PGM5_MOUSE
ID PGM5_MOUSE Reviewed; 567 AA.
AC Q8BZF8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phosphoglucomutase-like protein 5 {ECO:0000305};
GN Name=Pgm5 {ECO:0000312|MGI:MGI:1925668};
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=Urinary bladder;
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 INTERACTION WITH DMD, AND SUBCELLULAR LOCATION.
RX PubMed=7890770; DOI=10.1074/jbc.270.11.6328;
RA Belkin A.M., Burridge K.;
RT "Association of aciculin with dystrophin and utrophin.";
RL J. Biol. Chem. 270:6328-6337(1995).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120 AND SER-122, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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: Component of adherens-type cell-cell and cell-matrix
CC junctions. Has no phosphoglucomutase activity in vitro.
CC {ECO:0000250|UniProtKB:Q15124}.
CC -!- SUBUNIT: Interacts with DMD/dystrophin; the interaction is direct
CC (PubMed:7890770). Interacts with UTRN/utrophin (By similarity).
CC {ECO:0000250|UniProtKB:D3ZVR9, ECO:0000269|PubMed:7890770}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q15124}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q15124}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:7890770}. Note=Concentrated in focal contacts at
CC the ends of actin bundles, and associated with actin filaments.
CC {ECO:0000250|UniProtKB:Q15124}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29083.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK035507; BAC29083.1; ALT_INIT; mRNA.
DR CCDS; CCDS29714.1; -.
DR RefSeq; NP_778178.3; NM_175013.2.
DR AlphaFoldDB; Q8BZF8; -.
DR SMR; Q8BZF8; -.
DR BioGRID; 230463; 2.
DR IntAct; Q8BZF8; 1.
DR STRING; 10090.ENSMUSP00000036025; -.
DR iPTMnet; Q8BZF8; -.
DR PhosphoSitePlus; Q8BZF8; -.
DR jPOST; Q8BZF8; -.
DR MaxQB; Q8BZF8; -.
DR PaxDb; Q8BZF8; -.
DR PeptideAtlas; Q8BZF8; -.
DR PRIDE; Q8BZF8; -.
DR ProteomicsDB; 287691; -.
DR Antibodypedia; 26751; 101 antibodies from 18 providers.
DR DNASU; 226041; -.
DR Ensembl; ENSMUST00000047666; ENSMUSP00000036025; ENSMUSG00000041731.
DR GeneID; 226041; -.
DR KEGG; mmu:226041; -.
DR UCSC; uc008has.1; mouse.
DR CTD; 5239; -.
DR MGI; MGI:1925668; Pgm5.
DR VEuPathDB; HostDB:ENSMUSG00000041731; -.
DR eggNOG; KOG0625; Eukaryota.
DR GeneTree; ENSGT00940000158126; -.
DR HOGENOM; CLU_009330_0_1_1; -.
DR InParanoid; Q8BZF8; -.
DR OMA; RGHVREK; -.
DR OrthoDB; 555015at2759; -.
DR PhylomeDB; Q8BZF8; -.
DR TreeFam; TF300350; -.
DR BioGRID-ORCS; 226041; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Pgm5; mouse.
DR PRO; PR:Q8BZF8; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8BZF8; protein.
DR Bgee; ENSMUSG00000041731; Expressed in interventricular septum and 150 other tissues.
DR Genevisible; Q8BZF8; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0030055; C:cell-substrate junction; IDA:MGI.
DR GO; GO:0043034; C:costamere; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0005914; C:spot adherens junction; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030239; P:myofibril assembly; IBA:GO_Central.
DR GO; GO:0014706; P:striated muscle tissue development; IBA:GO_Central.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573; PTHR22573; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..567
FT /note="Phosphoglucomutase-like protein 5"
FT /id="PRO_0000294064"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 567 AA; 62220 MW; 46CD383095054BEB CRC64;
MEGSPIPVLT VPTAPYEDQR PTGGGGLRRP TGLFEGQRNY LPNFIQSVLS SIDLRDRQGC
TMVVGSDGRY FSRTATEIVV QMAAANGIGR LIIGQNGILS TPAVSCIIRK IKAAGGIILT
ASHCPGGPGG EFGVKFNVAN GGPAPDVVSD KIYQISKTIE EYAICPDLRI DLSRLGRQEF
DLENKFKPFR VEIVDPVDIY LNLLRNIFDF NAIKSLLTGP SQLKIRVDAM HGVMGPYVRK
VLCDELGAPA NSAINCVPLE DFGGQHPDPN LTYATTLLEA MKGGEYGFGA AFDADGDRYM
ILGQNGFFVS PSDSLAIIAA NLSCIPYFRQ MGVRGFGRSM PTSTALDRVA KSMKVPVYET
PAGWRFFSNL MDSGRCSLCG EESFGTGSDH LREKDGLWAV LVWLSIIAAR KQSVEEIVRD
HWAKYGRHYY CRFDYEGLEP KATYYIMRDL EALVTDKSFI GQQFAVGSHI YSIAKTDSFE
YVDPVDGTVT KKQGLRIIFS DASRLIFRLS SSSGVRATIR LYAESYERDP SGHDQEPQAV
LSPLIAIALK ISQIHERTGR RGPTVIT
