TAFA5_MOUSE
ID TAFA5_MOUSE Reviewed; 132 AA.
AC Q91WE9; Q8C1V6;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Chemokine-like protein TAFA-5;
DE Flags: Precursor;
GN Name=Tafa5; Synonyms=Fam19a5 {ECO:0000312|MGI:MGI:2146182};
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 2).
RC STRAIN=C57BL/6J;
RX PubMed=15028294; DOI=10.1016/j.ygeno.2003.10.006;
RA Tom Tang Y., Emtage P., Funk W.D., Hu T., Arterburn M., Park E.E., Rupp F.;
RT "TAFA: a novel secreted family with conserved cysteine residues and
RT restricted expression in the brain.";
RL Genomics 83:727-734(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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 2).
RC STRAIN=FVB/N; TISSUE=Kidney;
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.
RX PubMed=29138422; DOI=10.1038/s41598-017-15586-0;
RA Park M.Y., Kim H.S., Lee M., Park B., Lee H.Y., Cho E.B., Seong J.Y.,
RA Bae Y.S.;
RT "FAM19A5, a brain-specific chemokine, inhibits RANKL-induced osteoclast
RT formation through formyl peptide receptor 2.";
RL Sci. Rep. 7:15575-15575(2017).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=29453251; DOI=10.1161/circulationaha.117.032398;
RA Wang Y., Chen D., Zhang Y., Wang P., Zheng C., Zhang S., Yu B., Zhang L.,
RA Zhao G., Ma B., Cai Z., Xie N., Huang S., Liu Z., Mo X., Guan Y., Wang X.,
RA Fu Y., Ma D., Wang Y., Kong W.;
RT "Novel Adipokine, FAM19A5, Inhibits Neointima Formation After Injury
RT Through Sphingosine-1-Phosphate Receptor 2.";
RL Circulation 138:48-63(2018).
CC -!- FUNCTION: Acts as a chemokine-like protein by regulating cell
CC proliferation and migration through activation of G protein-coupled
CC receptors (GPCRs), such as S1PR2 and FPR2 (PubMed:29453251,
CC PubMed:29138422). Stimulates chemotactic migration of macrophages
CC mediated by the MAPK3/ERK1 and AKT1 pathway (PubMed:29138422). Blocks
CC TNFSF11/RANKL-induced osteoclast formation from macrophages by
CC inhibiting up-regulation of osteoclast fusogenic and differentiation
CC genes (PubMed:29138422). Stimulation of macrophage migration and
CC inhibition of osteoclast formation is mediated through the GPCR FPR2
CC (PubMed:29138422). Acts as an adipokine by negatively regulating
CC vascular smooth muscle cell (VSMC) proliferation and migration in
CC response to platelet-derived growth factor stimulation via GPCR S1PR2
CC and G protein GNA12/GNA13-transmitted RHOA signaling (By similarity).
CC Inhibits injury-induced cell proliferation and neointima formation in
CC the femoral arteries (PubMed:29453251). {ECO:0000250|UniProtKB:M0R7X9,
CC ECO:0000269|PubMed:29138422, ECO:0000269|PubMed:29453251}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29453251}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91WE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91WE9-2; Sequence=VSP_016069;
CC -!- TISSUE SPECIFICITY: Expressed in the subcutaneous, brown, epididymal
CC and perirenal adipose tissue (at protein level).
CC {ECO:0000269|PubMed:29453251}.
CC -!- INDUCTION: Repressed in epididymal adipose tissue of diet-induced obese
CC mice or leptin receptor-deficient mice. {ECO:0000269|PubMed:29453251}.
CC -!- MISCELLANEOUS: [Isoform 2]: Contains a predicted signal peptide at
CC positions 1-25. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TAFA family. {ECO:0000305}.
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DR EMBL; AY325124; AAP92416.1; -; mRNA.
DR EMBL; AK090194; BAC41130.1; -; mRNA.
DR EMBL; BC015306; AAH15306.1; -; mRNA.
DR CCDS; CCDS49693.1; -. [Q91WE9-2]
DR CCDS; CCDS88823.1; -. [Q91WE9-1]
DR RefSeq; NP_001239239.1; NM_001252310.1. [Q91WE9-1]
DR RefSeq; NP_598857.1; NM_134096.2. [Q91WE9-2]
DR AlphaFoldDB; Q91WE9; -.
DR STRING; 10090.ENSMUSP00000064808; -.
DR GlyGen; Q91WE9; 1 site.
DR PhosphoSitePlus; Q91WE9; -.
DR PeptideAtlas; Q91WE9; -.
DR PRIDE; Q91WE9; -.
DR ProteomicsDB; 275726; -. [Q91WE9-1]
DR ProteomicsDB; 275727; -. [Q91WE9-2]
DR Antibodypedia; 67212; 19 antibodies from 13 providers.
DR Ensembl; ENSMUST00000068088; ENSMUSP00000064808; ENSMUSG00000054863. [Q91WE9-2]
DR Ensembl; ENSMUST00000230414; ENSMUSP00000155322; ENSMUSG00000054863. [Q91WE9-1]
DR GeneID; 106014; -.
DR KEGG; mmu:106014; -.
DR UCSC; uc007xee.1; mouse. [Q91WE9-1]
DR UCSC; uc007xef.1; mouse. [Q91WE9-2]
DR CTD; 25817; -.
DR MGI; MGI:2146182; Tafa5.
DR VEuPathDB; HostDB:ENSMUSG00000054863; -.
DR GeneTree; ENSGT00940000160682; -.
DR HOGENOM; CLU_126078_5_1_1; -.
DR InParanoid; Q91WE9; -.
DR OMA; DANAWPR; -.
DR OrthoDB; 1417753at2759; -.
DR PhylomeDB; Q91WE9; -.
DR TreeFam; TF331749; -.
DR BioGRID-ORCS; 106014; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Tafa5; mouse.
DR PRO; PR:Q91WE9; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q91WE9; protein.
DR Bgee; ENSMUSG00000054863; Expressed in superior colliculus and 203 other tissues.
DR Genevisible; Q91WE9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0048018; F:receptor ligand activity; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IDA:MGI.
DR GO; GO:0061044; P:negative regulation of vascular wound healing; IDA:MGI.
DR InterPro; IPR020350; Chemokine-like_TAFA.
DR InterPro; IPR040329; TAFA-5.
DR PANTHER; PTHR31878; PTHR31878; 1.
DR Pfam; PF12020; TAFA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytokine; Glycoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..43
FT /evidence="ECO:0000250|UniProtKB:Q7Z5A7"
FT CHAIN 44..132
FT /note="Chemokine-like protein TAFA-5"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5A7"
FT /id="PRO_0000042733"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..38
FT /note="MAPSPRTSSRQDATALPSMSSTFWAFMILASLLIAYCS -> MQLLKALWAL
FT AGAALCCFLVLVIHAQFLKEG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15028294,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016069"
SQ SEQUENCE 132 AA; 14331 MW; 16BFF4357D3BA466 CRC64;
MAPSPRTSSR QDATALPSMS STFWAFMILA SLLIAYCSQL AAGTCEIVTL DRDSSQPRRT
IARQTARCAC RKGQIAGTTR ARPACVDARI IKTKQWCDML PCLEGEGCDL LINRSGWTCT
QPGGRIKTTT VS
