PCKGM_HUMAN
ID PCKGM_HUMAN Reviewed; 640 AA.
AC Q16822; B4DW73; O43253; Q86U01; Q9BV62;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP], mitochondrial;
DE Short=PEPCK-M;
DE EC=4.1.1.32;
DE Flags: Precursor;
GN Name=PCK2; Synonyms=PEPCK2;
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] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8645161; DOI=10.1042/bj3150807;
RA Modaressi S., Christ B., Bratke J., Zahn S., Heise T., Jungermann K.;
RT "Molecular cloning, sequencing and expression of the cDNA of the
RT mitochondrial form of phosphoenolpyruvate carboxykinase from human liver.";
RL Biochem. J. 315:807-814(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=9657976; DOI=10.1042/bj3330359;
RA Modaressi S., Brechtel K., Christ B., Jungermann K.;
RT "Human mitochondrial phosphoenolpyruvate carboxykinase 2 gene. Structure,
RT chromosomal localization and tissue-specific expression.";
RL Biochem. J. 333:359-366(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42; SER-115; THR-196 AND
RP SER-304, AND IDENTIFICATION BY 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).
RN [9]
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 conversion of oxaloacetate (OAA) to
CC phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic
CC pathway that produces glucose from lactate and other precursors derived
CC from the citric acid cycle. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC Q16822; P84022: SMAD3; NbExp=2; IntAct=EBI-2825219, EBI-347161;
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q16822-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16822-2; Sequence=VSP_038783;
CC Name=3;
CC IsoId=Q16822-3; Sequence=VSP_059389;
CC -!- DISEASE: Mitochondrial phosphoenolpyruvate carboxykinase deficiency (M-
CC PEPCKD) [MIM:261650]: Metabolic disorder resulting from impaired
CC gluconeogenesis. It is a rare disease with less than 10 cases reported
CC in the literature. Clinical characteristics include hypotonia,
CC hepatomegaly, failure to thrive, lactic acidosis and hypoglycemia.
CC Autopsy reveals fatty infiltration of both the liver and kidneys. The
CC disorder is transmitted as an autosomal recessive trait. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: In eukaryotes there are two isozymes: a cytoplasmic one
CC and a mitochondrial one.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD62600.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X92720; CAA63380.1; -; mRNA.
DR EMBL; Y11484; CAA72272.1; -; Genomic_DNA.
DR EMBL; BX248272; CAD62600.1; ALT_INIT; mRNA.
DR EMBL; AK301400; BAG62935.1; -; mRNA.
DR EMBL; AK316206; BAH14577.1; -; mRNA.
DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF455834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001454; AAH01454.1; -; mRNA.
DR CCDS; CCDS41928.1; -. [Q16822-2]
DR CCDS; CCDS76660.1; -. [Q16822-3]
DR CCDS; CCDS9609.1; -. [Q16822-1]
DR PIR; S69546; S69546.
DR RefSeq; NP_001018083.2; NM_001018073.2. [Q16822-2]
DR RefSeq; NP_001278485.1; NM_001291556.1. [Q16822-3]
DR RefSeq; NP_001294983.1; NM_001308054.1. [Q16822-3]
DR RefSeq; NP_004554.3; NM_004563.3. [Q16822-1]
DR AlphaFoldDB; Q16822; -.
DR SMR; Q16822; -.
DR BioGRID; 111137; 90.
DR IntAct; Q16822; 54.
DR MINT; Q16822; -.
DR STRING; 9606.ENSP00000216780; -.
DR ChEMBL; CHEMBL3096; -.
DR DrugBank; DB00787; Acyclovir.
DR GlyGen; Q16822; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16822; -.
DR PhosphoSitePlus; Q16822; -.
DR SwissPalm; Q16822; -.
DR BioMuta; PCK2; -.
DR DMDM; 290457671; -.
DR SWISS-2DPAGE; Q16822; -.
DR EPD; Q16822; -.
DR jPOST; Q16822; -.
DR MassIVE; Q16822; -.
DR MaxQB; Q16822; -.
DR PaxDb; Q16822; -.
DR PeptideAtlas; Q16822; -.
DR PRIDE; Q16822; -.
DR ProteomicsDB; 5315; -.
