C1QT9_MOUSE
ID C1QT9_MOUSE Reviewed; 333 AA.
AC Q4ZJN1; Q8BZS3;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Complement C1q and tumor necrosis factor-related protein 9;
DE Flags: Precursor;
GN Name=C1qtnf9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue;
RX PubMed=15231994; DOI=10.1073/pnas.0403760101;
RA Wong G.W., Wang J., Hug C., Tsao T.S., Lodish H.F.;
RT "A family of Acrp30/adiponectin structural and functional paralogs.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10302-10307(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
RN [4]
RP FUNCTION, INTERACTION WITH ADIPOQ, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, GLYCOSYLATION AT LYS-73 AND LYS-127, HYDROXYLATION AT PRO-31;
RP PRO-34; PRO-40; PRO-58; PRO-61; PRO-64; LYS-73; PRO-76; PRO-115; LYS-127;
RP PRO-151; PRO-160 AND PRO-175, MUTAGENESIS OF CYS-23, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18787108; DOI=10.1096/fj.08-114991;
RA Wong G.W., Krawczyk S.A., Kitidis-Mitrokostas C., Ge G., Spooner E.,
RA Hug C., Gimeno R., Lodish H.F.;
RT "Identification and characterization of CTRP9, a novel secreted
RT glycoprotein, from adipose tissue that reduces serum glucose in mice and
RT forms heterotrimers with adiponectin.";
RL FASEB J. 23:241-258(2009).
CC -!- FUNCTION: Probable adipokine. Activates AMPK, AKT, and p44/42 MAPK
CC signaling pathways. {ECO:0000269|PubMed:18787108}.
CC -!- SUBUNIT: Multimers (predominantly trimers). Interacts with ADIPOQ via
CC the C1q domain to form a heterotrimeric complex.
CC {ECO:0000269|PubMed:18787108}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18787108}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4ZJN1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4ZJN1-2; Sequence=VSP_026218;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in adipose tissue. Females
CC express higher levels than males. {ECO:0000269|PubMed:18787108}.
CC -!- PTM: The isomeric forms of the hydroxylated amino acids could not be
CC determined in the mass-spectrometric methods reported in
CC PubMed:18787108 but are assumed on the basis of their occurrence in
CC collagen-like domains. {ECO:0000269|PubMed:18787108}.
CC -!- MISCELLANEOUS: Overexpression of CTRP9 in obese (ob/ob) mice
CC significantly lowered serum glucose levels.
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DR EMBL; DQ002401; AAY21933.1; -; mRNA.
DR EMBL; AK033673; BAC28422.1; -; mRNA.
DR EMBL; BC115632; AAI15633.1; -; mRNA.
DR EMBL; BC115633; AAI15634.1; -; mRNA.
DR CCDS; CCDS27178.1; -. [Q4ZJN1-1]
DR RefSeq; NP_898998.2; NM_183175.4. [Q4ZJN1-1]
DR RefSeq; XP_006519046.1; XM_006518983.2. [Q4ZJN1-2]
DR RefSeq; XP_006519047.1; XM_006518984.2. [Q4ZJN1-2]
DR AlphaFoldDB; Q4ZJN1; -.
DR SMR; Q4ZJN1; -.
DR IntAct; Q4ZJN1; 1.
DR STRING; 10090.ENSMUSP00000025940; -.
DR GlyGen; Q4ZJN1; 2 sites.
DR PhosphoSitePlus; Q4ZJN1; -.
DR MaxQB; Q4ZJN1; -.
DR PaxDb; Q4ZJN1; -.
DR PRIDE; Q4ZJN1; -.
DR ProteomicsDB; 265400; -. [Q4ZJN1-1]
DR ProteomicsDB; 265401; -. [Q4ZJN1-2]
DR TopDownProteomics; Q4ZJN1-1; -. [Q4ZJN1-1]
DR DNASU; 239126; -.
DR Ensembl; ENSMUST00000025940; ENSMUSP00000025940; ENSMUSG00000071347. [Q4ZJN1-1]
DR GeneID; 239126; -.
DR KEGG; mmu:239126; -.
DR UCSC; uc007uff.2; mouse. [Q4ZJN1-1]
DR CTD; 338872; -.
DR MGI; MGI:3045252; C1qtnf9.
DR VEuPathDB; HostDB:ENSMUSG00000071347; -.
DR eggNOG; ENOG502QVBU; Eukaryota.
DR GeneTree; ENSGT00940000154936; -.
DR HOGENOM; CLU_001074_0_0_1; -.
DR InParanoid; Q4ZJN1; -.
DR OMA; SVGYKGQ; -.
DR OrthoDB; 1258047at2759; -.
DR PhylomeDB; Q4ZJN1; -.
DR TreeFam; TF334029; -.
DR BioGRID-ORCS; 239126; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q4ZJN1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q4ZJN1; protein.
DR Bgee; ENSMUSG00000071347; Expressed in interventricular septum and 85 other tissues.
DR Genevisible; Q4ZJN1; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005179; F:hormone activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0097009; P:energy homeostasis; IDA:MGI.
DR GO; GO:0019395; P:fatty acid oxidation; IDA:MGI.
DR GO; GO:0045792; P:negative regulation of cell size; IDA:MGI.
DR GO; GO:1900078; P:positive regulation of cellular response to insulin stimulus; IDA:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:MGI.
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 Alternative splicing; Collagen; Glycoprotein; Hormone; Hydroxylation;
KW Reference proteome; Repeat; 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 9"
FT /id="PRO_0000291752"
FT DOMAIN 24..82
FT /note="Collagen-like 1"
FT DOMAIN 84..130
FT /note="Collagen-like 2"
FT DOMAIN 134..193
FT /note="Collagen-like 3"
FT DOMAIN 197..333
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 22..194
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 66..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:18787108"
FT MOD_RES 34
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:18787108"
FT MOD_RES 40
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:18787108"
FT MOD_RES 58
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:18787108"
FT MOD_RES 61
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:18787108"
FT MOD_RES 64
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:18787108"
FT MOD_RES 73
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:18787108"
FT MOD_RES 76
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:18787108"
FT MOD_RES 115
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:18787108"
FT MOD_RES 127
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:18787108"
FT MOD_RES 151
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:18787108"
FT MOD_RES 160
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:18787108"
FT MOD_RES 175
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:18787108"
FT CARBOHYD 73
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000269|PubMed:18787108"
FT CARBOHYD 127
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000269|PubMed:18787108"
FT VAR_SEQ 1..138
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026218"
FT MUTAGEN 23
FT /note="C->A: No change in the interaction with ADIPOQ."
FT /evidence="ECO:0000269|PubMed:18787108"
SQ SEQUENCE 333 AA; 34566 MW; 7F68661C0A6841F3 CRC64;
MRIWWLLLVM GACTRSVFSQ DTCRQGHSGI PGNPGHNGLP GRDGRDGAKG DKGDAGEPGH
PGGPGKDGIR GEKGEPGADG RVEAKGIKGD PGSRGSPGKH GPKGSIGPTG EQGLPGETGP
QGQKGDKGEV GPTGPEGLMG STGPLGPKGL PGPMGPIGKP GPRGEAGPMG PQGEPGVRGM
RGWKGDRGEK GKVGEAPLVP KSAFTVGLTV ISKFPPPDAP IKFDKILYNE LNHYNVATGK
FTCHVAGVYY FTYHITVFSR NVQVSLVKNG VKVLHTKDSY MSSEDQASGG IVQELKLGDE
VWMQVTGGER FNGLFADEDD DTTFTGFLLF SSS
