MLF1_HUMAN
ID MLF1_HUMAN Reviewed; 268 AA.
AC P58340; E9PEU9; Q2TLE3; Q2TLE5; Q8N8F8; Q96MH1;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Myeloid leukemia factor 1;
DE AltName: Full=Myelodysplasia-myeloid leukemia factor 1;
GN Name=MLF1;
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), AND CHROMOSOMAL TRANSLOCATION.
RC TISSUE=Skeletal muscle, and Testis;
RX PubMed=8570204;
RA Yoneda-Kato N., Look A.T., Kirstein M.N., Valentine M.B., Raimondi S.C.,
RA Cohen K.J., Carroll A.J., Morris S.W.;
RT "The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid
RT leukemia produces a novel fusion gene, NPM-MLF1.";
RL Oncogene 12:265-275(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5).
RA Feng X., Ling S., Zhang H., Song X., Wang G., Chen K., Zhu C.;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
RC TISSUE=Brain, and 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 INTERACTION WITH CENPU.
RX PubMed=15116101; DOI=10.1038/sj.onc.1207448;
RA Hanissian S.H., Akbar U., Teng B., Janjetovic Z., Hoffmann A.,
RA Hitzler J.K., Iscove N., Hamre K., Du X., Tong Y., Mukatira S.,
RA Robertson J.H., Morris S.W.;
RT "cDNA cloning and characterization of a novel gene encoding the MLF1-
RT interacting protein MLF1IP.";
RL Oncogene 23:3700-3707(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH COPS3.
RX PubMed=15861129; DOI=10.1038/sj.emboj.7600656;
RA Yoneda-Kato N., Tomoda K., Umehara M., Arata Y., Kato J.-Y.;
RT "Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via COP9
RT signalosome subunit 3.";
RL EMBO J. 24:1739-1749(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-32, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 29-42 IN COMPLEX WITH YWHAE, AND
RP PHOSPHORYLATION AT SER-34.
RX PubMed=22151054; DOI=10.1111/j.1742-4658.2011.08445.x;
RA Molzan M., Weyand M., Rose R., Ottmann C.;
RT "Structural insights of the MLF1/14-3-3 interaction.";
RL FEBS J. 279:563-571(2012).
CC -!- FUNCTION: Involved in lineage commitment of primary hemopoietic
CC progenitors by restricting erythroid formation and enhancing myeloid
CC formation. Interferes with erythropoietin-induced erythroid terminal
CC differentiation by preventing cells from exiting the cell cycle through
CC suppression of CDKN1B/p27Kip1 levels. Suppresses COP1 activity via CSN3
CC which activates p53 and induces cell cycle arrest. Binds DNA and
CC affects the expression of a number of genes so may function as a
CC transcription factor in the nucleus. {ECO:0000269|PubMed:15861129}.
CC -!- SUBUNIT: Interacts with CENPU. Also interacts with NRBP1/MADM,
CC YWHAZ/14-3-3-zeta and HNRPUL2/MANP. NRBP1 recruits a serine kinase
CC which phosphorylates both itself and MLF1. Phosphorylated MLF1 then
CC binds to YWHAZ and is retained in the cytoplasm. Retained in the
CC nucleus by binding to HNRPUL2. Binds to COPS3/CSN3 which is required
CC for suppression of COP1 and activation of p53.
CC {ECO:0000269|PubMed:15116101, ECO:0000269|PubMed:15861129,
CC ECO:0000269|PubMed:22151054}.
CC -!- INTERACTION:
CC P58340; Q9BTE6-2: AARSD1; NbExp=2; IntAct=EBI-721328, EBI-9357295;
CC P58340; O75190: DNAJB6; NbExp=2; IntAct=EBI-721328, EBI-1053164;
CC P58340; P43364: MAGEA11; NbExp=5; IntAct=EBI-721328, EBI-739552;
CC P58340; Q15773: MLF2; NbExp=2; IntAct=EBI-721328, EBI-1051875;
CC P58340; Q13200: PSMD2; NbExp=2; IntAct=EBI-721328, EBI-357648;
CC P58340; P62258: YWHAE; NbExp=3; IntAct=EBI-721328, EBI-356498;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QWV4}. Nucleus
CC {ECO:0000250|UniProtKB:Q9QWV4}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9QWV4}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q9QWV4}. Note=Shuttles between the
CC cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q9QWV4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P58340-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P58340-2; Sequence=VSP_043130, VSP_043131;
CC Name=3;
CC IsoId=P58340-3; Sequence=VSP_043725, VSP_043726;
CC Name=5;
CC IsoId=P58340-5; Sequence=VSP_043130;
CC Name=4;
CC IsoId=P58340-4; Sequence=VSP_043130, VSP_043726;
CC -!- TISSUE SPECIFICITY: Most abundant in testis, ovary, skeletal muscle,
CC heart, kidney and colon. Low expression in spleen, thymus and
CC peripheral blood leukocytes.
