ID   MPPA_HUMAN              Reviewed;         525 AA.
AC   Q10713; B4DKL3; E7ET61; Q16639; Q5SXM9; Q8N513;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   11-APR-2003, sequence version 2.
DT   02-JUN-2021, entry version 195.
DE   RecName: Full=Mitochondrial-processing peptidase subunit alpha;
DE   AltName: Full=Alpha-MPP;
DE   AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000305};
DE   AltName: Full=P-55;
DE   Flags: Precursor;
GN   Name=PMPCA; Synonyms=INPP5E, KIAA0123, MPPA;
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).
RC   TISSUE=Bone marrow;
RX   PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA   Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA   Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. III. The
RT   coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 2:37-43(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Bone marrow;
RX   PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA   Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. IV. The
RT   coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 2:167-174(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Colon;
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   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney, Lymph, and Ovary;
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   MASS SPECTROMETRY.
RC   TISSUE=Mammary cancer;
RX   PubMed=11840567;
RX   DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h;
RA   Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
RA   Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
RA   Zvelebil M.J.;
RT   "Cluster analysis of an extensive human breast cancer cell line protein
RT   expression map database.";
RL   Proteomics 2:212-223(2002).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [9]
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   [10]
RP   INVOLVEMENT IN SCAR2, VARIANTS SCAR2 LEU-96; THR-377 AND ARG-515, FUNCTION,
RP   CHARACTERIZATION OF VARIANT SCAR2 THR-377, TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=25808372; DOI=10.1093/brain/awv057;
RA   Jobling R.K., Assoum M., Gakh O., Blaser S., Raiman J.A., Mignot C.,
RA   Roze E., Duerr A., Brice A., Levy N., Prasad C., Paton T., Paterson A.D.,
RA   Roslin N.M., Marshall C.R., Desvignes J.P., Roeckel-Trevisiol N.,
RA   Scherer S.W., Rouleau G.A., Megarbane A., Isaya G., Delague V., Yoon G.;
RT   "PMPCA mutations cause abnormal mitochondrial protein processing in
RT   patients with non-progressive cerebellar ataxia.";
RL   Brain 138:1505-1517(2015).
RN   [11]
RP   CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER PHE-33, AND
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).
RN   [12]
RP   VARIANT SCAR2 MET-256.
RX   PubMed=26657514; DOI=10.1093/brain/awv362;
RG   Care4Rare Consortium;
RA   Choquet K., Zurita-Rendon O., La Piana R., Yang S., Dicaire M.J.,
RA   Boycott K.M., Majewski J., Shoubridge E.A., Brais B., Tetreault M.;
RT   "Autosomal recessive cerebellar ataxia caused by a homozygous mutation in
RT   PMPCA.";
RL   Brain 139:E19-E19(2016).
CC   -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC       mitochondrial processing protease (MPP), which cleaves the
CC       mitochondrial sequence off newly imported precursors proteins.
CC       {ECO:0000269|PubMed:25808372}.
CC   -!- SUBUNIT: Heterodimer of PMPCA (alpha) and PMPCB (beta) subunits,
CC       forming the mitochondrial processing protease (MPP) in which PMPCA is
CC       involved in substrate recognition and binding and PMPCB is the
CC       catalytic subunit. {ECO:0000250|UniProtKB:P11914}.
CC   -!- INTERACTION:
CC       Q10713; P36508: ZNF76; NbExp=3; IntAct=EBI-2514696, EBI-7254550;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P20069}. Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:25808372}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q10713-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q10713-2; Sequence=VSP_054916, VSP_054917;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest expression in
CC       fetal tissues and adult brain, cerebellum and cerebellar vermis.
CC       {ECO:0000269|PubMed:25808372}.
CC   -!- MASS SPECTROMETRY: Mass=54624.57; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11840567};
CC   -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 2 (SCAR2)
CC       [MIM:213200]: A form of spinocerebellar ataxia, a clinically and
CC       genetically heterogeneous group of cerebellar disorders due to
CC       degeneration of the cerebellum with variable involvement of the
CC       brainstem and spinal cord. SCAR2 is characterized by onset of impaired
CC       motor development and ataxic gait in early childhood. Additional
CC       features often include loss of fine motor skills, dysarthria,
CC       nystagmus, cerebellar signs, and delayed cognitive development with
CC       intellectual disability. {ECO:0000269|PubMed:25808372,
CC       ECO:0000269|PubMed:26657514}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC   -!- CAUTION: Does not seem to have a protease activity as it lack the zinc-
CC       binding site. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH33103.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA04643.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA09472.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D21064; BAA04643.1; ALT_INIT; mRNA.
