ID A0A091RHK3_9GRUI Unreviewed; 236 AA.
AC A0A091RHK3;
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=N332_05386 {ECO:0000313|EMBL:KFQ39001.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ39001.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ39001.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ39001.1};
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; KK817998; KFQ39001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RHK3; -.
DR Proteomes; UP000053369; 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:UP000053369};
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_5001880794"
FT DOMAIN 104..236
FT /note="C1q"
FT /evidence="ECO:0000259|PROSITE:PS50871"
FT REGION 25..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ39001.1"
FT NON_TER 236
FT /evidence="ECO:0000313|EMBL:KFQ39001.1"
SQ SEQUENCE 236 AA; 24466 MW; 01BAB60B706EDA2D CRC64;
LASSTLAAML GMALLQDGVC RAPDGKDGFP GVPGLDGRPG QKGDVGEPGK SAQRTGIKGL
KGDTGEPGLP GIPGNRGYHG LHGPPGLAGQ AGPKGEKGVG VNIQKQPRPA FSASRRSPQF
TGRTVVFDNI ITNQESSYSP QTGEFTCSIP GLYYFVFQVV SNGDLCLSIT KNRERVVSFC
DHNSRNILQV NSGSSVLSLA MGDKVSISTG PVGGSTIYSG SEADSVFSGF MLFPQM
//
