ID A0A091JMR6_EGRGA Unreviewed; 236 AA.
AC A0A091JMR6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Complement C1q subcomponent subunit A {ECO:0000256|ARBA:ARBA00013456};
DE Flags: Fragment;
GN ORFNames=Z169_00496 {ECO:0000313|EMBL:KFP21050.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP21050.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP21050.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP21050.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1,
CC the first component of the serum complement system. The collagen-like
CC regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2)
CC proenzyme complex, and efficient activation of C1 takes place on
CC interaction of the globular heads of C1q with the Fc regions of IgG or
CC IgM antibody present in immune complexes.
CC {ECO:0000256|ARBA:ARBA00002781}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; KK502172; KFP21050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091JMR6; -.
DR STRING; 188379.A0A091JMR6; -.
DR Proteomes; UP000053119; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR15427:SF26; COMPLEMENT C1Q SUBCOMPONENT SUBUNIT A; 1.
DR PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 1.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; TNF-like; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053119};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..236
FT /note="Complement C1q subcomponent subunit A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001875561"
FT DOMAIN 104..236
FT /note="C1q"
FT /evidence="ECO:0000259|PROSITE:PS50871"
FT REGION 22..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP21050.1"
FT NON_TER 236
FT /evidence="ECO:0000313|EMBL:KFP21050.1"
SQ SEQUENCE 236 AA; 24791 MW; 73F48DF758DC41E9 CRC64;
LATSTLAAVL GMALLEEEVC KAPDGKDGFP GVPGLNGRPG QKGDTGEPGK STQRTGIRGL
KGDAGEPGHP GNPGNQGYHG SQGPPGPPGQ PGPKGQKGKA GNILEQPRPA FSASRKSPRS
MGRRVVFDNI ITNQENSYSP QTGEFTCRIP GLYYFAYQVV SIGDLCLSIT KNEEPMVSFC
DHNSRDILQV NSGSSVLSLS KGDRVSVSTD PARSSMIYSG SEADSVFSGF MLFPQM
//
