309; C5_CUB; 1.
DR Pfam; PF17790; MG1; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SMART; SM00104; ANATO; 1.
DR SMART; SM00643; C345C; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF47686; Anaphylotoxins (complement system); 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS50189; NTR; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1610
FT /note="Complement C5"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018097550"
FT DOMAIN 698..733
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 1466..1610
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
SQ SEQUENCE 1610 AA; 180885 MW; 9227C5293FC53FC9 CRC64;
MTILIYFIVL LFSGTTFSQE KTYVLTAPKI FRAGASEKIV VQAFGYEKEF PVNIALKSFP
DKLVVYSSAQ ISLTPANKFQ DAVTLTIQPA DLPRTDASDK YLYLEAVSPH FTRFKKIPVS
YDNGFLFIHT DKPVYTPDQS VKVRVYSLNE ELQPARRETV LTFVVLGKYL MARLPLKSPL
KDEDSPIDKN NLYGIWKIKA KYKKDFVTSA VAKFEVKEYA MPSFSITIEP ESNFISSDKF
ENFRIVVKAS YFSNKKLPSA DVFLRFGIIE ESEKRMMPQA MHVTRIENGV AEINFNSKRA
ASSIGFDSLE ALDGSYLYIV ASVLESMGGL SGEVEFTGVR FAVSPYKLSL VATPLFVKPG
LPFFIKVQVK DTMDDFVGNV PVTVTAKSFS EQMDETWLIS EGSESGRRKT SISDGTALFV
VNIPPNSKML EFQVKTADPH LSDENQASKS YEAKAYSSLS QSYLYIDWAS NHKTLEVGDV
ININVYPQSH YIDKIHHYSY LITSKGKTVS FGTQERIKDL EYEHLTFQIT QEMVPSARLI
VYYIVMGEGA AELVADSVWL NVEQKCGNSL DIKLQSSKAT LKPAEVVSLT MKTQSNSFVA
LSSIDKAIYG VTGRRKRAME KIMLQLEKSD LGCGAGGGQN NIAVFRMAGL TFLTNANADD
SEEADEPCKE VLRTKRSDFK EKILKEVAKY RDPEARQCCM AGVKAYPVSE TCRERAQRIR
RRQRCISAFT DCCEFANKLR LEEPNKLLIL ARMHFEALLE LDEAQVRSYF PESWLWEVHQ
VSSRSKTLSV TLPDSLTTWE VQGVGISDKG ICVAAPVEIQ VVKDIFLSIY VPYSVVRGEQ
IELKGTVYNH KASAIKFCVQ IAAGNGVCTF GDSASARSRM QSCKLKNLDA GSSSAVTFRI
LPLELGLHTV NFTLLTLRNS EIVVKTLRVV PEGIRKELHA GFTLDPQGVY GSIKRRQEFR
YKVPLNLVPK TQIDRSVSVK GHLMGEVIAT VLSPKGLQML SSLPRGSAEA ELMSIAPVFY
VFHYLEESDN WHLLGPRTLS SRTQMRRKIK EGIVSISSFR NADCSYSMWK NGQASTWLTA
FALRILGQVN QYIELDQKSV CDSLLWLIDN CQMSDGSFNE FSNYEPVKLQ GTLPREAKEK
SLYLTAFSII GIDKSMKICP TQKIHDARSR AGDYLVQNVQ LAQSPFTVAI AAYALALLEP
NHHAARAAFS ALRREAFVTG DPPIYRFWKD AFKTQDQPTP NSVTAQMDTI NALEALTEYS
LLVKRLHLDM DVKVAYKNGG PLNLFKLTED NFVGRTMEVR TVYNTIGTSE EFCNFELKIV
PKRDDGSFLV IYGRVFTDGG VRKKYDGEWE GLQYRPSARE PRSGSAHAVM DIGLLASGVD
QLIADYEIKD GHVLLQIDSV PAHKFLCVGF RISELFRVGM LNPATFTVYE YHAPDKRCTI
LYNPYGNEKL VRLCEGDECK CMEAECGKVQ ERLGRSVTAE SRREAACQED TAYVYKVNIL
SRSEEGFFVK YSANLLDLYK RGQAFAQKNN EITFVKKKTC TEVELSPGEQ YLIMGKEALK
ISIGYSFKFQ YPLDSSTWIE WWPSNTACAS CQEFLNTMDD FAEDLLISGC
//