DR ProteomicsDB; 61082; -. [Q16822-1]
DR ProteomicsDB; 61083; -. [Q16822-2]
DR TopDownProteomics; Q16822-2; -. [Q16822-2]
DR Antibodypedia; 8846; 306 antibodies from 36 providers.
DR DNASU; 5106; -.
DR Ensembl; ENST00000216780.9; ENSP00000216780.4; ENSG00000100889.12. [Q16822-1]
DR Ensembl; ENST00000396973.8; ENSP00000380171.4; ENSG00000100889.12. [Q16822-2]
DR Ensembl; ENST00000545054.6; ENSP00000441826.2; ENSG00000100889.12. [Q16822-3]
DR Ensembl; ENST00000561286.5; ENSP00000454011.1; ENSG00000100889.12. [Q16822-3]
DR Ensembl; ENST00000644679.1; ENSP00000496102.1; ENSG00000285241.2. [Q16822-3]
DR Ensembl; ENST00000645217.2; ENSP00000494919.1; ENSG00000285241.2. [Q16822-1]
DR Ensembl; ENST00000645536.1; ENSP00000496343.1; ENSG00000285241.2. [Q16822-3]
DR Ensembl; ENST00000645709.1; ENSP00000494029.1; ENSG00000285241.2. [Q16822-2]
DR GeneID; 5106; -.
DR KEGG; hsa:5106; -.
DR MANE-Select; ENST00000216780.9; ENSP00000216780.4; NM_004563.4; NP_004554.3.
DR UCSC; uc001wlt.4; human. [Q16822-1]
DR UCSC; uc010tnw.3; human.
DR CTD; 5106; -.
DR DisGeNET; 5106; -.
DR GeneCards; PCK2; -.
DR HGNC; HGNC:8725; PCK2.
DR HPA; ENSG00000100889; Group enriched (intestine, kidney, liver).
DR MalaCards; PCK2; -.
DR MIM; 261650; phenotype.
DR MIM; 614095; gene.
DR neXtProt; NX_Q16822; -.
DR OpenTargets; ENSG00000100889; -.
DR Orphanet; 2880; Phosphoenolpyruvate carboxykinase deficiency.
DR PharmGKB; PA33070; -.
DR VEuPathDB; HostDB:ENSG00000100889; -.
DR eggNOG; KOG3749; Eukaryota.
DR GeneTree; ENSGT00390000001912; -.
DR HOGENOM; CLU_028872_1_0_1; -.
DR InParanoid; Q16822; -.
DR OMA; PAGKKHY; -.
DR OrthoDB; 286671at2759; -.
DR PhylomeDB; Q16822; -.
DR TreeFam; TF314402; -.
DR BioCyc; MetaCyc:HS02160-MON; -.
DR BRENDA; 4.1.1.32; 2681.
DR PathwayCommons; Q16822; -.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR SignaLink; Q16822; -.
DR SIGNOR; Q16822; -.
DR UniPathway; UPA00138; -.
DR BioGRID-ORCS; 5106; 21 hits in 1076 CRISPR screens.
DR ChiTaRS; PCK2; human.
DR GenomeRNAi; 5106; -.
DR Pharos; Q16822; Tbio.
DR PRO; PR:Q16822; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q16822; protein.
DR Bgee; ENSG00000100889; Expressed in right lobe of liver and 103 other tissues.
DR ExpressionAtlas; Q16822; baseline and differential.
DR Genevisible; Q16822; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IBA:GO_Central.
DR GO; GO:0004611; F:phosphoenolpyruvate carboxykinase activity; TAS:ProtInc.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IBA:GO_Central.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0046327; P:glycerol biosynthetic process from pyruvate; IBA:GO_Central.
DR GO; GO:0070365; P:hepatocyte differentiation; IBA:GO_Central.
DR GO; GO:0006116; P:NADH oxidation; IEA:Ensembl.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0019543; P:propionate catabolic process; IBA:GO_Central.
DR GO; GO:0033993; P:response to lipid; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR CDD; cd00819; PEPCK_GTP; 1.
DR Gene3D; 3.40.449.10; -; 1.
DR Gene3D; 3.90.228.20; -; 1.
DR HAMAP; MF_00452; PEPCK_GTP; 1.
DR InterPro; IPR018091; PEP_carboxykin_GTP_CS.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008209; PEP_carboxykinase_GTP.
