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Database: UniProt
Entry: W5MF43_LEPOC
LinkDB: W5MF43_LEPOC
Original site: W5MF43_LEPOC 
ID   W5MF43_LEPOC            Unreviewed;       239 AA.
AC   W5MF43;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Complement C1q B chain {ECO:0000313|Ensembl:ENSLOCP00000007002.1};
GN   Name=C1QB {ECO:0000313|Ensembl:ENSLOCP00000007002.1};
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:ENSLOCP00000007002.1, 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:ENSLOCP00000007002.1}
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; AHAT01018478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5MF43; -.
DR   STRING; 7918.ENSLOCP00000007002; -.
DR   Ensembl; ENSLOCT00000007010.1; ENSLOCP00000007002.1; ENSLOCG00000005797.1.
DR   eggNOG; ENOG502S2X9; Eukaryota.
DR   GeneTree; ENSGT00940000161091; -.
DR   HOGENOM; CLU_001074_0_2_1; -.
DR   InParanoid; W5MF43; -.
DR   OMA; CDTSEGF; -.
DR   Proteomes; UP000018468; Linkage group LG26.
DR   Bgee; ENSLOCG00000005797; Expressed in heart and 13 other cell types or tissues.
DR   Gene3D; 2.60.120.40; -; 1.
DR   InterPro; IPR001073; C1q_dom.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   PANTHER; PTHR15427:SF18; COMPLEMENT C1Q SUBCOMPONENT SUBUNIT B; 1.
DR   PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1.
DR   Pfam; PF00386; C1q; 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   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..239
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004867705"
FT   DOMAIN          111..239
FT                   /note="C1q"
FT                   /evidence="ECO:0000259|PROSITE:PS50871"
FT   REGION          39..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   239 AA;  24678 MW;  A39364569AD8FF31 CRC64;
     QACDIMACKA VVLVVVLTSA VTLSAADTCS KYRGYPGIPG KPGAHGAHGK DGVPGEKGEK
     GDDGRLVKGQ KGEPGPMGSP GRAGLQGDPG EQGLPGPAGP KGAMGSPVAI NTTEKSVFSF
     SKTSNMPPRS YQPIRFERAN LAGDPLPGGR FTCEAKGAYY FTYHVTARGP VCIGIHKGAD
     KVVVFCDSVY QGYLVTSGSV VLQLDKGDVV SLQPTEKNSV LGSDGADSIF TGFLLFPMK
//
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