RPP21_HUMAN
ID RPP21_HUMAN Reviewed; 154 AA.
AC Q9H633; A2AAZ8; B0S834; B0S835; Q5JPL9; Q5JPM1; Q5STF8; Q5STF9; Q5STG2;
AC Q5SU41; Q5SU42; Q86Y49; Q86Y50; Q86Y51; Q96F16;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Ribonuclease P protein subunit p21;
DE Short=RNaseP protein p21;
DE AltName: Full=Ribonuclease P/MRP 21 kDa subunit;
DE AltName: Full=Ribonucleoprotein V;
GN Name=RPP21; Synonyms=C6orf135, CAT60;
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 SUBCELLULAR LOCATION.
RX PubMed=11497433; DOI=10.1017/s1355838201010469;
RA Jarrous N., Reiner R., Wesolowski D., Mann H., Guerrier-Takada C.,
RA Altman S.;
RT "Function and subnuclear distribution of Rpp21, a protein subunit of the
RT human ribonucleoprotein ribonuclease P.";
RL RNA 7:1153-1164(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT HIS-77.
RC TISSUE=Spleen;
RA Raha-Chowdhury R., Andrews S.R., Gruen J.R., Weissman S.M.;
RT "Genes from major histocompatibility complex (MHC) class I region from HLA-
RT C to HLA-A.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Small intestine;
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], AND VARIANTS HIS-77 AND
RP LYS-149.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP HIS-77.
RC TISSUE=Hypothalamus, and Skin;
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 IN RNASE P COMPLEX, AND SUBUNIT.
RX PubMed=16723659; DOI=10.1261/rna.2293906;
RA Welting T.J., Kikkert B.J., van Venrooij W.J., Pruijn G.J.;
RT "Differential association of protein subunits with the human RNase MRP and
RT RNase P complexes.";
RL RNA 12:1373-1382(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9] {ECO:0007744|PDB:6AHR, ECO:0007744|PDB:6AHU}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.66 ANGSTROMS) OF RNASE P HOLOENZYME IN
RP COMPLEX WITH TRNA, FUNCTION, AND SUBUNIT.
RX PubMed=30454648; DOI=10.1016/j.cell.2018.10.003;
RA Wu J., Niu S., Tan M., Huang C., Li M., Song Y., Wang Q., Chen J., Shi S.,
RA Lan P., Lei M.;
RT "Cryo-EM Structure of the Human Ribonuclease P Holoenzyme.";
RL Cell 175:1393-1404.e11(2018).
CC -!- FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that
CC generates mature tRNA molecules by cleaving their 5'-ends.
CC {ECO:0000269|PubMed:30454648}.
CC -!- SUBUNIT: RNase P consists of a catalytic RNA moiety and about 10
CC protein subunits; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30,
CC RPP38 and RPP40 (PubMed:16723659, PubMed:30454648). Within the RNase P
CC complex, POP1, POP7 and RPP25 form the 'finger' subcomplex, POP5,
CC RPP14, RPP40 and homodimeric RPP30 form the 'palm' subcomplex, and
CC RPP21, POP4 and RPP38 form the 'wrist' subcomplex. All subunits of the
CC RNase P complex interact with the catalytic RNA (PubMed:30454648).
CC {ECO:0000269|PubMed:16723659, ECO:0000269|PubMed:30454648}.
CC -!- INTERACTION:
CC Q9H633; O75818: RPP40; NbExp=2; IntAct=EBI-366586, EBI-366505;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11497433}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=CAT60-V1;
CC IsoId=Q9H633-1; Sequence=Displayed;
CC Name=2; Synonyms=CAT60-V3;
CC IsoId=Q9H633-2; Sequence=VSP_010695;
CC Name=3; Synonyms=CAT60-V4;
CC IsoId=Q9H633-3; Sequence=VSP_010696;
CC Name=4;
CC IsoId=Q9H633-4; Sequence=VSP_044901;
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BI598757; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF212152; AAK39955.2; -; mRNA.