DR InterPro; IPR035077; PEP_carboxykinase_GTP_C.
DR InterPro; IPR035078; PEP_carboxykinase_GTP_N.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR PANTHER; PTHR11561; PTHR11561; 1.
DR Pfam; PF00821; PEPCK_GTP; 1.
DR Pfam; PF17297; PEPCK_N; 1.
DR PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR SUPFAM; SSF68923; SSF68923; 1.
DR PROSITE; PS00505; PEPCK_GTP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Decarboxylase; Gluconeogenesis;
KW GTP-binding; Lyase; Manganese; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 33..640
FT /note="Phosphoenolpyruvate carboxykinase [GTP],
FT mitochondrial"
FT /id="PRO_0000023568"
FT ACT_SITE 306
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 253..255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 262
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 282
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 305..310
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 329
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 421..423
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 423
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 454
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 548..551
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT MOD_RES 42
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 88
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35558"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 457
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BH04"
FT VAR_SEQ 1..134
FT /note="Missing (in isoform 3)"
FT /id="VSP_059389"
FT VAR_SEQ 413..640
FT /note="DKEPCAHPNSRFCAPARQCPIMDPAWEAPEGVPIDAIIFGGRRPKGVPLVYE
FT AFNWRHGVFVGSAMRSESTAAAEHKGKIIMHDPFAMRPFFGYNFGHYLEHWLSMEGRKG
FT AQLPRIFHVNWFRRDEAGHFLWPGFGENARVLDWICRRLEGEDSARETPIGLVPKEGAL
FT DLSGLRAIDTTQLFSLPKDFWEQEVRDIRSYLTEQVNQDLPKEVLAELEALERRVHKM
FT -> MCGGEGVAQPPGLSTLMVEKLSPQPPTIF (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_038783"
FT VARIANT 31
FT /note="R -> Q (in dbSNP:rs2229660)"
FT /id="VAR_042445"
FT VARIANT 64
FT /note="D -> N (in dbSNP:rs10132601)"
FT /id="VAR_042446"
FT VARIANT 406
FT /note="G -> S (in dbSNP:rs17101262)"
FT /id="VAR_042447"
FT VARIANT 521
FT /note="R -> H (in dbSNP:rs35618680)"
FT /id="VAR_056662"
FT CONFLICT 121
FT /note="P -> Q (in Ref. 3; CAD62600)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="R -> C (in Ref. 1; CAA63380)"
FT /evidence="ECO:0000305"
FT CONFLICT 296..298
FT /note="RYV -> ALC (in Ref. 1; CAA63380 and 2; CAA72272)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="S -> R (in Ref. 1; CAA63380 and 2; CAA72272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 640 AA; 70699 MW; DCE561252EBF8871 CRC64;
MAALYRPGLR LNWHGLSPLG WPSCRSIQTL RVLSGDLGQL PTGIRDFVEH SARLCQPEGI
HICDGTEAEN TATLTLLEQQ GLIRKLPKYN NCWLARTDPK DVARVESKTV IVTPSQRDTV
PLPPGGARGQ LGNWMSPADF QRAVDERFPG CMQGRTMYVL PFSMGPVGSP LSRIGVQLTD
SAYVVASMRI MTRLGTPVLQ ALGDGDFVKC LHSVGQPLTG QGEPVSQWPC NPEKTLIGHV
PDQREIISFG SGYGGNSLLG KKCFALRIAS RLARDEGWLA EHMLILGITS PAGKKRYVAA
AFPSACGKTN LAMMRPALPG WKVECVGDDI AWMRFDSEGR LRAINPENGF FGVAPGTSAT
TNPNAMATIQ SNTIFTNVAE TSDGGVYWEG IDQPLPPGVT VTSWLGKPWK PGDKEPCAHP
NSRFCAPARQ CPIMDPAWEA PEGVPIDAII FGGRRPKGVP LVYEAFNWRH GVFVGSAMRS
ESTAAAEHKG KIIMHDPFAM RPFFGYNFGH YLEHWLSMEG RKGAQLPRIF HVNWFRRDEA
GHFLWPGFGE NARVLDWICR RLEGEDSARE TPIGLVPKEG ALDLSGLRAI DTTQLFSLPK
DFWEQEVRDI RSYLTEQVNQ DLPKEVLAEL EALERRVHKM