CC -!- PTM: Phosphorylation is required for binding to YWHAZ. {ECO:0000250}.
CC -!- DISEASE: Note=A chromosomal aberration involving MLF1 is a cause of
CC myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with
CC NPM1/NPM. {ECO:0000269|PubMed:8570204}.
CC -!- SIMILARITY: Belongs to the MLF family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MLF1ID18.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L49054; AAA99997.1; -; mRNA.
DR EMBL; AY848700; AAX46015.1; -; mRNA.
DR EMBL; AY848702; AAX46017.1; -; mRNA.
DR EMBL; AK056948; BAB71320.1; -; mRNA.
DR EMBL; AK096889; BAC04885.1; -; mRNA.
DR EMBL; AK297488; BAG59906.1; -; mRNA.
DR EMBL; AC025033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78689.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78690.1; -; Genomic_DNA.
DR EMBL; BC007045; AAH07045.1; -; mRNA.
DR CCDS; CCDS3182.1; -. [P58340-1]
DR CCDS; CCDS46945.1; -. [P58340-5]
DR CCDS; CCDS56286.1; -. [P58340-4]
DR CCDS; CCDS56287.1; -. [P58340-4]
DR CCDS; CCDS56288.1; -. [P58340-2]
DR RefSeq; NP_001123628.1; NM_001130156.2. [P58340-5]
DR RefSeq; NP_001123629.1; NM_001130157.2. [P58340-5]
DR RefSeq; NP_001182361.1; NM_001195432.1. [P58340-4]
DR RefSeq; NP_001182362.1; NM_001195433.1. [P58340-2]
DR RefSeq; NP_001182363.1; NM_001195434.1. [P58340-4]
DR RefSeq; NP_071888.1; NM_022443.4. [P58340-1]
DR RefSeq; XP_005247537.1; XM_005247480.2.
DR RefSeq; XP_011511154.1; XM_011512852.2.
DR RefSeq; XP_011511155.1; XM_011512853.2.
DR PDB; 3UAL; X-ray; 1.80 A; P=29-42.
DR PDB; 3UBW; X-ray; 1.90 A; P=29-42.
DR PDB; 6Y8E; X-ray; 1.42 A; P=31-38.
DR PDBsum; 3UAL; -.
DR PDBsum; 3UBW; -.
DR PDBsum; 6Y8E; -.
DR AlphaFoldDB; P58340; -.
DR SMR; P58340; -.
DR BioGRID; 110437; 119.
DR ELM; P58340; -.
DR IntAct; P58340; 132.
DR MINT; P58340; -.
DR STRING; 9606.ENSP00000376568; -.
DR MoonDB; P58340; Predicted.
DR iPTMnet; P58340; -.
DR PhosphoSitePlus; P58340; -.
DR BioMuta; MLF1; -.
DR DMDM; 17368170; -.
DR EPD; P58340; -.
DR jPOST; P58340; -.
DR MassIVE; P58340; -.
DR MaxQB; P58340; -.
DR PeptideAtlas; P58340; -.
DR PRIDE; P58340; -.
DR ProteomicsDB; 57064; -. [P58340-1]
DR ProteomicsDB; 57065; -. [P58340-2]
DR ProteomicsDB; 57066; -. [P58340-3]
DR ProteomicsDB; 57067; -. [P58340-4]
DR ProteomicsDB; 61497; -.
DR Antibodypedia; 18436; 572 antibodies from 34 providers.
DR DNASU; 4291; -.
