MPPA_HUMAN
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 03-AUG-2022, entry version 199.
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 AlphaFoldDB; Q10713; -.
DR SMR; Q10713; -.
DR BioGRID; 116811; 373.
DR ComplexPortal; CPX-6243; Mitochondrial processing peptidase complex.
DR IntAct; Q10713; 65.
DR MINT; Q10713; -.
DR STRING; 9606.ENSP00000360782; -.
DR ChEMBL; CHEMBL4295809; -.
DR MEROPS; M16.971; -.
DR MEROPS; M16.P01; -.
DR GlyGen; Q10713; 1 site, 1 O-linked glycan (1 site).
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 MaxQB; Q10713; -.
DR PaxDb; Q10713; -.
DR PeptideAtlas; Q10713; -.
DR PRIDE; Q10713; -.
DR ProteomicsDB; 4468; -.
DR ProteomicsDB; 58867; -. [Q10713-1]
DR Antibodypedia; 18730; 130 antibodies from 25 providers.
DR DNASU; 23203; -.
DR Ensembl; ENST00000371717.8; ENSP00000360782.3; ENSG00000165688.12. [Q10713-1]
DR Ensembl; ENST00000399219.7; ENSP00000416702.2; ENSG00000165688.12. [Q10713-2]
DR GeneID; 23203; -.
DR KEGG; hsa:23203; -.
DR MANE-Select; ENST00000371717.8; ENSP00000360782.3; NM_015160.3; NP_055975.1.
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; -.
DR eggNOG; KOG2067; Eukaryota.
DR GeneTree; ENSGT00940000156724; -.
DR HOGENOM; CLU_009902_5_2_1; -.
DR InParanoid; Q10713; -.
DR OMA; LKYHHSP; -.
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; 733 hits in 1091 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 right lobe of liver and 189 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:0017087; C:mitochondrial processing peptidase complex; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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;
KW Intellectual disability; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Neurodegeneration; Reference proteome;
KW 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
