C1T9A_HUMAN
ID C1T9A_HUMAN Reviewed; 333 AA.
AC P0C862; A2A3T6; Q0VGC5; Q5VX65; Q5VX66; Q8IUU4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Complement C1q and tumor necrosis factor-related protein 9A;
DE AltName: Full=Complement C1q and tumor necrosis factor-related protein 9;
DE Flags: Precursor;
GN Name=C1QTNF9; Synonyms=C1QTNF9A; ORFNames=UNQ6503/PRO21380;
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], AND VARIANT VAL-219.
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], AND VARIANTS VAL-219 AND
RP MET-301.
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-219.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Probable adipokine. Activates AMPK, AKT, and p44/42 MAPK
CC signaling pathways. {ECO:0000250|UniProtKB:Q4ZJN1}.
CC -!- SUBUNIT: Multimers (predominantly trimers). Interacts with ADIPOQ via
CC the C1q domain to form a heterotrimeric complex (By similarity).
CC Interacts with CTRP9B. Forms heterotrimers and heterooligomeric
CC complexes with CTRP9B. {ECO:0000250, ECO:0000269|PubMed:19666007}.
CC -!- INTERACTION:
CC P0C862; P0C862: C1QTNF9; NbExp=2; IntAct=EBI-5654640, EBI-5654640;
CC P0C862; B2RNN3: C1QTNF9B; NbExp=3; IntAct=EBI-5654640, EBI-10828035;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in adipose tissue.
CC {ECO:0000269|PubMed:19666007}.
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DR EMBL; AY358145; AAQ88512.1; -; mRNA.
DR EMBL; AL359736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040438; AAH40438.1; -; mRNA.
DR CCDS; CCDS9306.1; -.
DR RefSeq; NP_001290066.1; NM_001303137.1.
DR RefSeq; NP_001290067.1; NM_001303138.1.
DR RefSeq; NP_848635.2; NM_178540.4.
DR AlphaFoldDB; P0C862; -.
DR SMR; P0C862; -.
DR BioGRID; 130809; 36.
DR IntAct; P0C862; 31.
DR STRING; 9606.ENSP00000371503; -.
DR TCDB; 8.A.94.1.2; the adiponectin (adiponectin) family.
DR GlyGen; P0C862; 2 sites.
DR iPTMnet; P0C862; -.
DR PhosphoSitePlus; P0C862; -.
DR BioMuta; C1QTNF9; -.
DR DMDM; 205686199; -.
DR jPOST; P0C862; -.
DR MassIVE; P0C862; -.
DR MaxQB; P0C862; -.
DR PaxDb; P0C862; -.
DR PeptideAtlas; P0C862; -.
DR PRIDE; P0C862; -.
DR ProteomicsDB; 52399; -.
DR Antibodypedia; 34999; 63 antibodies from 17 providers.
DR DNASU; 338872; -.
DR Ensembl; ENST00000332018.4; ENSP00000333737.4; ENSG00000240654.6.
DR Ensembl; ENST00000382071.6; ENSP00000371503.2; ENSG00000240654.6.
DR GeneID; 338872; -.
DR KEGG; hsa:338872; -.
DR MANE-Select; ENST00000332018.5; ENSP00000333737.4; NM_178540.5; NP_848635.2.
DR UCSC; uc001upj.4; human.
DR CTD; 338872; -.
DR DisGeNET; 338872; -.
DR GeneCards; C1QTNF9; -.
DR HGNC; HGNC:28732; C1QTNF9.
DR HPA; ENSG00000240654; Tissue enhanced (skeletal).
DR MIM; 614285; gene.
DR neXtProt; NX_P0C862; -.
DR OpenTargets; ENSG00000240654; -.
DR PharmGKB; PA145008937; -.
DR VEuPathDB; HostDB:ENSG00000240654; -.
DR eggNOG; ENOG502QVBU; Eukaryota.
DR GeneTree; ENSGT00940000154936; -.
DR HOGENOM; CLU_001074_0_0_1; -.
DR InParanoid; P0C862; -.
DR OMA; SVGYKGQ; -.
DR OrthoDB; 1258047at2759; -.
DR PhylomeDB; P0C862; -.
DR TreeFam; TF334029; -.
DR PathwayCommons; P0C862; -.
DR SignaLink; P0C862; -.
DR BioGRID-ORCS; 338872; 13 hits in 986 CRISPR screens.
DR ChiTaRS; C1QTNF9; human.
DR GenomeRNAi; 338872; -.
DR Pharos; P0C862; Tbio.
DR PRO; PR:P0C862; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P0C862; protein.
DR Bgee; ENSG00000240654; Expressed in apex of heart and 84 other tissues.
DR ExpressionAtlas; P0C862; baseline and differential.
DR Genevisible; P0C862; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; 3.
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; Glycoprotein; Hormone; Hydroxylation; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..333
FT /note="Complement C1q and tumor necrosis factor-related
FT protein 9A"
FT /id="PRO_0000291751"
FT DOMAIN 24..82
FT /note="Collagen-like 1"
FT DOMAIN 95..154
FT /note="Collagen-like 2"
FT DOMAIN 155..191
FT /note="Collagen-like 3"
FT DOMAIN 197..333
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 24..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 34
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 58
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 127
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 151
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 160
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 175
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT CARBOHYD 73
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 127
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT VARIANT 6
FT /note="L -> F (in dbSNP:rs1974332)"
FT /id="VAR_059148"
FT VARIANT 219
FT /note="M -> V (in dbSNP:rs3751357)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15057823, ECO:0000269|PubMed:15489334"
FT /id="VAR_032840"
FT VARIANT 301
FT /note="V -> M (in dbSNP:rs4589405)"
FT /evidence="ECO:0000269|PubMed:15057823"
FT /id="VAR_032841"
SQ SEQUENCE 333 AA; 34681 MW; F2EBF303B034E307 CRC64;
MRIWWLLLAI EICTGNINSQ DTCRQGHPGI PGNPGHNGLP GRDGRDGAKG DKGDAGEPGR
PGSPGKDGTS GEKGERGADG KVEAKGIKGD QGSRGSPGKH GPKGLAGPMG EKGLRGETGP
QGQKGNKGDV GPTGPEGPRG NIGPLGPTGL PGPMGPIGKP GPKGEAGPTG PQGEPGVRGI
RGWKGDRGEK GKIGETLVLP KSAFTVGLTV LSKFPSSDMP IKFDKILYNE FNHYDTAAGK
FTCHIAGVYY FTYHITVFSR NVQVSLVKNG VKILHTKDAY MSSEDQASGG IVLQLKLGDE
VWLQVTGGER FNGLFADEDD DTTFTGFLLF SSP
