ID H0VP49_CAVPO Unreviewed; 614 AA.
AC H0VP49;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Phosphoglucomutase 2 {ECO:0000313|Ensembl:ENSCPOP00000012254.3};
GN Name=PGM2 {ECO:0000313|Ensembl:ENSCPOP00000012254.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000012254.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000012254.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000012254.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; AAKN02027990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003471584.2; XM_003471536.3.
DR AlphaFoldDB; H0VP49; -.
DR STRING; 10141.ENSCPOP00000012254; -.
DR Ensembl; ENSCPOT00000013747.3; ENSCPOP00000012254.3; ENSCPOG00000013611.4.
DR GeneID; 100731750; -.
DR KEGG; cpoc:100731750; -.
DR CTD; 55276; -.
DR VEuPathDB; HostDB:ENSCPOG00000013611; -.
DR eggNOG; KOG1220; Eukaryota.
DR GeneTree; ENSGT00940000156247; -.
DR HOGENOM; CLU_016950_0_1_1; -.
DR InParanoid; H0VP49; -.
DR OMA; HVTKASY; -.
DR OrthoDB; 1482at2759; -.
DR TreeFam; TF300692; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000013611; Expressed in pituitary gland and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:Ensembl.
DR GO; GO:0008973; F:phosphopentomutase activity; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:Ensembl.
DR GO; GO:0005980; P:glycogen catabolic process; IEA:Ensembl.
DR CDD; cd05799; PGM2; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
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 PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR PANTHER; PTHR45745:SF3; PHOSPHOPENTOMUTASE; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT DOMAIN 57..201
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 230..335
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 346..473
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 68301 MW; 7C075C554AD913F6 CRC64;
MAAAGTPAPG GNGRAAGGRR RPRWLRWDKN PLTLESVKQL IAAGTKEELQ ECFGARMEFG
TAGLRAPMGA GISRMNDLTI IQTTQGFCRY LEEQFSDLRQ RGVVISFDAR AHPPSGGSSR
RFARLAATTF ISQGIPVHLF SDITPTPFVP YTVSHLKLCA GIMITASHNP KQDNGYKVYW
DNGAQIISPH DKGISQAIEE NLEPWPQAWD DSLIDGSPLL HNPTASINND YFEDLKKYCF
HRSVNRETQE KFVHTSVHGV AHDFVQAAFK AFSLAPPEAV PQQKDPDPEF PTVKYPNPEE
GKGVLTLSFA LADKIKAKIV LANDPDADRL AVAEKQDSGE WRVFSGNELG ALLGWWLFTS
WKEKNQDRSA LRDTYMLSST VSSKILRAIA LKEGFHFEET LTGFKWMGNR AKQLIDQGKT
VLFAFEEAIG YMCCPFVLDK DGVSAAVISA ELASFLATKN LSLSQQLKAI YVEYGYHITK
ASYFICHDQG IIKKLFENLR NYDGKNHYPK TCGKFEISAI RDLTTGYDDS QPDKKAVLPT
SKSSQMITFT FANGGVATMR TSGTEPKIKY YAELCAPPGN SDPEHLKKEL NELVDAIEEN
FFQPQKYNLQ PKAE
//
