MYADM_MOUSE
ID MYADM_MOUSE Reviewed; 320 AA.
AC O35682; Q8BGS9; Q8BPS8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Myeloid-associated differentiation marker;
DE AltName: Full=Myeloid up-regulated protein;
GN Name=Myadm; Synonyms=Mug;
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=10733104; DOI=10.1002/jlb.67.3.423;
RA Pettersson M., Nilsson K., Jonsson J.I.;
RT "Isolation of MYADM, a novel hematopoietic-associated marker gene expressed
RT in multipotent progenitor cells and up-regulated during myeloid
RT differentiation.";
RL J. Leukoc. Biol. 67:423-431(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Dendritic cell, Embryonic heart, Eye, Macrophage, and Osteoclast;
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 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MAL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA04870.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ001616; CAA04870.1; ALT_FRAME; mRNA.
DR EMBL; AK052258; BAC34900.1; -; mRNA.
DR EMBL; AK053414; BAC35377.1; -; mRNA.
DR EMBL; AK089538; BAC40918.1; -; mRNA.
DR EMBL; AK149962; BAE29196.1; -; mRNA.
DR EMBL; AK159160; BAE34863.1; -; mRNA.
DR CCDS; CCDS51964.1; -.
DR RefSeq; NP_001087233.1; NM_001093764.1.
DR RefSeq; NP_001087234.1; NM_001093765.1.
DR RefSeq; NP_001087235.1; NM_001093766.1.
DR RefSeq; NP_058665.2; NM_016969.2.
DR RefSeq; XP_006540234.1; XM_006540171.3.
DR AlphaFoldDB; O35682; -.
DR SMR; O35682; -.
DR BioGRID; 206157; 3.
DR IntAct; O35682; 2.
DR MINT; O35682; -.
DR STRING; 10090.ENSMUSP00000131318; -.
DR iPTMnet; O35682; -.
DR PhosphoSitePlus; O35682; -.
DR SwissPalm; O35682; -.
DR jPOST; O35682; -.
DR PaxDb; O35682; -.
DR PeptideAtlas; O35682; -.
DR PRIDE; O35682; -.
DR ProteomicsDB; 287646; -.
DR Antibodypedia; 19206; 229 antibodies from 19 providers.
DR DNASU; 50918; -.
DR Ensembl; ENSMUST00000096744; ENSMUSP00000094505; ENSMUSG00000068566.
DR Ensembl; ENSMUST00000164553; ENSMUSP00000131318; ENSMUSG00000068566.
DR Ensembl; ENSMUST00000203328; ENSMUSP00000144984; ENSMUSG00000068566.
DR Ensembl; ENSMUST00000203566; ENSMUSP00000145120; ENSMUSG00000068566.
DR GeneID; 50918; -.
DR KEGG; mmu:50918; -.
DR UCSC; uc009eup.1; mouse.
DR CTD; 91663; -.
DR MGI; MGI:1355332; Myadm.
DR VEuPathDB; HostDB:ENSMUSG00000068566; -.
DR eggNOG; KOG4788; Eukaryota.
DR GeneTree; ENSGT00950000182933; -.
DR HOGENOM; CLU_068368_0_0_1; -.
DR InParanoid; O35682; -.
DR OMA; DCTNMLP; -.
DR OrthoDB; 1056604at2759; -.
DR PhylomeDB; O35682; -.
DR TreeFam; TF331088; -.
DR BioGRID-ORCS; 50918; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Myadm; mouse.
DR PRO; PR:O35682; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O35682; protein.
DR Bgee; ENSMUSG00000068566; Expressed in internal carotid artery and 253 other tissues.
DR ExpressionAtlas; O35682; baseline and differential.
DR Genevisible; O35682; MM.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0031579; P:membrane raft organization; ISO:MGI.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0044860; P:protein localization to plasma membrane raft; ISO:MGI.
DR InterPro; IPR008253; Marvel.
DR Pfam; PF01284; MARVEL; 2.
DR PROSITE; PS51225; MARVEL; 2.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..320
FT /note="Myeloid-associated differentiation marker"
FT /id="PRO_0000156817"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 25..157
FT /note="MARVEL 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT DOMAIN 162..317
FT /note="MARVEL 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT CONFLICT 186
FT /note="S -> G (in Ref. 1; CAA04870)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 35285 MW; 7404E588226E756E CRC64;
MPVTVTRTTI TTTTSSSTTV GSARALTQPL GLLRLLQLIS TCVAFSLVAS VGAWTGPMGN
WAMFTWCFCF AVTLIILIVE LGGLQAHFPL SWRNFPITFA CYAALFCLSS SIIYPTTYVQ
FLAHGRTRDH AIAATTFSCV ACLAYATEVA WTRARPGEIT GYMATVPGLL KVFETFVACI
IFAFISEPLL YNQKPALEWC VAVYAICFIL AGVTILLNLG DCTNVLPIPF PTFLSGLALL
SVLFYATAIV LWPLYQFDQR YQGQPRRSMD PSCTRSISYI QPNTVCFWDR RLAVSILTGI
NLLAYVSDLV YSTRLVFVKV
