APMAP_MOUSE
ID APMAP_MOUSE Reviewed; 415 AA.
AC Q9D7N9; A2AQX3; Q3U4F4;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Adipocyte plasma membrane-associated protein;
DE AltName: Full=Protein DD16;
GN Name=Apmap;
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].
RC TISSUE=Brain;
RX PubMed=11583587; DOI=10.1042/0264-6021:3590393;
RA Albrektsen T., Richter H.E., Clausen J.T., Fleckner J.;
RT "Identification of a novel integral plasma membrane protein induced during
RT adipocyte differentiation.";
RL Biochem. J. 359:393-402(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Tongue;
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 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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [6]
RP PROTEIN SEQUENCE OF 170-178; 183-194; 196-206 AND 324-341, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
CC -!- FUNCTION: Exhibits strong arylesterase activity with beta-naphthyl
CC acetate and phenyl acetate (By similarity). May play a role in
CC adipocyte differentiation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in adipose tissue. Highly
CC expressed in liver, heart, and kidney. Expressed at intermediate level
CC in brain and lung. Weakly expressed in spleen, skeletal muscle and
CC testis.
CC -!- DEVELOPMENTAL STAGE: Expressed during adipocyte differentiation.
CC Expression appears 3 days following induction of adipose conversion.
CC -!- PTM: Glycosylated in vitro.
CC -!- SIMILARITY: Belongs to the strictosidine synthase family.
CC {ECO:0000305}.
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DR EMBL; AJ310638; CAC83967.1; -; mRNA.
DR EMBL; AK009057; BAB26050.1; -; mRNA.
DR EMBL; AK154266; BAE32477.1; -; mRNA.
DR EMBL; AL845174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28569.1; -; Genomic_DNA.
DR EMBL; BC055706; AAH55706.1; -; mRNA.
DR CCDS; CCDS16858.1; -.
DR RefSeq; NP_082253.1; NM_027977.2.
DR AlphaFoldDB; Q9D7N9; -.
DR SMR; Q9D7N9; -.
DR BioGRID; 215002; 12.
DR IntAct; Q9D7N9; 2.
DR STRING; 10090.ENSMUSP00000040840; -.
DR GlyConnect; 2112; 6 N-Linked glycans (1 site).
DR GlyGen; Q9D7N9; 1 site, 6 N-linked glycans (1 site).
DR iPTMnet; Q9D7N9; -.
DR PhosphoSitePlus; Q9D7N9; -.
DR SwissPalm; Q9D7N9; -.
DR EPD; Q9D7N9; -.
DR jPOST; Q9D7N9; -.
DR MaxQB; Q9D7N9; -.
DR PaxDb; Q9D7N9; -.
DR PeptideAtlas; Q9D7N9; -.
DR PRIDE; Q9D7N9; -.
DR ProteomicsDB; 296380; -.
DR Antibodypedia; 2012; 300 antibodies from 22 providers.
DR DNASU; 71881; -.
DR Ensembl; ENSMUST00000046399; ENSMUSP00000040840; ENSMUSG00000033096.
DR GeneID; 71881; -.
DR KEGG; mmu:71881; -.
DR UCSC; uc008mud.1; mouse.
DR CTD; 57136; -.
DR MGI; MGI:1919131; Apmap.
DR VEuPathDB; HostDB:ENSMUSG00000033096; -.
DR eggNOG; KOG1520; Eukaryota.
DR GeneTree; ENSGT00440000039984; -.
DR HOGENOM; CLU_023267_0_0_1; -.
DR InParanoid; Q9D7N9; -.
DR OMA; ERLWENQ; -.
DR OrthoDB; 757814at2759; -.
DR PhylomeDB; Q9D7N9; -.
DR TreeFam; TF316475; -.
DR BioGRID-ORCS; 71881; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Apmap; mouse.
DR PRO; PR:Q9D7N9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D7N9; protein.
DR Bgee; ENSMUSG00000033096; Expressed in decidua and 247 other tissues.
DR Genevisible; Q9D7N9; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0004064; F:arylesterase activity; ISO:MGI.
DR GO; GO:0016844; F:strictosidine synthase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR018119; Strictosidine_synth_cons-reg.
DR Pfam; PF03088; Str_synth; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9HDC9"
FT CHAIN 2..415
FT /note="Adipocyte plasma membrane-associated protein"
FT /id="PRO_0000205946"
FT TOPO_DOM 2..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HDC9"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HDC9"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 415 AA; 46434 MW; 10BA522364CC03D8 CRC64;
MSEADGLRQR RPLRPQVVTD DGQVPEVKEG SSFSGRVFRM TFLMLAVSLA IPLLGAMMLL
ESPIDPQSFS FKEPPFMFGV LHPNTKLRQA ERLFENQLSG PESIVNIGDV LFTGTADGRV
VKLENGEIET IARFGSGPCK TRDDEPTCGR PLGIRAGPNG TLFVVDAYKG LFEVNPQKRS
VKLLLSSETP IEGKKMSFVN DLTVTRDGRK IYFTDSSSKW QRRDYLLLVM EATDDGRLLE
YDTVTKEVKV LLDQLQFPNG VQLSPEEDFV LVAETTMARI RRVYVSGLMK GGADMFVENM
PGFPDNIRPS SSGGYWVAAA TIRANPGFSM LDFLSDKPFI KRMIFKMFSQ ETVMKFVPRY
SLVLEVSDSG AFRRSLHDPD GQVVTYVSEA HEHDGYLYLG SFRSPFICRL SLQSI
