ID A0A3M0ITK3_HIRRU Unreviewed; 243 AA.
AC A0A3M0ITK3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Complement C1q subcomponent subunit A {ECO:0000256|ARBA:ARBA00013456};
GN ORFNames=DUI87_31978 {ECO:0000313|EMBL:RMB91748.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMB91748.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMB91748.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMB91748.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMB91748.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) 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}.
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:RMB91748.1}.
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DR EMBL; QRBI01000235; RMB91748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0ITK3; -.
DR STRING; 333673.A0A3M0ITK3; -.
DR Proteomes; UP000269221; 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:UP000269221};
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..243
FT /note="Complement C1q subcomponent subunit A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018040290"
FT DOMAIN 110..243
FT /note="C1q"
FT /evidence="ECO:0000259|PROSITE:PS50871"
FT REGION 29..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 243 AA; 24526 MW; E74ECE7EFFD41F70 CRC64;
MQPGFLLAAS TLAAVLGMAL LEDGVCKAPD GKNGSPGAPG RDGRPGQKGE MGEPGRSGLS
VNTRGPRGDT GEPGTPGFPG MRGPPGAPGP MGMAGVPGPP GQKGKASDVL EHPRPAFSAS
RLSPPLTGTT VVFDRVITNQ ENSYSPQTGK FTCGIPGLYY FTFQVVSNGD LCLSIAKNGV
RVVSFCDNNS QGILQVNSGS SVLSLAVGDQ VSLVTNPGGS NSIYSGSDVD SVFSGFLVSP
VTA
//