DR Ensembl; ENST00000355893.11; ENSP00000348157.5; ENSG00000178053.20. [P58340-1]
DR Ensembl; ENST00000359117.9; ENSP00000352025.5; ENSG00000178053.20. [P58340-5]
DR Ensembl; ENST00000392822.4; ENSP00000376568.3; ENSG00000178053.20. [P58340-3]
DR Ensembl; ENST00000469452.5; ENSP00000418595.1; ENSG00000178053.20. [P58340-2]
DR Ensembl; ENST00000471745.5; ENSP00000420134.1; ENSG00000178053.20. [P58340-4]
DR Ensembl; ENST00000477042.6; ENSP00000419637.2; ENSG00000178053.20. [P58340-4]
DR Ensembl; ENST00000478894.7; ENSP00000417777.3; ENSG00000178053.20. [P58340-3]
DR Ensembl; ENST00000482628.5; ENSP00000417141.1; ENSG00000178053.20. [P58340-5]
DR Ensembl; ENST00000484955.5; ENSP00000417835.1; ENSG00000178053.20. [P58340-5]
DR Ensembl; ENST00000618075.4; ENSP00000484169.1; ENSG00000178053.20. [P58340-2]
DR Ensembl; ENST00000651874.1; ENSP00000498363.1; ENSG00000178053.20. [P58340-5]
DR GeneID; 4291; -.
DR KEGG; hsa:4291; -.
DR UCSC; uc003fbx.4; human. [P58340-1]
DR CTD; 4291; -.
DR DisGeNET; 4291; -.
DR GeneCards; MLF1; -.
DR HGNC; HGNC:7125; MLF1.
DR HPA; ENSG00000178053; Tissue enhanced (skeletal muscle, testis).
DR MalaCards; MLF1; -.
DR MIM; 601402; gene.
DR neXtProt; NX_P58340; -.
DR OpenTargets; ENSG00000178053; -.
DR PharmGKB; PA30843; -.
DR VEuPathDB; HostDB:ENSG00000178053; -.
DR eggNOG; KOG4049; Eukaryota.
DR GeneTree; ENSGT00390000005023; -.
DR InParanoid; P58340; -.
DR PhylomeDB; P58340; -.
DR TreeFam; TF317561; -.
DR PathwayCommons; P58340; -.
DR SignaLink; P58340; -.
DR SIGNOR; P58340; -.
DR BioGRID-ORCS; 4291; 9 hits in 1081 CRISPR screens.
DR ChiTaRS; MLF1; human.
DR GeneWiki; MLF1; -.
DR GenomeRNAi; 4291; -.
DR Pharos; P58340; Tbio.
DR PRO; PR:P58340; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P58340; protein.
DR Bgee; ENSG00000178053; Expressed in left testis and 209 other tissues.
DR ExpressionAtlas; P58340; baseline and differential.
DR Genevisible; P58340; HS.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0002318; P:myeloid progenitor cell differentiation; ISS:UniProtKB.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IPI:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IPI:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
DR IDEAL; IID00458; -.
DR InterPro; IPR019376; Myeloid_leukemia_factor.
DR PANTHER; PTHR13105; PTHR13105; 1.
DR Pfam; PF10248; Mlf1IP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell projection;
KW Chromosomal rearrangement; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..268
FT /note="Myeloid leukemia factor 1"
FT /id="PRO_0000220752"
FT REGION 44..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..125
FT /note="Interaction with COPS3"
FT /evidence="ECO:0000269|PubMed:15861129"
FT REGION 209..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 16..17
FT /note="Breakpoint for translocation to form NPM-MLF1"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22151054"
FT VAR_SEQ 1..25
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_043130"
FT VAR_SEQ 1..15
FT /note="MFRMLNSSFEDDPFF -> MLKEVLQREGKSYKSETLMYIKKARASENKL
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043725"
FT VAR_SEQ 65
FT /note="T -> TATSCSLVPFGDFGGM (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043726"
FT VAR_SEQ 94..136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_043131"
FT VARIANT 226
FT /note="P -> T (in dbSNP:rs15967)"
FT /id="VAR_022070"
SQ SEQUENCE 268 AA; 30627 MW; 08774217329F737A CRC64;
MFRMLNSSFE DDPFFSESIL AHRENMRQMI RSFSEPFGRD LLSISDGRGR AHNRRGHNDG
EDSLTHTDVS SFQTMDQMVS NMRNYMQKLE RNFGQLSVDP NGHSFCSSSV MTYSKIGDEP
PKVFQASTQT RRAPGGIKET RKAMRDSDSG LEKMAIGHHI HDRAHVIKKS KNKKTGDEEV
NQEFINMNES DAHAFDEEWQ SEVLKYKPGR HNLGNTRMRS VGHENPGSRE LKRREKPQQS
PAIEHGRRSN VLGDKLHIKG SSVKSNKK
