PGM5_HUMAN
ID PGM5_HUMAN Reviewed; 567 AA.
AC Q15124; B1AM46; B4DLQ6; Q5VYV3; Q8N527; Q9UDH4;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Phosphoglucomutase-like protein 5 {ECO:0000305};
DE AltName: Full=Aciculin {ECO:0000303|PubMed:8631316};
DE AltName: Full=Phosphoglucomutase-related protein;
DE Short=PGM-RP;
GN Name=PGM5 {ECO:0000312|HGNC:HGNC:8908}; Synonyms=PGMRP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-87.
RX PubMed=9342213; DOI=10.1111/j.1432-1033.1997.00634.x;
RA Moiseeva E.P., Critchley D.R.;
RT "Characterisation of the promoter which regulates expression of a
RT phosphoglucomutase-related protein, a component of the dystrophin/utrophin
RT cytoskeleton predominantly expressed in smooth muscle.";
RL Eur. J. Biochem. 248:634-643(1997).
RN [5]
RP PROTEIN SEQUENCE OF 29-55; 158-169; 191-224; 227-239; 355-375; 433-492 AND
RP 497-504, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Parker K.;
RL Submitted (JUN-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-567, AND TISSUE SPECIFICITY.
RC TISSUE=Uterus;
RX PubMed=8631316; DOI=10.1111/j.1432-1033.1996.00103.x;
RA Moiseeva E.P., Belkin A.M., Spurr N.K., Koteliansky V.E., Critchley D.R.;
RT "A novel dystrophin/utrophin-associated protein is an enzymatically
RT inactive member of the phosphoglucomutase superfamily.";
RL Eur. J. Biochem. 235:103-113(1996).
RN [7]
RP PROTEIN SEQUENCE OF 82-104; 234-262 AND 447-467, FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Uterus;
RX PubMed=8175905; DOI=10.1242/jcs.107.1.159;
RA Belkin A.M., Klimanskaya I.V., Lukashev M.E., Lilley K., Critchley D.R.,
RA Koteliansky V.E.;
RT "A novel phosphoglucomutase-related protein is concentrated in adherens
RT junctions of muscle and nonmuscle cells.";
RL J. Cell Sci. 107:159-173(1994).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Component of adherens-type cell-cell and cell-matrix
CC junctions (PubMed:8175905). Has no phosphoglucomutase activity in vitro
CC (PubMed:8175905). {ECO:0000269|PubMed:8175905}.
CC -!- SUBUNIT: Interacts with DMD/dystrophin; the interaction is direct (By
CC similarity). Interacts with UTRN/utrophin (By similarity).
CC {ECO:0000250|UniProtKB:D3ZVR9, ECO:0000250|UniProtKB:Q8BZF8}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:8175905}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:8175905}. 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:0000269|PubMed:8175905}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15124-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15124-2; Sequence=VSP_030014, VSP_030015;
CC -!- TISSUE SPECIFICITY: Detected in smooth and cardiac muscle at high
CC levels and in skeletal muscle at low level. Present in other tissues
CC due to vascular or other smooth muscle component. Low levels are
CC present in liver, kidney, skin and brain (at protein level).
CC {ECO:0000269|PubMed:8175905, ECO:0000269|PubMed:8631316}.
CC -!- DEVELOPMENTAL STAGE: In the developing aorta, expressed at low levels
CC in 10-12 week old fetuses. Levels increase progressively in 24 week
CC fetus, 6 month old child and 1.5 year old child aortic smooth muscle,
CC reaching a maximum at maturity. {ECO:0000269|PubMed:8175905}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC41948.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH33073.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA73882.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK297108; BAG59618.1; -; mRNA.
DR EMBL; AL161457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033073; AAH33073.1; ALT_INIT; mRNA.
DR EMBL; Y13478; CAA73882.1; ALT_INIT; Genomic_DNA.
DR EMBL; L40933; AAC41948.1; ALT_INIT; Genomic_DNA.
DR CCDS; CCDS6622.2; -. [Q15124-1]
DR PIR; S62629; S62629.
DR RefSeq; NP_068800.2; NM_021965.3. [Q15124-1]
DR AlphaFoldDB; Q15124; -.
DR SMR; Q15124; -.
DR BioGRID; 111258; 9.
DR STRING; 9606.ENSP00000379678; -.
DR iPTMnet; Q15124; -.
DR PhosphoSitePlus; Q15124; -.
DR BioMuta; PGM5; -.
DR DMDM; 152031655; -.
DR EPD; Q15124; -.
DR jPOST; Q15124; -.
DR MassIVE; Q15124; -.
