ATRN_MOUSE
ID ATRN_MOUSE Reviewed; 1428 AA.
AC Q9WU60; A2AP43; Q9R263; Q9WU77;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Attractin;
DE AltName: Full=Protein mahogany;
DE Flags: Precursor;
GN Name=Atrn; Synonyms=Mg, Mgca;
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].
RX PubMed=10086355; DOI=10.1038/18210;
RA Nagle D.L., McGrail S.H., Vitale J., Woolf E.A., Dussault B.J. Jr.,
RA DiRocco L., Holmgren L., Montagno J., Bork P., Huszar D.,
RA Fairchild-Huntress V., Ge P., Keilty J., Ebeling C., Baldini L.,
RA Gilchrist J., Burn P., Carlson G.A., Moore K.J.;
RT "The mahogany protein is a receptor involved in suppression of obesity.";
RL Nature 398:148-152(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=10086356; DOI=10.1038/18217;
RA Gunn T.M., Miller K.A., He L., Hyman R.W., Davis R.W., Azarani A.,
RA Schlossman S.F., Duke-Cohan J.S., Barsh G.S.;
RT "The mouse mahogany locus encodes a transmembrane form of human
RT attractin.";
RL Nature 398:152-156(1999).
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 FUNCTION.
RX PubMed=11137996; DOI=10.1038/83741;
RA He L., Gunn T.M., Bouley D.M., Lu X.Y., Watson S.J., Schlossman S.F.,
RA Duke-Cohan J.S., Barsh G.S.;
RT "A biochemical function for attractin in agouti-induced pigmentation and
RT obesity.";
RL Nat. Genet. 27:40-47(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Involved in the initial immune cell clustering during
CC inflammatory response and may regulate chemotactic activity of
CC chemokines (By similarity). May play a role in melanocortin signaling
CC pathways that regulate energy homeostasis and hair color. Low-affinity
CC receptor for agouti. Has a critical role in normal myelination in the
CC central nervous system (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11137996}.
CC -!- SUBUNIT: Monomer and homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75882};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75882}.
CC -!- PTM: Heavily glycosylated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD20947.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Attractin;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_150";
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DR EMBL; AF116897; AAD20947.1; ALT_FRAME; mRNA.
DR EMBL; AF119821; AAD25372.1; -; mRNA.
DR EMBL; AH007542; AAD22476.1; -; Genomic_DNA.
DR EMBL; AL833771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28292.1; -; Genomic_DNA.
DR CCDS; CCDS16751.1; -.
DR RefSeq; NP_033860.2; NM_009730.3.
DR AlphaFoldDB; Q9WU60; -.
DR SMR; Q9WU60; -.
DR IntAct; Q9WU60; 1.
DR MINT; Q9WU60; -.
DR STRING; 10090.ENSMUSP00000028781; -.
DR GlyConnect; 2145; 10 N-Linked glycans (8 sites).
DR GlyGen; Q9WU60; 25 sites, 10 N-linked glycans (8 sites).
DR iPTMnet; Q9WU60; -.
DR PhosphoSitePlus; Q9WU60; -.
DR SwissPalm; Q9WU60; -.
DR MaxQB; Q9WU60; -.
DR PaxDb; Q9WU60; -.
DR PRIDE; Q9WU60; -.
DR ProteomicsDB; 277219; -.
DR Antibodypedia; 2265; 260 antibodies from 31 providers.
DR DNASU; 11990; -.
DR Ensembl; ENSMUST00000028781; ENSMUSP00000028781; ENSMUSG00000027312.
DR GeneID; 11990; -.
DR KEGG; mmu:11990; -.
DR UCSC; uc008mkc.1; mouse.
DR CTD; 8455; -.
DR MGI; MGI:1341628; Atrn.
DR VEuPathDB; HostDB:ENSMUSG00000027312; -.
DR eggNOG; KOG1388; Eukaryota.
DR GeneTree; ENSGT00940000157346; -.
