PGM5_RAT
ID PGM5_RAT Reviewed; 567 AA.
AC D3ZVR9;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 3.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Phosphoglucomutase-like protein 5;
GN Name=Pgm5 {ECO:0000312|RGD:1307969};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP INTERACTION WITH UTRN.
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] {ECO:0007744|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By
CC similarity). Interacts with UTRN/utrophin (PubMed:7890770).
CC {ECO:0000250|UniProtKB:Q8BZF8, 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:0000250|UniProtKB:Q8BZF8}. 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}.
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DR EMBL; AABR07006615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07006616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07006617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07006618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; D3ZVR9; -.
DR SMR; D3ZVR9; -.
DR STRING; 10116.ENSRNOP00000020763; -.
DR iPTMnet; D3ZVR9; -.
DR PhosphoSitePlus; D3ZVR9; -.
DR PaxDb; D3ZVR9; -.
DR PeptideAtlas; D3ZVR9; -.
DR PRIDE; D3ZVR9; -.
DR Ensembl; ENSRNOT00000020763; ENSRNOP00000020763; ENSRNOG00000015406.
DR UCSC; RGD:1307969; rat.
DR RGD; 1307969; Pgm5.
DR eggNOG; KOG0625; Eukaryota.
DR GeneTree; ENSGT00940000158126; -.
DR HOGENOM; CLU_009330_0_1_1; -.
DR InParanoid; D3ZVR9; -.
DR OMA; RGHVREK; -.
DR TreeFam; TF300350; -.
DR PRO; PR:D3ZVR9; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000015406; Expressed in heart and 18 other tissues.
DR Genevisible; D3ZVR9; RN.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0030055; C:cell-substrate junction; ISO:RGD.
DR GO; GO:0043034; C:costamere; ISO:RGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0014704; C:intercalated disc; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0005914; C:spot adherens junction; ISO:RGD.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
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.
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_0000455425"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZF8"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZF8"
SQ SEQUENCE 567 AA; 62204 MW; 9D1820C03E0755A6 CRC64;
MEGSPIPVLT VPTAPYEDQR PTGGGGLRRP TGLFEGQRNY LPNFIQSVLS SIDLRDRQGC
TMVVGSDGRY FSRTATEIVV QMAAANGIGR LIIGQNGILS TPAVSCIIRK IKAAGGIILT
ASHCPGGPGG EFGVKFNVAN GGPAPDVVSD KIYQISKTIE EYTICPDLRI DLSRLGRQEF
DLENKFKPFR VEIVDPVDIY LNLLRTIFDF NAIKSLLTGP SQLKIRVDAM HGVMGPYVRK
VLCDELGAPA NSAINCVPLE DFGGQHPDPN LTYATTLLEA MKGGEYGFGA AFDADGDRYM
ILGQNGFFVS PSDSLAIIAA NLSCIPYFRQ MGVRGFGRSM PTSMALDRVA KSMKVPVYET
PAGWRFFSNL MDSGRCSLCG EESFGTGSDH LREKDGLWAV LVWLSIIAAR KQSVEEIVRD
HWAKYGRHYY CRVLYEAKSP KATYYIMRDL EALVTDKSFI GQQFAVGSHI YSIAKTDSFE
YVDPVDGTVT KKQGLRIIFS DASRLIFRLS SSSGVRATIR LYAESYERDP SGHDQEPQAV
LSPLIAIALK ISQIHERTGR RGPTVIT
