PMM1_HUMAN
ID PMM1_HUMAN Reviewed; 262 AA.
AC Q92871; A8K003; Q92586;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Phosphomannomutase 1 {ECO:0000303|PubMed:9070917};
DE Short=PMM 1 {ECO:0000303|PubMed:9070917};
DE EC=5.4.2.8 {ECO:0000303|PubMed:16540464};
DE AltName: Full=PMMH-22;
GN Name=PMM1; Synonyms=PMMH22;
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 [MRNA].
RC TISSUE=Liver;
RX PubMed=9070917; DOI=10.1006/geno.1996.4536;
RA Matthijs G., Schollen E., Pirard M., Budarf M.L., van Schaftingen E.,
RA Cassiman J.-J.;
RT "PMM (PMM1), the human homologue of SEC53 or yeast phosphomannomutase, is
RT localized on chromosome 22q13.";
RL Genomics 40:41-47(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9119384; DOI=10.1006/geno.1996.4487;
RA Wada Y., Sakamoto M.;
RT "Isolation of the human phosphomannomutase gene (PMM1) and assignment to
RT chromosome 22q13.";
RL Genomics 39:416-417(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Hansen S.H., Frank S.R., Casanova J.E.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Pancreas;
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND
RP MANNOSE 1-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR,
RP SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16540464; DOI=10.1074/jbc.m601505200;
RA Silvaggi N.R., Zhang C., Lu Z., Dai J., Dunaway-Mariano D., Allen K.N.;
RT "The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal
RT the structural basis of congenital disorder of glycosylation type 1a.";
RL J. Biol. Chem. 281:14918-14926(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND
RP INOSINE MONOPHOSPHATE.
RX PubMed=29695157; DOI=10.1021/acs.biochem.8b00223;
RA Ji T., Zhang C., Zheng L., Dunaway-Mariano D., Allen K.N.;
RT "Structural basis of the molecular switch between phosphatase and mutase
RT functions of human phosphomannomutase 1 under ischemic conditions.";
RL Biochemistry 57:3480-3492(2018).
CC -!- FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-
CC phosphate-mannose required for a number of critical mannosyl transfer
CC reactions. In addition, may be responsible for the degradation of
CC glucose-1,6-bisphosphate in ischemic brain.
CC {ECO:0000269|PubMed:16540464}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC EC=5.4.2.8; Evidence={ECO:0000269|PubMed:16540464};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16540464};
CC -!- ACTIVITY REGULATION: IMP, a metabolite whose concentration is elevated
CC in anoxia, inhibits phosphomannomutase and phosphoglucomutase
CC activities and strongly enhances glucose-1,6-bisphosphatase activity.
CC {ECO:0000250|UniProtKB:O35621}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=54 uM for alpha-D-mannose 1-phosphate
CC {ECO:0000269|PubMed:16540464};
CC KM=7.5 uM for alpha-D-glucose 1-phosphate
CC {ECO:0000269|PubMed:16540464};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16540464}.
CC -!- INTERACTION:
CC Q92871; P20340: RAB6A; NbExp=4; IntAct=EBI-746784, EBI-1052826;
CC Q92871; P20340-2: RAB6A; NbExp=3; IntAct=EBI-746784, EBI-8840191;
CC Q92871; Q9NRW1: RAB6B; NbExp=5; IntAct=EBI-746784, EBI-1760079;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35621}.
CC -!- TISSUE SPECIFICITY: Strong expression in liver, heart, brain, and
CC pancreas; lower expression in skeletal muscle.
CC -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR EMBL; U62526; AAC51117.1; -; mRNA.
DR EMBL; D87810; BAA13460.1; -; mRNA.
DR EMBL; U86070; AAC00023.1; -; mRNA.
DR EMBL; CR456544; CAG30430.1; -; mRNA.
DR EMBL; AK289368; BAF82057.1; -; mRNA.
DR EMBL; AK316580; BAG38168.1; -; mRNA.
DR EMBL; AL023553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60443.1; -; Genomic_DNA.
DR EMBL; BC010855; AAH10855.1; -; mRNA.
DR EMBL; BC016818; AAH16818.1; -; mRNA.
DR CCDS; CCDS14020.1; -.
DR RefSeq; NP_002667.2; NM_002676.2.
DR PDB; 2FUC; X-ray; 2.10 A; A=1-262.
DR PDB; 2FUE; X-ray; 1.75 A; A=1-262.
DR PDB; 6CFR; X-ray; 2.07 A; A=1-262.
DR PDB; 6CFS; X-ray; 2.07 A; A=1-262.
DR PDB; 6CFT; X-ray; 2.43 A; A=1-262.
DR PDB; 6CFU; X-ray; 2.24 A; A=1-262.
DR PDB; 6CFV; X-ray; 1.92 A; A=1-262.
DR PDBsum; 2FUC; -.
DR PDBsum; 2FUE; -.
DR PDBsum; 6CFR; -.
DR PDBsum; 6CFS; -.
DR PDBsum; 6CFT; -.
DR PDBsum; 6CFU; -.
DR PDBsum; 6CFV; -.
DR AlphaFoldDB; Q92871; -.
DR SMR; Q92871; -.
DR BioGRID; 111385; 19.
DR ComplexPortal; CPX-2131; alpha-D-mannose 1,6-phosphomutase.
DR IntAct; Q92871; 14.
DR MINT; Q92871; -.
DR STRING; 9606.ENSP00000216259; -.
DR iPTMnet; Q92871; -.
DR PhosphoSitePlus; Q92871; -.
DR BioMuta; PMM1; -.
DR DMDM; 2499519; -.
