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Database: UniProt
Entry: W5MSB8_LEPOC
LinkDB: W5MSB8_LEPOC
Original site: W5MSB8_LEPOC 
ID   W5MSB8_LEPOC            Unreviewed;       505 AA.
AC   W5MSB8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Complement C1q subcomponent subunit A {ECO:0000256|ARBA:ARBA00013456};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000011277.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000011277.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR   EMBL; AHAT01012921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006638028.2; XM_006637965.2.
DR   AlphaFoldDB; W5MSB8; -.
DR   STRING; 7918.ENSLOCP00000011277; -.
DR   Ensembl; ENSLOCT00000011293.1; ENSLOCP00000011277.1; ENSLOCG00000009248.1.
DR   GeneID; 102694436; -.
DR   KEGG; loc:102694436; -.
DR   eggNOG; ENOG502RRBA; Eukaryota.
DR   GeneTree; ENSGT00940000155435; -.
DR   HOGENOM; CLU_001074_0_0_1; -.
DR   InParanoid; W5MSB8; -.
DR   OMA; IPFFCIC; -.
DR   OrthoDB; 5361526at2759; -.
DR   Proteomes; UP000018468; Linkage group LG14.
DR   Bgee; ENSLOCG00000009248; Expressed in zone of skin and 1 other cell type or tissue.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
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; 4.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; TNF-like; 1.
DR   PROSITE; PS50871; C1Q; 1.
PE   4: Predicted;
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..505
FT                   /note="Complement C1q subcomponent subunit A"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004866583"
FT   DOMAIN          340..473
FT                   /note="C1q"
FT                   /evidence="ECO:0000259|PROSITE:PS50871"
FT   REGION          34..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..55
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   505 AA;  52913 MW;  3C445547A0C7DA93 CRC64;
     MTHCTTGLTM KTPLLLLCLQ LLWPLCGAMI TPHPPPERGG PEKPPNPPPN QDYHPMNPAD
     QPHIYSPQRF PLTENDPFPG NISSRSFVPD MSQTVGLEPD MSYCQMLLES PVPPPIESVP
     WFCLCMNCKG TMGPKGDRGE RGLPGHPGSP GPRGFSGFRG RPGFVGRQGL KGQKGDDGEK
     GDQGVSGFRG AKGERGLKGD KGDQGLDGIP GLPGPQGEPG QCPVVCQGDL GLPGMTGLPG
     PAGVRGPPGA DGVPGHPGQK GDMGSIGAPG PQGTQGPKGE HGAEGQCNCT DGEKGAHGEV
     GPQGPPGNAG HPGAKGEAGL PGTKGEKGDE GLRGVPGPCS PTIQSGFSAA LDSIYPAPNR
     PVPFGKVIYN LQGHFDPFNG IYMAPVNGTY VFSYQLVVFS KVLKVGLFLN FKPVVKTTEP
     SDLGSASQMV VLQLSRGDRV WLQVKDTSTN GMYASSDSTS TFSGYLLYPD SCEMPLSRDF
     PTYEEGDYSW GDEDEPPTRH STTPP
//
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