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   24-JAN-2024, entry version 111.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyCosmos; P0C862; 2 sites, No reported glycans.
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; 9606-ENSP00000371503; -.
DR   PeptideAtlas; P0C862; -.
DR   ProteomicsDB; 52399; -.
DR   Antibodypedia; 34999; 84 antibodies from 18 providers.
DR   DNASU; 338872; -.
DR   Ensembl; ENST00000332018.5; 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   AGR; HGNC:28732; -.
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; HTKDSYM; -.
DR   OrthoDB; 4224143at2759; -.
DR   PhylomeDB; P0C862; -.
DR   TreeFam; TF334029; -.
DR   PathwayCommons; P0C862; -.
DR   SignaLink; P0C862; -.
DR   BioGRID-ORCS; 338872; 13 hits in 1045 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 male germ line stem cell (sensu Vertebrata) in testis and 84 other cell types or tissues.
DR   ExpressionAtlas; P0C862; baseline and differential.
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   PANTHER; PTHR15427:SF21; COMPLEMENT C1Q AND TUMOR NECROSIS FACTOR-RELATED PROTEIN 9A; 1.
DR   PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF01391; Collagen; 3.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; TNF-like; 1.
DR   PROSITE; PS50871; C1Q; 1.
DR   Genevisible; P0C862; HS.
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
//