DR HOGENOM; CLU_003930_0_0_1; -.
DR InParanoid; Q9WU60; -.
DR OMA; EACNIAA; -.
DR OrthoDB; 49565at2759; -.
DR PhylomeDB; Q9WU60; -.
DR TreeFam; TF321873; -.
DR BioGRID-ORCS; 11990; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Atrn; mouse.
DR PRO; PR:Q9WU60; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9WU60; protein.
DR Bgee; ENSMUSG00000027312; Expressed in urinary bladder urothelium and 231 other tissues.
DR Genevisible; Q9WU60; MM.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IPI:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0021549; P:cerebellum development; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00055; EGF_Lam; 3.
DR Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 2.60.120.290; -; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF01344; Kelch_1; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF01437; PSI; 2.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00423; PSI; 5.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 3.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein;
KW Inflammatory response; Kelch repeat; Laminin EGF-like domain; Lectin;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..82
FT /evidence="ECO:0000250"
FT /id="PRO_0000394772"
FT CHAIN 83..1428
FT /note="Attractin"
FT /id="PRO_0000007484"
FT TOPO_DOM 83..1278
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1279..1299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1300..1428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 100..128
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 131..247
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REPEAT 351..401
FT /note="Kelch 1"
FT REPEAT 402..450
FT /note="Kelch 2"
FT REPEAT 460..507
FT /note="Kelch 3"
FT REPEAT 512..563
FT /note="Kelch 4"
FT REPEAT 565..623
FT /note="Kelch 5"
FT REPEAT 624..670
FT /note="Kelch 6"
FT DOMAIN 702..747
FT /note="PSI 1"
FT DOMAIN 754..793
FT /note="PSI 2"
FT DOMAIN 794..918
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 931..982
FT /note="PSI 3"
FT DOMAIN 985..1060
FT /note="PSI 4"
FT DOMAIN 1062..1107
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1108..1156
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 15..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 913
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 922
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 985
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1042
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1053
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1072
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..110
FT /evidence="ECO:0000250"
FT DISULFID 104..117
FT /evidence="ECO:0000250"
FT DISULFID 119..128
FT /evidence="ECO:0000250"
FT DISULFID 131..157
FT /evidence="ECO:0000250"
FT DISULFID 249..259
FT /evidence="ECO:0000250"
FT DISULFID 253..270
FT /evidence="ECO:0000250"
FT DISULFID 272..281
FT /evidence="ECO:0000250"
FT DISULFID 815..917
FT /evidence="ECO:0000250"
FT DISULFID 1062..1070
FT /evidence="ECO:0000250"