DR MaxQB; Q15124; -.
DR PaxDb; Q15124; -.
DR PeptideAtlas; Q15124; -.
DR PRIDE; Q15124; -.
DR ProteomicsDB; 60450; -. [Q15124-1]
DR ProteomicsDB; 60451; -. [Q15124-2]
DR TopDownProteomics; Q15124-2; -. [Q15124-2]
DR Antibodypedia; 26751; 101 antibodies from 18 providers.
DR DNASU; 5239; -.
DR Ensembl; ENST00000396392.5; ENSP00000379674.1; ENSG00000154330.13. [Q15124-2]
DR Ensembl; ENST00000396396.6; ENSP00000379678.1; ENSG00000154330.13. [Q15124-1]
DR GeneID; 5239; -.
DR KEGG; hsa:5239; -.
DR MANE-Select; ENST00000396396.6; ENSP00000379678.1; NM_021965.4; NP_068800.2.
DR UCSC; uc004agr.3; human. [Q15124-1]
DR CTD; 5239; -.
DR DisGeNET; 5239; -.
DR GeneCards; PGM5; -.
DR HGNC; HGNC:8908; PGM5.
DR HPA; ENSG00000154330; Tissue enhanced (seminal vesicle, urinary bladder).
DR MIM; 600981; gene.
DR neXtProt; NX_Q15124; -.
DR OpenTargets; ENSG00000154330; -.
DR PharmGKB; PA33245; -.
DR VEuPathDB; HostDB:ENSG00000154330; -.
DR eggNOG; KOG0625; Eukaryota.
DR GeneTree; ENSGT00940000158126; -.
DR HOGENOM; CLU_009330_0_0_1; -.
DR InParanoid; Q15124; -.
DR OMA; RGHVREK; -.
DR OrthoDB; 555015at2759; -.
DR PhylomeDB; Q15124; -.
DR TreeFam; TF300350; -.
DR PathwayCommons; Q15124; -.
DR SignaLink; Q15124; -.
DR BioGRID-ORCS; 5239; 22 hits in 1060 CRISPR screens.
DR ChiTaRS; PGM5; human.
DR GeneWiki; PGM5; -.
DR GenomeRNAi; 5239; -.
DR Pharos; Q15124; Tbio.
DR PRO; PR:Q15124; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q15124; protein.
DR Bgee; ENSG00000154330; Expressed in saphenous vein and 171 other tissues.
DR ExpressionAtlas; Q15124; baseline and differential.
DR Genevisible; Q15124; HS.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0030055; C:cell-substrate junction; IBA:GO_Central.
DR GO; GO:0043034; C:costamere; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0005914; C:spot adherens junction; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0016868; F:intramolecular transferase activity, phosphotransferases; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
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 Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..567
FT /note="Phosphoglucomutase-like protein 5"
FT /id="PRO_0000147787"
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:0007744|PubMed:24275569"
FT VAR_SEQ 387
FT /note="G -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030014"
FT VAR_SEQ 388..567
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030015"
FT CONFLICT 22
FT /note="A -> S (in Ref. 4; CAA73882)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="D -> E (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..261
FT /note="ED -> DE (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 62225 MW; 00583A442977A025 CRC64;
MEGSPIPVLT VPTAPYEDQR PAGGGGLRRP TGLFEGQRNY LPNFIQSVLS SIDLRDRQGC
TMVVGSDGRY FSRTAIEIVV QMAAANGIGR LIIGQNGILS TPAVSCIIRK IKAAGGIILT
ASHCPGGPGG EFGVKFNVAN GGPAPDVVSD KIYQISKTIE EYAICPDLRI DLSRLGRQEF
DLENKFKPFR VEIVDPVDIY LNLLRTIFDF HAIKGLLTGP SQLKIRIDAM HGVMGPYVRK
VLCDELGAPA NSAINCVPLE DFGGQHPDPN LTYATTLLEA MKGGEYGFGA AFDADGDRYM
ILGQNGFFVS PSDSLAIIAA NLSCIPYFRQ MGVRGFGRSM PTSMALDRVA KSMKVPVYET
PAGWRFFSNL MDSGRCNLCG EESFGTGSDH LREKDGLWAV LVWLSIIAAR KQSVEEIVRD
HWAKFGRHYY CRFDYEGLDP KTTYYIMRDL EALVTDKSFI GQQFAVGSHV YSVAKTDSFE
YVDPVDGTVT KKQGLRIIFS DASRLIFRLS SSSGVRATLR LYAESYERDP SGHDQEPQAV
LSPLIAIALK ISQIHERTGR RGPTVIT
