NAGPA_HUMAN
ID NAGPA_HUMAN Reviewed; 515 AA.
AC Q9UK23; B2RAS1; Q96EJ8;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase;
DE EC=3.1.4.45;
DE AltName: Full=Mannose 6-phosphate-uncovering enzyme;
DE AltName: Full=Phosphodiester alpha-GlcNAcase;
DE Flags: Precursor;
GN Name=NAGPA;
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] (ISOFORMS 1 AND 2), AND VARIANT ILE-465.
RX PubMed=10551838; DOI=10.1074/jbc.274.46.32778;
RA Kornfeld R.H., Bao M., Brewer K., Noll C., Canfield W.M.;
RT "Molecular cloning and functional expression of two splice forms of human
RT N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase.";
RL J. Biol. Chem. 274:32778-32785(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Colon;
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 [6]
RP PROTEIN SEQUENCE OF 26-36, SIGNAL SEQUENCE CLEAVAGE SITE, PROTEOLYTIC
RP PROCESSING, AND SUBCELLULAR LOCATION.
RX PubMed=12058031; DOI=10.1074/jbc.m202369200;
RA Do H., Lee W.S., Ghosh P., Hollowell T., Canfield W., Kornfeld S.;
RT "Human mannose 6-phosphate-uncovering enzyme is synthesized as a proenzyme
RT that is activated by the endoprotease furin.";
RL J. Biol. Chem. 277:29737-29744(2002).
RN [7]
RP POSSIBLE INVOLVEMENT IN PERSISTENT STUTTERING, AND VARIANTS GLN-84 AND
RP CYS-328.
RX PubMed=20147709; DOI=10.1056/nejmoa0902630;
RA Kang C., Riazuddin S., Mundorff J., Krasnewich D., Friedman P.,
RA Mullikin J.C., Drayna D.;
RT "Mutations in the lysosomal enzyme-targeting pathway and persistent
RT stuttering.";
RL N. Engl. J. Med. 362:677-685(2010).
RN [8]
RP MUTAGENESIS OF CYS-51; CYS-115; CYS-132; ASN-137; CYS-221; GLN-225;
RP THR-227; ARG-247; ASN-284; ASP-286; GLY-287; GLY-288; GLY-289; SER-290;
RP THR-320 AND VAL-322, 3D-STRUCTURE MODELING, DISULFIDE BONDS, AND FUNCTION.
RX PubMed=23572527; DOI=10.1074/jbc.m112.434977;
RA Das D., Lee W.S., Grant J.C., Chiu H.J., Farr C.L., Vance J., Klock H.E.,
RA Knuth M.W., Miller M.D., Elsliger M.A., Deacon A.M., Godzik A.,
RA Lesley S.A., Kornfeld S., Wilson I.A.;
RT "Structure and function of the DUF2233 domain in bacteria and in the human
RT mannose 6-phosphate uncovering enzyme.";
RL J. Biol. Chem. 288:16789-16799(2013).
RN [9]
RP INTERACTION WITH AP4M1, AND MUTAGENESIS OF TYR-486; TYR-488 AND LEU-491.
RX PubMed=26544806; DOI=10.1016/j.ajhg.2015.10.007;
RA Raza M.H., Mattera R., Morell R., Sainz E., Rahn R., Gutierrez J.,
RA Paris E., Root J., Solomon B., Brewer C., Basra M.A., Khan S.,
RA Riazuddin S., Braun A., Bonifacino J.S., Drayna D.;
RT "Association between rare variants in AP4E1, a component of intracellular
RT trafficking, and persistent stuttering.";
RL Am. J. Hum. Genet. 97:715-725(2015).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Catalyzes the second step in the formation of the mannose 6-
CC phosphate targeting signal on lysosomal enzyme oligosaccharides by
CC removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which
CC are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor
CC for Golgi N-acetylglucosaminyltransferases.
CC {ECO:0000269|PubMed:23572527}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-[6-(N-acetyl-alpha-D-glucosaminyl-1-phospho)-alpha-
CC D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein]
CC = H(+) + N(4)-[6-phospho-alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-
CC (glycan)]-L-asparaginyl-[protein] + N-acetyl-D-glucosamine;
CC Xref=Rhea:RHEA:24372, Rhea:RHEA-COMP:14508, Rhea:RHEA-COMP:14509,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:140369,
CC ChEBI:CHEBI:140371, ChEBI:CHEBI:506227; EC=3.1.4.45;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homotetramer arranged as two disulfide-linked homodimers.
CC Interacts with AP4M1. {ECO:0000250|UniProtKB:P68827,
CC ECO:0000269|PubMed:26544806}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:12058031}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12058031}. Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:12058031}. Note=Cis/medial Golgi.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UK23-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UK23-2; Sequence=VSP_012269;
CC Name=3;
CC IsoId=Q9UK23-3; Sequence=VSP_012267, VSP_012268;
CC -!- TISSUE SPECIFICITY: Isoform 2 may be brain-specific.
