C1QT8_HUMAN
ID C1QT8_HUMAN Reviewed; 252 AA.
AC P60827; B7U178;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Complement C1q tumor necrosis factor-related protein 8;
DE AltName: Full=C1q/TNF-related protein 8;
DE Short=CTRP8 {ECO:0000303|PubMed:19666007};
DE Flags: Precursor;
GN Name=C1QTNF8 {ECO:0000312|HGNC:HGNC:31374};
GN ORFNames=UNQ5829/PRO19648 {ECO:0000303|PubMed:12975309};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH C1QL1,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Hippocampus;
RX PubMed=19666007; DOI=10.1016/j.bbrc.2009.08.014;
RA Peterson J.M., Wei Z., Wong G.W.;
RT "CTRP8 and CTRP9B are novel proteins that hetero-oligomerize with C1q/TNF
RT family members.";
RL Biochem. Biophys. Res. Commun. 388:360-365(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH RXFP1, AND
RP FUNCTION.
RX PubMed=24014093; DOI=10.1002/path.4257;
RA Glogowska A., Kunanuvat U., Stetefeld J., Patel T.R., Thanasupawat T.,
RA Krcek J., Weber E., Wong G.W., Del Bigio M.R., Hoang-Vu C.,
RA Hombach-Klonisch S., Klonisch T.;
RT "C1q-tumour necrosis factor-related protein 8 (CTRP8) is a novel
RT interaction partner of relaxin receptor RXFP1 in human brain cancer
RT cells.";
RL J. Pathol. 231:466-479(2013).
CC -!- FUNCTION: May play a role as ligand of RXFP1.
CC {ECO:0000269|PubMed:24014093}.
CC -!- SUBUNIT: Homotrimer (PubMed:19666007). Forms heteromeric complexes with
CC C1QL1 (PubMed:19666007). Interacts with RXFP1 (PubMed:24014093).
CC {ECO:0000269|PubMed:19666007, ECO:0000269|PubMed:24014093}.
CC -!- INTERACTION:
CC P60827; O75973: C1QL1; NbExp=2; IntAct=EBI-10826404, EBI-10826419;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19666007,
CC ECO:0000269|PubMed:24014093}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in lung and testis
CC (PubMed:19666007). Expressed in astrocytes (PubMed:24014093).
CC {ECO:0000269|PubMed:19666007, ECO:0000269|PubMed:24014093}.
CC -!- PTM: Not N-glycosylated. {ECO:0000269|PubMed:19666007}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ89191.1; Type=Miscellaneous discrepancy; Note=Contains a 30 bp insertion which does not match the genome.; Evidence={ECO:0000305};
CC Sequence=ACJ46463.1; Type=Miscellaneous discrepancy; Note=Contains a 30 bp insertion which does not match the genome.; Evidence={ECO:0000305};
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DR EMBL; FJ422561; ACJ46463.1; ALT_SEQ; mRNA.
DR EMBL; AY358832; AAQ89191.1; ALT_SEQ; mRNA.
DR EMBL; AC009041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS32358.1; -.
DR RefSeq; NP_997302.2; NM_207419.3.
DR RefSeq; XP_011520785.1; XM_011522483.2.
DR AlphaFoldDB; P60827; -.
DR SMR; P60827; -.
DR BioGRID; 133653; 95.
DR IntAct; P60827; 1.
DR STRING; 9606.ENSP00000330426; -.
DR iPTMnet; P60827; -.
DR PhosphoSitePlus; P60827; -.
DR BioMuta; C1QTNF8; -.
DR DMDM; 290457629; -.
DR MassIVE; P60827; -.
DR PaxDb; P60827; -.
DR PeptideAtlas; P60827; -.
DR PRIDE; P60827; -.
DR TopDownProteomics; P60827; -.
DR Antibodypedia; 62521; 36 antibodies from 16 providers.
DR DNASU; 390664; -.
DR Ensembl; ENST00000328449.6; ENSP00000330426.5; ENSG00000184471.9.
DR GeneID; 390664; -.
DR KEGG; hsa:390664; -.
DR MANE-Select; ENST00000328449.6; ENSP00000330426.5; NM_207419.3; NP_997302.2.
DR UCSC; uc010uuw.2; human.
DR CTD; 390664; -.
DR DisGeNET; 390664; -.
DR GeneCards; C1QTNF8; -.
DR HGNC; HGNC:31374; C1QTNF8.
DR HPA; ENSG00000184471; Group enriched (brain, fallopian tube, pituitary gland).
DR MIM; 614147; gene.
DR neXtProt; NX_P60827; -.
DR OpenTargets; ENSG00000184471; -.
DR PharmGKB; PA134914298; -.
DR VEuPathDB; HostDB:ENSG00000184471; -.
DR eggNOG; ENOG502QT5D; Eukaryota.
DR GeneTree; ENSGT00940000163090; -.
DR HOGENOM; CLU_001074_3_0_1; -.
DR InParanoid; P60827; -.
DR OMA; HLIKPAV; -.
DR OrthoDB; 1136568at2759; -.
DR PhylomeDB; P60827; -.
DR TreeFam; TF329591; -.
DR PathwayCommons; P60827; -.
DR SignaLink; P60827; -.
DR BioGRID-ORCS; 390664; 11 hits in 1058 CRISPR screens.
DR GenomeRNAi; 390664; -.
DR Pharos; P60827; Tdark.
DR PRO; PR:P60827; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P60827; protein.
DR Bgee; ENSG00000184471; Expressed in right uterine tube and 36 other tissues.
DR ExpressionAtlas; P60827; baseline and differential.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:2000147; P:positive regulation of cell motility; IDA:UniProtKB.
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 Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 1.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW Collagen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..252
FT /note="Complement C1q tumor necrosis factor-related protein
FT 8"
FT /id="PRO_0000003541"
FT DOMAIN 69..111
FT /note="Collagen-like"
FT DOMAIN 112..252
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 74..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 252 AA; 27685 MW; 42F987B300C9C1BC CRC64;
MAAPALLLLA LLLPVGAWPG LPRRPCVHCC RPAWPPGPYA RVSDRDLWRG DLWRGLPRVR
PTIDIEILKG EKGEAGVRGR AGRSGKEGPP GARGLQGRRG QKGQVGPPGA ACRRAYAAFS
VGRREGLHSS DHFQAVPFDT ELVNLDGAFD LAAGRFLCTV PGVYFLSLNV HTWNYKETYL
HIMLNRRPAA VLYAQPSERS VMQAQSLMLL LAAGDAVWVR MFQRDRDNAI YGEHGDLYIT
FSGHLVKPAA EL