DR EMBL; AJ504713; CAD44289.1; -; mRNA.
DR EMBL; AJ504714; CAD44290.1; -; mRNA.
DR EMBL; AJ504715; CAD44291.1; -; mRNA.
DR EMBL; AJ504716; CAD44292.1; -; mRNA.
DR EMBL; AK026291; BAB15433.1; -; mRNA.
DR EMBL; AL662832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL773535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX294158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03287.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03288.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03289.1; -; Genomic_DNA.
DR EMBL; BC011730; AAH11730.1; -; mRNA.
DR EMBL; BI598757; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS4679.1; -. [Q9H633-1]
DR CCDS; CCDS56409.1; -. [Q9H633-4]
DR CCDS; CCDS56410.1; -. [Q9H633-3]
DR RefSeq; NP_001186049.1; NM_001199120.1. [Q9H633-4]
DR RefSeq; NP_001186050.1; NM_001199121.1. [Q9H633-3]
DR RefSeq; NP_079115.1; NM_024839.2. [Q9H633-1]
DR PDB; 6AHR; EM; 3.92 A; K=1-154.
DR PDB; 6AHU; EM; 3.66 A; K=1-154.
DR PDBsum; 6AHR; -.
DR PDBsum; 6AHU; -.
DR AlphaFoldDB; Q9H633; -.
DR SMR; Q9H633; -.
DR BioGRID; 122981; 23.
DR CORUM; Q9H633; -.
DR IntAct; Q9H633; 11.
DR STRING; 9606.ENSP00000409799; -.
DR iPTMnet; Q9H633; -.
DR PhosphoSitePlus; Q9H633; -.
DR BioMuta; RPP21; -.
DR DMDM; 52001252; -.
DR EPD; Q9H633; -.
DR jPOST; Q9H633; -.
DR MassIVE; Q9H633; -.
DR MaxQB; Q9H633; -.
DR PaxDb; Q9H633; -.
DR PeptideAtlas; Q9H633; -.
DR PRIDE; Q9H633; -.
DR ProteomicsDB; 63919; -.
DR ProteomicsDB; 80953; -. [Q9H633-1]
DR ProteomicsDB; 80954; -. [Q9H633-2]
DR ProteomicsDB; 80955; -. [Q9H633-3]
DR Antibodypedia; 34965; 57 antibodies from 14 providers.
DR DNASU; 79897; -.
DR Ensembl; ENST00000376642.8; ENSP00000365829.4; ENSG00000239927.6. [Q9H633-1]
DR Ensembl; ENST00000411784.6; ENSP00000412619.2; ENSG00000241863.6. [Q9H633-2]
DR Ensembl; ENST00000414187.6; ENSP00000398396.2; ENSG00000243009.6.
DR Ensembl; ENST00000415583.6; ENSP00000403747.2; ENSG00000239927.6. [Q9H633-3]
DR Ensembl; ENST00000416977.6; ENSP00000404312.2; ENSG00000241779.6.
DR Ensembl; ENST00000424616.6; ENSP00000399295.2; ENSG00000241863.6. [Q9H633-1]
DR Ensembl; ENST00000425575.2; ENSP00000405834.2; ENSG00000239927.6. [Q9H633-4]
DR Ensembl; ENST00000428040.6; ENSP00000394320.2; ENSG00000241370.6. [Q9H633-2]
DR Ensembl; ENST00000430900.6; ENSP00000415046.2; ENSG00000239927.6. [Q9H633-2]
DR Ensembl; ENST00000433076.6; ENSP00000409799.2; ENSG00000241370.6. [Q9H633-4]
DR Ensembl; ENST00000434282.6; ENSP00000414284.2; ENSG00000242726.6.