FT DISULFID 1064..1076
FT /evidence="ECO:0000250"
FT DISULFID 1079..1088
FT /evidence="ECO:0000250"
FT DISULFID 1091..1105
FT /evidence="ECO:0000250"
FT DISULFID 1108..1117
FT /evidence="ECO:0000250"
FT DISULFID 1110..1124
FT /evidence="ECO:0000250"
FT DISULFID 1126..1136
FT /evidence="ECO:0000250"
FT DISULFID 1139..1154
FT /evidence="ECO:0000250"
FT CONFLICT 6
FT /note="A -> V (in Ref. 2; AAD25372)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="A -> S (in Ref. 2; AAD25372)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="A -> T (in Ref. 1; AAD20947)"
FT /evidence="ECO:0000305"
FT CONFLICT 164..169
FT /note="QPNRIM -> YPNAVL (in Ref. 2; AAD25372)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="G -> A (in Ref. 2; AAD25372)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="V -> A (in Ref. 2; AAD25372)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="F -> L (in Ref. 2; AAD25372)"
FT /evidence="ECO:0000305"
FT CONFLICT 1075
FT /note="I -> V (in Ref. 2; AAD25372)"
FT /evidence="ECO:0000305"
FT CONFLICT 1140
FT /note="E -> K (in Ref. 2; AAD25372)"
FT /evidence="ECO:0000305"
FT CONFLICT 1171
FT /note="E -> G (in Ref. 2; AAD25372)"
FT /evidence="ECO:0000305"
FT CONFLICT 1192
FT /note="L -> F (in Ref. 2; AAD25372)"
FT /evidence="ECO:0000305"
FT CONFLICT 1201
FT /note="N -> K (in Ref. 2; AAD25372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1428 AA; 158058 MW; BB54C24E7EF1CE34 CRC64;
MVAVAAAAAT EARLRGSTTA TAAPAGRKGR QHRPCTATGA WRPGPRARLC LPRVLSRALP
PPPLLPLLFS LLLLPLPREA EAAAVAAAVS GSAAAEAKEC DRPCVNGGRC NPGTGQCVCP
TGWVGEQCQH CGGRFRLTGS SGFVTDGPGN YKYKTKCTWL IEGQPNRIMR LRFNHFATEC
SWDHLYVYDG DSIYAPLIAA FSGLIVPERD GNETAPEVTV TSGYALLHFF SDAAYNLTGF
NITYNFDMCP NNCSGRGECK SSNSSSAVEC ECSENWKGES CDIPHCTDNC GFPHRGICNA
SDTRGCSCFP HWQGPGCSIP VPANQSFWTR EEYSDLKLPR ASHKAVVNGN IMWVVGGYMF
NHSDYSMVLA YDLTSREWLP LNHSVNSVVV RYGHSLALHK DKIYMYGGKI DSTGNVTNEL
RVFHIHNESW VLLTPKAKDQ YAVVGHSAHI VTLASGRVVM LVIFGHCPLY GYISVVQEYD
LEKNTWSILH TQGALVQGGY GHSSVYDDRT KALYVHGGYK AFSANKYRLA DDLYRYDVDT
QMWTILKDSR FFRYLHTAVI VSGTMLVFGG NTHNDTSMSH GAKCFSSDFM AYDIACDRWS
VLPRPELHHD VNRFGHSAVL YNSTMYVFGG FNSLLLSDVL VFTSEQCDAH RSEAACVAAG
PGIRCLWDTQ SSRCTSWELA TEEQAEKLKS ECFSKRTLDH DRCDQHTDCY SCTANTNDCH
WCNDHCVPVN HSCTEGQISI AKYESCPKDN PMYYCNKKTS CRSCALDQNC QWEPRNQECI
ALPENICGNG WHLVGNSCLK ITTAKENYDN AKLSCRNHNA FLASLTSQKK VEFVLKQLRL
MQSSQSMSKL TLTPWVGLRK INVSYWCWED MSPFTNSLLQ WMPSEPSDAG FCGILSEPST
RGLKAATCIN PLNGSVCERP ANHSAKQCRT PCALRTACGE CTSSSSECMW CSNMKQCVDS
NAYVASFPFG QCMEWYTMSS CPPENCSGYC TCSHCLEQPG CGWCTDPSNT GKGKCIEGSY
KGPVKMPSQA SAGNVYPQPL LNSSMCLEDS RYNWSFIHCP ACQCNGHSKC INQSICEKCE
DLTTGKHCET CISGFYGDPT NGGKCQPCKC NGHASLCNTN TGKCFCTTKG VKGDECQLCE
VENRYQGNPL KGTCYYTLLI DYQFTFSLSQ EDDRYYTAIN FVATPDEQNR DLDMFINASK
NFNLNITWAT SFPAGTQTGE EVPVVSKTNI KEYKDSFSNE KFDFRNHPNI TFFVYVSNFT
WPIKIQIAFS QHSNFMDLVQ FFVTFFSCFL SLLLVAAVVW KIKQSCWASR RREQLLREMQ
QMASRPFASV NVALETDEEP PDLIGGSIKT VPKPIALEPC FGNKAAVLSV FVRLPRGLGG
IPPPGQSGLA VASALVDISQ QMPIVYKEKS GAVRNRKQQP PAQPGTCI