DR   EMBL; D50913; BAA09472.2; ALT_INIT; mRNA.
DR   EMBL; AK296617; BAG59225.1; -; mRNA.
DR   EMBL; AL592301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471090; EAW88232.1; -; Genomic_DNA.
DR   EMBL; BC022949; AAH22949.1; -; mRNA.
DR   EMBL; BC033103; AAH33103.2; ALT_INIT; mRNA.
DR   EMBL; BC111399; AAI11400.1; -; mRNA.
DR   EMBL; BC132724; AAI32725.1; -; mRNA.
DR   EMBL; BC136599; AAI36600.1; -; mRNA.
DR   CCDS; CCDS35180.1; -. [Q10713-1]
DR   CCDS; CCDS65192.1; -. [Q10713-2]
DR   RefSeq; NP_001269873.1; NM_001282944.1. [Q10713-2]
DR   RefSeq; NP_001269875.1; NM_001282946.1.
DR   RefSeq; NP_055975.1; NM_015160.2. [Q10713-1]
DR   SMR; Q10713; -.
DR   BioGRID; 116811; 358.
DR   ComplexPortal; CPX-6243; Mitochondrial processing peptidase complex.
DR   IntAct; Q10713; 62.
DR   MINT; Q10713; -.
DR   STRING; 9606.ENSP00000360782; -.
DR   ChEMBL; CHEMBL4295809; -.
DR   MEROPS; M16.P01; -.
DR   iPTMnet; Q10713; -.
DR   MetOSite; Q10713; -.
DR   PhosphoSitePlus; Q10713; -.
DR   SwissPalm; Q10713; -.
DR   BioMuta; PMPCA; -.
DR   DMDM; 29840846; -.
DR   EPD; Q10713; -.
DR   jPOST; Q10713; -.
DR   MassIVE; Q10713; -.
DR   PaxDb; Q10713; -.
DR   PeptideAtlas; Q10713; -.
DR   PRIDE; Q10713; -.
DR   ProteomicsDB; 4468; -.
DR   ProteomicsDB; 58867; -. [Q10713-1]
DR   Antibodypedia; 18730; 123 antibodies.
DR   DNASU; 23203; -.
DR   Ensembl; ENST00000371717; ENSP00000360782; ENSG00000165688. [Q10713-1]
DR   Ensembl; ENST00000399219; ENSP00000416702; ENSG00000165688. [Q10713-2]
DR   GeneID; 23203; -.
DR   KEGG; hsa:23203; -.
DR   UCSC; uc004chl.5; human. [Q10713-1]
DR   CTD; 23203; -.
DR   DisGeNET; 23203; -.
DR   GeneCards; PMPCA; -.
DR   HGNC; HGNC:18667; PMPCA.
DR   HPA; ENSG00000165688; Low tissue specificity.
DR   MalaCards; PMPCA; -.
DR   MIM; 213200; phenotype.
DR   MIM; 613036; gene.
DR   neXtProt; NX_Q10713; -.
DR   OpenTargets; ENSG00000165688; -.
DR   Orphanet; 1170; Autosomal recessive cerebelloparenchymal disorder type 3.
DR   PharmGKB; PA38629; -.
DR   VEuPathDB; HostDB:ENSG00000165688.11; -.
DR   eggNOG; KOG2067; Eukaryota.
DR   GeneTree; ENSGT00940000156724; -.
DR   HOGENOM; CLU_009902_5_2_1; -.
DR   InParanoid; Q10713; -.
DR   OMA; YTHILNH; -.
DR   OrthoDB; 631107at2759; -.
DR   PhylomeDB; Q10713; -.
DR   TreeFam; TF105031; -.
DR   BRENDA; 3.4.24.64; 2681.
DR   PathwayCommons; Q10713; -.
