ID   A0A218UM21_9PASE        Unreviewed;       660 AA.
AC   A0A218UM21;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Complement C1q subcomponent subunit A {ECO:0000256|ARBA:ARBA00013456};
GN   Name=C1QB {ECO:0000313|EMBL:OWK54621.1};
GN   ORFNames=RLOC_00013244 {ECO:0000313|EMBL:OWK54621.1};
OS   Lonchura striata domestica (Bengalese finch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Lonchura.
OX   NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK54621.1, ECO:0000313|Proteomes:UP000197619};
RN   [1] {ECO:0000313|EMBL:OWK54621.1, ECO:0000313|Proteomes:UP000197619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=White83orange57 {ECO:0000313|EMBL:OWK54621.1};
RA   Colquitt B.M., Brainard M.S.;
RT   "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL   Submitted (MAY-2017) 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:OWK54621.1}.
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DR   EMBL; MUZQ01000232; OWK54621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218UM21; -.
DR   STRING; 299123.ENSLSDP00000021220; -.
DR   Proteomes; UP000197619; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.60.120.40; -; 3.
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; 3.
DR   Pfam; PF01391; Collagen; 1.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 3.
DR   SUPFAM; SSF49842; TNF-like; 3.
DR   PROSITE; PS50871; C1Q; 3.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000197619};
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..660
FT                   /note="Complement C1q subcomponent subunit A"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012826756"
FT   DOMAIN          36..170
FT                   /note="C1q"
FT                   /evidence="ECO:0000259|PROSITE:PS50871"
FT   DOMAIN          276..408
FT                   /note="C1q"
FT                   /evidence="ECO:0000259|PROSITE:PS50871"
FT   DOMAIN          524..660
FT                   /note="C1q"
FT                   /evidence="ECO:0000259|PROSITE:PS50871"
FT   REGION          30..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   660 AA;  70407 MW;  D1FFF2243B082E17 CRC64;
     MQPGVLLAAS TLAAVLGVAL LEDGVCRAPD GKNGSPGVPG RDGRPGQKGD VGEPGTTVVF
     DRIITNQENS YSPQTGKFTC RIPGLYYFAF QVVSSGDLCL SITRNGLGVV SFCDNSRGLL
     QVNSGSSVLS LAVGDQVSLT TNPAQGSSIY SGSEADSVFT DKERSDSSLS LALQMQKDRE
     EWSVQSELTL PGGKRNIWDR KTKMEKRFWE QLYLALTLLL LDLGSAVTVE NPHNCYGAPG
     LPGMPGKPGI PGLPGAMGIP GEAGDAGPPG IPGSYKQKQQ SAFSVTRQTS QYPLKNVPVV
     FNNVITNTNH DYNTTTGKFT CRLPGVYYFI FHSSHTANLC VILHKNQSRI ASFCDHKTNT
     MQVSSGGSLL HLAAADEVWL GVNDYNGMDT GVLDTAPSPH LMNKEIKESP RHRSVLPQMW
     IMWAMLICLA GGQPASDTLC RTYGTIPGIP GLPGQPGSNG RDGENGPKGE QGPPGQSGAE
     RGEKGDPGLP GLPGKVGPSG IPGPVGVPGY RGMPGPMGEP GGYKVTFKSA FSAARSISSY
     PRREQPVRFD RIITNENGHY ENRYGRFTCR VPGIYYFTYH VTSRGNLCLS IKKGQGASRG
     DRVVTFCDFV QNSFQVTTGG VVLKVAMNES VWLEPTEKNS LVGLEGSDSV FSGFLIVPEA
//