ID W5MUJ5_LEPOC Unreviewed; 286 AA.
AC W5MUJ5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=C1q and TNF related 7 {ECO:0000313|Ensembl:ENSLOCP00000012054.1};
GN Name=C1QTNF7 {ECO:0000313|Ensembl:ENSLOCP00000012054.1};
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:ENSLOCP00000012054.1, 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:ENSLOCP00000012054.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR EMBL; AHAT01001116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006629653.1; XM_006629590.2.
DR RefSeq; XP_015200272.1; XM_015344786.1.
DR AlphaFoldDB; W5MUJ5; -.
DR Ensembl; ENSLOCT00000012075.1; ENSLOCP00000012054.1; ENSLOCG00000009865.1.
DR GeneID; 102693607; -.
DR KEGG; loc:102693607; -.
DR CTD; 114905; -.
DR GeneTree; ENSGT00940000159588; -.
DR HOGENOM; CLU_001074_0_3_1; -.
DR OrthoDB; 3013859at2759; -.
DR Proteomes; UP000018468; Linkage group LG4.
DR Bgee; ENSLOCG00000009865; Expressed in zone of skin and 7 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:SF24; COMPLEMENT C1Q TUMOR NECROSIS FACTOR-RELATED PROTEIN 7; 1.
DR PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 2.
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..286
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004866802"
FT DOMAIN 141..277
FT /note="C1q"
FT /evidence="ECO:0000259|PROSITE:PS50871"
FT REGION 34..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 286 AA; 30195 MW; 2C462431EBDABAB6 CRC64;
MLVLIGIISV FNCISGQTLE SKWKGNPPRY ICSVPGLPGP PGHPGSNGAA GPHGRIGLPG
RDGRDGRKGE KGEKGDPGLR GKAGPAGKIG GRGDRGPVGK RGPNGTGGEK GFVGPAGPPG
EKGDKGNRGI PGKPGICKCG SLVPKSAFSV GITTSYPVEL TPIKFNKVLF NEGEHYNPNT
GKFICAYPGI YYFSYDITLA NKHLAIGLVQ NGQYRIKTFD ANTGNHDVAS GSTVMYLNPE
DEVWLEIFFT DQNGLFSDPS WADSLFSGFL LYADTNYLDA LSEDYA
//