C1T9B_HUMAN
ID C1T9B_HUMAN Reviewed; 333 AA.
AC B2RNN3; A2A3T6; B9EH31; Q0VGC5; Q5VX65; Q5VX66; Q8IUU4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Complement C1q and tumor necrosis factor-related protein 9B;
DE AltName: Full=C1q/TNF-related protein 9B;
DE Short=CTRP9B;
DE AltName: Full=Complement C1q and tumor necrosis factor-related protein 9-like;
DE Flags: Precursor;
GN Name=C1QTNF9B;
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 [LARGE SCALE GENOMIC DNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
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 [3]
RP IDENTIFICATION, SUBUNIT, SUBCELLULAR LOCATION, 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).
CC -!- FUNCTION: Probable adipokine. Activates AMPK, AKT, and p44/42 MAPK
CC signaling pathways. {ECO:0000250|UniProtKB:Q4ZJN1}.
CC -!- SUBUNIT: Interacts with CTRP9A and ADIPOQ. Forms heterotrimers and
CC heterooligomeric complexes with CTRP9A. {ECO:0000269|PubMed:19666007}.
CC -!- INTERACTION:
CC B2RNN3; P0C862: C1QTNF9; NbExp=3; IntAct=EBI-10828035, EBI-5654640;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19666007}.
CC Note=Heteromeric complex formation with CTRP9A or ADIPOQ is required
CC for secretion, otherwise, it is retained in the endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B2RNN3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B2RNN3-2; Sequence=VSP_035153, VSP_035154;
CC -!- TISSUE SPECIFICITY: Expressed at low levels. Not expressed in adipose
CC tissues. {ECO:0000269|PubMed:19666007}.
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DR EMBL; AL445985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110413; AAI10414.1; -; mRNA.
DR EMBL; BC137004; AAI37005.1; -; mRNA.
DR EMBL; BC137006; AAI37007.1; -; mRNA.
DR CCDS; CCDS31947.1; -. [B2RNN3-1]
DR RefSeq; NP_001007538.1; NM_001007537.2. [B2RNN3-1]
DR RefSeq; XP_011533372.1; XM_011535070.2.
DR AlphaFoldDB; B2RNN3; -.
DR SMR; B2RNN3; -.
DR BioGRID; 132501; 65.
DR IntAct; B2RNN3; 2.
DR STRING; 9606.ENSP00000371572; -.
DR iPTMnet; B2RNN3; -.
DR PhosphoSitePlus; B2RNN3; -.
DR BioMuta; C1QTNF9B; -.
DR jPOST; B2RNN3; -.
DR MassIVE; B2RNN3; -.
DR MaxQB; B2RNN3; -.
DR PaxDb; B2RNN3; -.
DR PeptideAtlas; B2RNN3; -.
DR PRIDE; B2RNN3; -.
DR ProteomicsDB; 3442; -. [B2RNN3-1]
DR Antibodypedia; 78005; 37 antibodies from 9 providers.
DR DNASU; 387911; -.
DR Ensembl; ENST00000382137.7; ENSP00000371572.3; ENSG00000205863.11. [B2RNN3-1]
DR GeneID; 387911; -.
DR KEGG; hsa:387911; -.
DR UCSC; uc001uoz.3; human. [B2RNN3-1]
DR CTD; 387911; -.
DR DisGeNET; 387911; -.
DR GeneCards; C1QTNF9B; -.
DR HGNC; HGNC:34072; C1QTNF9B.
DR HPA; ENSG00000205863; Tissue enhanced (brain, skin, testis).
DR MIM; 614148; gene.
DR neXtProt; NX_B2RNN3; -.
DR OpenTargets; ENSG00000205863; -.
DR VEuPathDB; HostDB:ENSG00000205863; -.
DR eggNOG; ENOG502QVBU; Eukaryota.
DR GeneTree; ENSGT00940000154936; -.
DR HOGENOM; CLU_001074_0_0_1; -.
DR InParanoid; B2RNN3; -.
DR OMA; AVGKFTC; -.
DR OrthoDB; 1258047at2759; -.
DR PhylomeDB; B2RNN3; -.
DR TreeFam; TF334029; -.
DR PathwayCommons; B2RNN3; -.
DR SignaLink; B2RNN3; -.
DR BioGRID-ORCS; 387911; 14 hits in 987 CRISPR screens.
DR ChiTaRS; C1QTNF9B; human.
DR GenomeRNAi; 387911; -.
DR Pharos; B2RNN3; Tdark.
DR PRO; PR:B2RNN3; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; B2RNN3; protein.
DR Bgee; ENSG00000205863; Expressed in skin of leg and 87 other tissues.
DR ExpressionAtlas; B2RNN3; baseline and differential.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 Alternative splicing; Collagen; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..333
FT /note="Complement C1q and tumor necrosis factor-related
FT protein 9B"
FT /id="PRO_0000348424"
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..189
FT /note="Disordered"
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 VAR_SEQ 89..99
FT /note="GDQGSRGSPGK -> EMFRCLWSKME (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035153"
FT VAR_SEQ 100..333
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035154"
SQ SEQUENCE 333 AA; 34713 MW; A15F3F7546938A70 CRC64;
MRIWWLLLAI EICTGNINSQ DTCRQGHPGI PGNPGHNGLP GRDGRDGAKG DKGDAGEPGC
PGSPGKDGTS GEKGERGADG KVEAKGIKGD QGSRGSPGKH GPKGLAGPMG EKGLRGETGP
QGQKGNKGDV GPTGPEGPRG NIGPLGPTGL PGPMGPIGKP GPKGEAGPTG PQGEPGVRGI
RGWKGDRGEK GKIGETLVLP KSAFTVGLTV LSKFPSSDVP IKFDKILYNE FNHYDTAVGK
FTCHIAGVYY FTYHITVFSR NVQVSLVKNG VKILHTRDAY VSSEDQASGS IVLQLKLGDE
MWLQVTGGER FNGLFADEDD DTTFTGFLLF SSQ