DR Ensembl; ENST00000435318.2; ENSP00000411003.2; ENSG00000239865.6. [Q9H633-3]
DR Ensembl; ENST00000436442.2; ENSP00000397778.2; ENSG00000241370.6. [Q9H633-3]
DR Ensembl; ENST00000437470.2; ENSP00000408610.2; ENSG00000241863.6. [Q9H633-3]
DR Ensembl; ENST00000442966.7; ENSP00000403833.2; ENSG00000241370.6. [Q9H633-1]
DR Ensembl; ENST00000455025.6; ENSP00000409193.2; ENSG00000241863.6. [Q9H633-4]
DR GeneID; 79897; -.
DR KEGG; hsa:79897; -.
DR MANE-Select; ENST00000442966.7; ENSP00000403833.2; NM_024839.4; NP_079115.1.
DR UCSC; uc003nqd.3; human. [Q9H633-1]
DR CTD; 79897; -.
DR DisGeNET; 79897; -.
DR GeneCards; RPP21; -.
DR HGNC; HGNC:21300; RPP21.
DR HPA; ENSG00000241370; Low tissue specificity.
DR MIM; 612524; gene.
DR neXtProt; NX_Q9H633; -.
DR OpenTargets; ENSG00000241370; -.
DR PharmGKB; PA134960979; -.
DR VEuPathDB; HostDB:ENSG00000241370; -.
DR eggNOG; KOG4394; Eukaryota.
DR GeneTree; ENSGT00390000003020; -.
DR HOGENOM; CLU_079140_2_1_1; -.
DR InParanoid; Q9H633; -.
DR OMA; DPKHLLW; -.
DR PhylomeDB; Q9H633; -.
DR BRENDA; 3.1.26.5; 2681.
DR PathwayCommons; Q9H633; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9H633; -.
DR BioGRID-ORCS; 79897; 706 hits in 1056 CRISPR screens.
DR GenomeRNAi; 79897; -.
DR Pharos; Q9H633; Tbio.
DR PRO; PR:Q9H633; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9H633; protein.
DR Bgee; ENSG00000241370; Expressed in muscle layer of sigmoid colon and 97 other tissues.
DR ExpressionAtlas; Q9H633; baseline and differential.
DR Genevisible; Q9H633; HS.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; IDA:UniProtKB.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR GO; GO:0033204; F:ribonuclease P RNA binding; IDA:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:UniProtKB.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR InterPro; IPR007175; Rpr2/Snm1/Rpp21.
DR Pfam; PF04032; Rpr2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Metal-binding; Nucleus;
KW Reference proteome; RNA-binding; tRNA processing; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..154
FT /note="Ribonuclease P protein subunit p21"
FT /id="PRO_0000153845"
FT REGION 117..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 19
FT /note="Q -> QVSLRQGPHGDGARRPRVTAPLPQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010695"
FT VAR_SEQ 52
FT /note="R -> RRPLSSSAP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044901"
FT VAR_SEQ 123..154
FT /note="DSKPLQPLPNTAHSISDRLPEEKMQTQGSSNQ -> GERFQTTTTLAKHSPL
FT HFRPPS (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010696"
FT VARIANT 77
FT /note="Q -> H (in dbSNP:rs6986)"
FT /evidence="ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_019116"
FT VARIANT 149
FT /note="Q -> K (in dbSNP:rs974963)"
FT /evidence="ECO:0000269|PubMed:14574404"
FT /id="VAR_045986"
FT CONFLICT 9
FT /note="E -> K (in Ref. 6; BI598757)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="R -> Q (in Ref. 2; CAD44290)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 17570 MW; F8BD15AA20AE695F CRC64;
MAGPVKDREA FQRLNFLYQA AHCVLAQDPE NQALARFYCY TERTIAKRLV LRRDPSVKRT
LCRGCSSLLV PGLTCTQRQR RCRGQRWTVQ TCLTCQRSQR FLNDPGHLLW GDRPEAQLGS
QADSKPLQPL PNTAHSISDR LPEEKMQTQG SSNQ