CC -!- DOMAIN: The tyrosine-based internalization signal may be essential for
CC its retrieval from the plasma membrane to the TGN.
CC -!- DOMAIN: The C-terminal NPFKD sequence is an attractive candidate for
CC either an endocytosis signal acting at the plasma membrane or a
CC retrieval signal acting at the TGN to return the enzyme to the
CC cis/medial-Golgi.
CC -!- PTM: The precursor is cleaved and activated in the trans-Golgi network
CC by a furin endopeptidase. {ECO:0000269|PubMed:12058031}.
CC -!- DISEASE: Note=Defects in NAGPA have been suggested to play a role in
CC susceptibility to persistent stuttering. Stuttering is a common speech
CC disorder characterized by repetitions, prolongations, and interruptions
CC in the flow of speech. {ECO:0000269|PubMed:20147709}.
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DR EMBL; AF187072; AAF08273.1; -; mRNA.
DR EMBL; AK127952; BAG54605.1; -; mRNA.
DR EMBL; AK314320; BAG36968.1; -; mRNA.
DR EMBL; AC026458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85245.1; -; Genomic_DNA.
DR EMBL; BC012194; AAH12194.1; -; mRNA.
DR CCDS; CCDS10527.1; -. [Q9UK23-1]
DR RefSeq; NP_057340.2; NM_016256.3. [Q9UK23-1]
DR AlphaFoldDB; Q9UK23; -.
DR SMR; Q9UK23; -.
DR BioGRID; 119351; 37.
DR IntAct; Q9UK23; 13.
DR MINT; Q9UK23; -.
DR STRING; 9606.ENSP00000310998; -.
DR ChEMBL; CHEMBL5920; -.
DR DrugBank; DB00141; N-Acetylglucosamine.
DR GlyGen; Q9UK23; 6 sites.
DR iPTMnet; Q9UK23; -.
DR PhosphoSitePlus; Q9UK23; -.
DR BioMuta; NAGPA; -.
DR DMDM; 296439239; -.
DR EPD; Q9UK23; -.
DR jPOST; Q9UK23; -.
DR MassIVE; Q9UK23; -.
DR MaxQB; Q9UK23; -.
DR PaxDb; Q9UK23; -.
DR PeptideAtlas; Q9UK23; -.
DR PRIDE; Q9UK23; -.
DR ProteomicsDB; 84708; -. [Q9UK23-1]
DR ProteomicsDB; 84709; -. [Q9UK23-2]
DR ProteomicsDB; 84710; -. [Q9UK23-3]
DR Antibodypedia; 24469; 40 antibodies from 14 providers.
DR DNASU; 51172; -.
DR Ensembl; ENST00000312251.8; ENSP00000310998.3; ENSG00000103174.13. [Q9UK23-1]
DR Ensembl; ENST00000381955.7; ENSP00000371381.3; ENSG00000103174.13. [Q9UK23-2]
DR Ensembl; ENST00000562746.5; ENSP00000455900.1; ENSG00000103174.13. [Q9UK23-3]
DR Ensembl; ENST00000649828.1; ENSP00000498032.1; ENSG00000103174.13. [Q9UK23-3]
DR GeneID; 51172; -.
DR KEGG; hsa:51172; -.
DR MANE-Select; ENST00000312251.8; ENSP00000310998.3; NM_016256.4; NP_057340.2.
DR UCSC; uc002cyg.4; human. [Q9UK23-1]
DR CTD; 51172; -.
DR DisGeNET; 51172; -.
DR GeneCards; NAGPA; -.
DR HGNC; HGNC:17378; NAGPA.
DR HPA; ENSG00000103174; Tissue enhanced (brain).
DR MIM; 607985; gene.
DR neXtProt; NX_Q9UK23; -.
DR OpenTargets; ENSG00000103174; -.
DR PharmGKB; PA134940049; -.
DR VEuPathDB; HostDB:ENSG00000103174; -.
DR eggNOG; ENOG502QRY5; Eukaryota.
DR GeneTree; ENSGT01030000234566; -.
DR HOGENOM; CLU_031673_1_0_1; -.
DR InParanoid; Q9UK23; -.
DR OMA; RPCKCEH; -.
DR OrthoDB; 18592at2759; -.
DR PhylomeDB; Q9UK23; -.
DR TreeFam; TF331920; -.
DR BRENDA; 3.1.4.45; 2681.
DR PathwayCommons; Q9UK23; -.
DR SignaLink; Q9UK23; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 51172; 17 hits in 1076 CRISPR screens.
DR GeneWiki; NAGPA; -.
DR GenomeRNAi; 51172; -.
DR Pharos; Q9UK23; Tbio.
DR PRO; PR:Q9UK23; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9UK23; protein.
DR Bgee; ENSG00000103174; Expressed in middle temporal gyrus and 161 other tissues.
DR ExpressionAtlas; Q9UK23; baseline and differential.
DR Genevisible; Q9UK23; HS.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0003944; F:N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase activity; TAS:ProtInc.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0007040; P:lysosome organization; TAS:ProtInc.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0006622; P:protein targeting to lysosome; TAS:ProtInc.
