ARXS2_MOUSE
ID ARXS2_MOUSE Reviewed; 180 AA.
AC C0HK80; B1AUR7; Q8BK31; Q9D365; Q9D6F2;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Adipocyte-related X-chromosome expressed sequence 2 {ECO:0000303|PubMed:21177646};
GN Name=Arxes2 {ECO:0000303|PubMed:21177646, ECO:0000312|MGI:MGI:1924226};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Hippocampus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION.
RX PubMed=21177646; DOI=10.1093/nar/gkq1289;
RA Prokesch A., Bogner-Strauss J.G., Hackl H., Rieder D., Neuhold C.,
RA Walenta E., Krogsdam A., Scheideler M., Papak C., Wong W.C., Vinson C.,
RA Eisenhaber F., Trajanoski Z.;
RT "Arxes: retrotransposed genes required for adipogenesis.";
RL Nucleic Acids Res. 39:3224-3239(2011).
CC -!- FUNCTION: Plays a role in adipogenesis. {ECO:0000269|PubMed:21177646}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21177646}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in epididymal white and brown
CC adipose tissue with low levels in heart. {ECO:0000269|PubMed:21177646}.
CC -!- DEVELOPMENTAL STAGE: Strongly up-regulated during adipogenesis.
CC {ECO:0000269|PubMed:21177646}.
CC -!- INDUCTION: By the PPARG agonist rosiglitazone.
CC {ECO:0000269|PubMed:21177646}.
CC -!- MISCELLANEOUS: Arxes1 and Arxes2 appear to have arisen by
CC retrotransposition of the signal peptidase Spcs3 followed by a
CC segmental duplication event. {ECO:0000303|PubMed:21177646}.
CC -!- SIMILARITY: Belongs to the SPCS3 family. {ECO:0000305}.
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DR EMBL; AK013740; BAB28979.1; -; mRNA.
DR EMBL; AK077432; BAC36797.1; -; mRNA.
DR EMBL; AL671914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466616; EDL23842.1; -; Genomic_DNA.
DR EMBL; CH466616; EDL23843.1; -; Genomic_DNA.
DR CCDS; CCDS30411.1; -.
DR RefSeq; NP_083817.1; NM_029541.3.
DR RefSeq; NP_084099.1; NM_029823.2.
DR AlphaFoldDB; C0HK80; -.
DR SMR; C0HK80; -.
DR GlyGen; C0HK80; 1 site.
DR iPTMnet; C0HK80; -.
DR PhosphoSitePlus; C0HK80; -.
DR EPD; C0HK80; -.
DR PRIDE; C0HK80; -.
DR DNASU; 76219; -.
DR Ensembl; ENSMUST00000057625; ENSMUSP00000062660; ENSMUSG00000048355.
DR Ensembl; ENSMUST00000058119; ENSMUSP00000051250; ENSMUSG00000048040.
DR GeneID; 76219; -.
DR GeneID; 76976; -.
DR KEGG; mmu:76219; -.
DR KEGG; mmu:76976; -.
DR CTD; 76219; -.
DR CTD; 76976; -.
DR MGI; MGI:1924226; Arxes2.
DR VEuPathDB; HostDB:ENSMUSG00000048040; -.
DR VEuPathDB; HostDB:ENSMUSG00000048355; -.
DR GeneTree; ENSGT00390000009223; -.
DR OMA; THEREIM; -.
DR OrthoDB; 1514162at2759; -.
DR BioGRID-ORCS; 76219; 1 hit in 33 CRISPR screens.
DR BioGRID-ORCS; 76976; 2 hits in 31 CRISPR screens.
DR PRO; PR:C0HK80; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; C0HK80; protein.
DR Bgee; ENSMUSG00000048040; Expressed in gonadal fat pad and 257 other tissues.
DR ExpressionAtlas; C0HK80; baseline and differential.
DR Genevisible; Q9D365; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; ISO:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
DR GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0006465; P:signal peptide processing; ISO:MGI.
DR GO; GO:0019082; P:viral protein processing; ISO:MGI.
DR InterPro; IPR007653; SPC3.
DR PANTHER; PTHR12804; PTHR12804; 1.
DR Pfam; PF04573; SPC22; 1.
DR PIRSF; PIRSF016089; SPC22; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..180
FT /note="Adipocyte-related X-chromosome expressed sequence 2"
FT /id="PRO_0000438511"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..180
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="S -> P (in Ref. 1; BAB28979)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="S -> P (in Ref. 1; BAB28979)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="F -> P (in Ref. 1; BAB28979)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="L -> P (in Ref. 1; BAB28979)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="L -> M (in Ref. 1; BAB28979)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="K -> N (in Ref. 1; BAC36797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 20146 MW; 7980A041F61AAFBB CRC64;
MNSLLSRANS LFAFTLSVMA ALTLGCILTT AFKDRSAPVR LHVSRILLKK VEDFTGPRKK
SDLGFITFHI SADLEKTFDW NVKQLFLYLS AEYSTKSNAV NQVVLWDKIL LRGENPKLNL
KDVKSKYFFF DDGHGLKGNR NVTLTLSWQV IPIAGILPLV TGSGRVSVPF PDSYEIATTF