DR EPD; Q92871; -.
DR jPOST; Q92871; -.
DR MassIVE; Q92871; -.
DR MaxQB; Q92871; -.
DR PaxDb; Q92871; -.
DR PeptideAtlas; Q92871; -.
DR PRIDE; Q92871; -.
DR ProteomicsDB; 75557; -.
DR Antibodypedia; 26980; 99 antibodies from 20 providers.
DR DNASU; 5372; -.
DR Ensembl; ENST00000216259.8; ENSP00000216259.7; ENSG00000100417.12.
DR GeneID; 5372; -.
DR KEGG; hsa:5372; -.
DR MANE-Select; ENST00000216259.8; ENSP00000216259.7; NM_002676.3; NP_002667.2.
DR UCSC; uc003bal.3; human.
DR CTD; 5372; -.
DR DisGeNET; 5372; -.
DR GeneCards; PMM1; -.
DR HGNC; HGNC:9114; PMM1.
DR HPA; ENSG00000100417; Low tissue specificity.
DR MIM; 601786; gene.
DR neXtProt; NX_Q92871; -.
DR OpenTargets; ENSG00000100417; -.
DR PharmGKB; PA33440; -.
DR VEuPathDB; HostDB:ENSG00000100417; -.
DR eggNOG; KOG3189; Eukaryota.
DR GeneTree; ENSGT00390000002918; -.
DR HOGENOM; CLU_065642_0_1_1; -.
DR InParanoid; Q92871; -.
DR OMA; VYSPEHT; -.
DR OrthoDB; 1038583at2759; -.
DR PhylomeDB; Q92871; -.
DR TreeFam; TF300874; -.
DR BRENDA; 5.4.2.8; 2681.
DR PathwayCommons; Q92871; -.
DR Reactome; R-HSA-446205; Synthesis of GDP-mannose.
DR SABIO-RK; Q92871; -.
DR SignaLink; Q92871; -.
DR UniPathway; UPA00126; UER00424.
DR BioGRID-ORCS; 5372; 10 hits in 1077 CRISPR screens.
DR ChiTaRS; PMM1; human.
DR EvolutionaryTrace; Q92871; -.
DR GeneWiki; PMM1; -.
DR GenomeRNAi; 5372; -.
DR Pharos; Q92871; Tbio.
DR PRO; PR:Q92871; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q92871; protein.
DR Bgee; ENSG00000100417; Expressed in lower esophagus mucosa and 185 other tissues.
DR ExpressionAtlas; Q92871; baseline and differential.
DR Genevisible; Q92871; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IDA:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; TAS:Reactome.
DR GO; GO:0006013; P:mannose metabolic process; IDA:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR CDD; cd02585; HAD_PMM; 1.
DR Gene3D; 3.30.1240.20; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005002; PMM.
DR InterPro; IPR043169; PMM_cap.
DR PANTHER; PTHR10466; PTHR10466; 1.
DR Pfam; PF03332; PMM; 1.
DR SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isomerase; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..262
FT /note="Phosphomannomutase 1"
FT /id="PRO_0000199692"
FT ACT_SITE 19
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:16540464"
FT ACT_SITE 21
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:16540464"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16540464,
FT ECO:0007744|PDB:2FUC, ECO:0007744|PDB:2FUE"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16540464,
FT ECO:0007744|PDB:2FUC, ECO:0007744|PDB:2FUE"
FT BINDING 28
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000269|PubMed:16540464"
FT BINDING 132
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000269|PubMed:16540464"
FT BINDING 143
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000269|PubMed:16540464"
FT BINDING 150
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000269|PubMed:16540464"
FT BINDING 186
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000269|PubMed:16540464"
FT BINDING 188
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000269|PubMed:16540464"
FT BINDING 190
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000269|PubMed:16540464"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16540464,
FT ECO:0007744|PDB:2FUC, ECO:0007744|PDB:2FUE"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16540464,
FT ECO:0007744|PDB:2FUC, ECO:0007744|PDB:2FUE"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16540464,
FT ECO:0007744|PDB:2FUC, ECO:0007744|PDB:2FUE"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16540464,
FT ECO:0007744|PDB:2FUC, ECO:0007744|PDB:2FUE"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35621"
FT CONFLICT 11
FT /note="K -> R (in Ref. 1; AAC51117)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="A -> D (in Ref. 1; AAC51117)"
FT /evidence="ECO:0000305"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:2FUE"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:2FUE"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:2FUE"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2FUE"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:2FUE"
FT HELIX 56..63
FT /evidence="ECO:0007829|PDB:2FUE"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:2FUE"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:2FUE"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:2FUE"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2FUE"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:2FUE"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2FUC"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:2FUE"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:2FUE"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2FUE"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2FUE"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:2FUE"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:2FUE"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2FUE"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:2FUE"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2FUE"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:2FUE"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:2FUE"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:2FUE"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:2FUC"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:2FUE"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:2FUE"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:2FUE"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:2FUE"
SQ SEQUENCE 262 AA; 29747 MW; 1FBA7BFC9C3BB0BB CRC64;
MAVTAQAARR KERVLCLFDV DGTLTPARQK IDPEVAAFLQ KLRSRVQIGV VGGSDYCKIA
EQLGDGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL GEELLQDLIN FCLSYMALLR
LPKKRGTFIE FRNGMLNISP IGRSCTLEER IEFSELDKKE KIREKFVEAL KTEFAGKGLR
FSRGGMISFD VFPEGWDKRY CLDSLDQDSF DTIHFFGNET SPGGNDFEIF ADPRTVGHSV
VSPQDTVQRC REIFFPETAH EA