DR GO; GO:0033299; P:secretion of lysosomal enzymes; IBA:GO_Central.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018711; NAGPA.
DR Pfam; PF09992; NAGPA; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:12058031"
FT PROPEP 26..49
FT /note="Removed in mature form"
FT /id="PRO_0000424659"
FT CHAIN 50..515
FT /note="N-acetylglucosamine-1-phosphodiester alpha-N-
FT acetylglucosaminidase"
FT /id="PRO_0000021788"
FT TOPO_DOM 50..448
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 358..390
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 486..493
FT /note="Mediates the interaction with AP4M1"
FT /evidence="ECO:0000269|PubMed:26544806"
FT MOTIF 488..491
FT /note="Tyrosine-based internalization motif"
FT MOTIF 511..515
FT /note="NPF internalization motif"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..148
FT /evidence="ECO:0000305|PubMed:23572527"
FT DISULFID 132..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000269|PubMed:23572527"
FT DISULFID 307..314
FT /evidence="ECO:0000305|PubMed:23572527"
FT DISULFID 362..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 380..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 307..309
FT /note="CQD -> WQA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012267"
FT VAR_SEQ 310..515
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012268"
FT VAR_SEQ 392..425
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10551838"
FT /id="VSP_012269"
FT VARIANT 84
FT /note="H -> Q (rare variant; found in individuals suffering
FT from stuttering; unknown pathological significance;
FT dbSNP:rs755458782)"
FT /evidence="ECO:0000269|PubMed:20147709"
FT /id="VAR_073225"
FT VARIANT 328
FT /note="R -> C (rare variant; found in individuals suffering
FT from stuttering; unknown pathological significance;
FT dbSNP:rs139526942)"
FT /evidence="ECO:0000269|PubMed:20147709"
FT /id="VAR_073226"
FT VARIANT 465
FT /note="T -> I (in dbSNP:rs7188856)"
FT /evidence="ECO:0000269|PubMed:10551838"
FT /id="VAR_020609"
FT MUTAGEN 51
FT /note="C->M: 65% of wild-type of activity."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 115
FT /note="C->S: 15% of wild-type of activity, and almost no
FT traffic to Golgi."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 132
FT /note="C->V: No traffic to Golgi."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 137
FT /note="N->A: 11% of wild-type of activity."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 221
FT /note="C->L: 10% of wild-type of activity; when associated
FT with M-51."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 225
FT /note="Q->H: 6% of wild-type of activity."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 227
FT /note="T->R: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 247
FT /note="R->A: 87% of wild-type of activity."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 284
FT /note="N->A: 22% of wild-type of activity."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 286
FT /note="D->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 287
FT /note="G->A: 16% of wild-type of activity."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 288
FT /note="G->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 289
FT /note="G->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 290
FT /note="S->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 320
FT /note="T->A: 43% of wild-type of activity."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 322
FT /note="V->A: 67% of wild-type of activity."
FT /evidence="ECO:0000269|PubMed:23572527"
FT MUTAGEN 486
FT /note="Y->A: Interaction with AP4M1 is abolished."
FT /evidence="ECO:0000269|PubMed:26544806"
FT MUTAGEN 488
FT /note="Y->A: Interaction with AP4M1 is abolished."
FT /evidence="ECO:0000269|PubMed:26544806"
FT MUTAGEN 491
FT /note="L->A: Interaction with AP4M1 is abolished."
FT /evidence="ECO:0000269|PubMed:26544806"
FT CONFLICT 259
FT /note="Q -> H (in Ref. 1; AAF08273)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="P -> R (in Ref. 1; AAF08273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 56073 MW; 9B80335E7F9DBAA9 CRC64;
MATSTGRWLL LRLALFGFLW EASGGLDSGA SRDDDLLLPY PRARARLPRD CTRVRAGNRE
HESWPPPPAT PGAGGLAVRT FVSHFRDRAV AGHLTRAVEP LRTFSVLEPG GPGGCAARRR
ATVEETARAA DCRVAQNGGF FRMNSGECLG NVVSDERRVS SSGGLQNAQF GIRRDGTLVT
GYLSEEEVLD TENPFVQLLS GVVWLIRNGS IYINESQATE CDETQETGSF SKFVNVISAR
TAIGHDRKGQ LVLFHADGQT EQRGINLWEM AEFLLKQDVV NAINLDGGGS ATFVLNGTLA
SYPSDHCQDN MWRCPRQVST VVCVHEPRCQ PPDCHGHGTC VDGHCQCTGH FWRGPGCDEL
DCGPSNCSQH GLCTETGCRC DAGWTGSNCS EECPLGWHGP GCQRPCKCEH HCPCDPKTGN
CSVSRVKQCL QPPEATLRAG ELSFFTRTAW LALTLALAFL LLISTAANLS LLLSRAERNR
RLHGDYAYHP LQEMNGEPLA AEKEQPGGAH NPFKD