DR   Reactome; R-HSA-1268020; Mitochondrial protein import.
DR   Reactome; R-HSA-8949664; Processing of SMDT1.
DR   SignaLink; Q10713; -.
DR   BioGRID-ORCS; 23203; 719 hits in 1005 CRISPR screens.
DR   ChiTaRS; PMPCA; human.
DR   GeneWiki; PMPCA; -.
DR   GenomeRNAi; 23203; -.
DR   Pharos; Q10713; Tbio.
DR   PRO; PR:Q10713; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q10713; protein.
DR   Bgee; ENSG00000165688; Expressed in heart left ventricle and 230 other tissues.
DR   ExpressionAtlas; Q10713; baseline and differential.
DR   Genevisible; Q10713; HS.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; TAS:Reactome.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IDA:UniProtKB.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR037715; PMPCA.
DR   PANTHER; PTHR11851:SF192; PTHR11851:SF192; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Disease variant; Membrane;
KW   Mental retardation; Mitochondrion; Mitochondrion inner membrane;
KW   Neurodegeneration; Reference proteome; Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0007744|PubMed:25944712"
FT   CHAIN           34..525
FT                   /note="Mitochondrial-processing peptidase subunit alpha"
FT                   /id="PRO_0000026767"
FT   MOD_RES         64
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DC61"
FT   MOD_RES         299
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         1..46
FT                   /note="MAAVVLAATRLLRGSGSWGCSRLRFGPPAYRRFSSGGAYPNIPLSS -> MK
FT                   RNTLVELLTFWKNWHFRLLLDLTAKMKFCLRWKSMGVSVTARHQ (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054916"
FT   VAR_SEQ         47..177
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054917"
FT   VARIANT         96
FT                   /note="S -> L (in SCAR2; dbSNP:rs869025292)"
FT                   /evidence="ECO:0000269|PubMed:25808372"
FT                   /id="VAR_076237"
FT   VARIANT         256
FT                   /note="V -> M (in SCAR2; dbSNP:rs746549806)"
FT                   /evidence="ECO:0000269|PubMed:26657514"
FT                   /id="VAR_076238"
FT   VARIANT         377
FT                   /note="A -> T (in SCAR2; impairs cleavage of FXN; does not
FT                   impair cleavage of DLD, NFS1 and PRDX3; dbSNP:rs753611141)"
FT                   /evidence="ECO:0000269|PubMed:25808372"
FT                   /id="VAR_076239"
FT   VARIANT         515
FT                   /note="G -> R (in SCAR2; dbSNP:rs869025293)"
FT                   /evidence="ECO:0000269|PubMed:25808372"
FT                   /id="VAR_076240"
FT   CONFLICT        495
FT                   /note="G -> C (in Ref. 6; AAH22949)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        505
FT                   /note="H -> D (in Ref. 1; BAA04643)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   525 AA;  58253 MW;  2751E7FCDC864E3F CRC64;
     MAAVVLAATR LLRGSGSWGC SRLRFGPPAY RRFSSGGAYP NIPLSSPLPG VPKPVFATVD
     GQEKFETKVT TLDNGLRVAS QNKFGQFCTV GILINSGSRY EAKYLSGIAH FLEKLAFSST
     ARFDSKDEIL LTLEKHGGIC DCQTSRDTTM YAVSADSKGL DTVVALLADV VLQPRLTDEE
     VEMTRMAVQF ELEDLNLRPD PEPLLTEMIH EAAYRENTVG LHRFCPTENV AKINREVLHS
     YLRNYYTPDR MVLAGVGVEH EHLVDCARKY LLGVQPAWGS AEAVDIDRSV AQYTGGIAKL
     ERDMSNVSLG PTPIPELTHI MVGLESCSFL EEDFIPFAVL NMMMGGGGSF SAGGPGKGMF
     SRLYLNVLNR HHWMYNATSY HHSYEDTGLL CIHASADPRQ VREMVEIITK EFILMGGTVD
     TVELERAKTQ LTSMLMMNLE SRPVIFEDVG RQVLATRSRK LPHELCTLIR NVKPEDVKRV
     ASKMLRGKPA VAALGDLTDL PTYEHIQTAL SSKDGRLPRT YRLFR
//