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   24-JAN-2024, entry version 162.
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   EMDB; EMD-9626; -.
DR   EMDB; EMD-9627; -.
DR   SMR; Q9H633; -.
DR   BioGRID; 122981; 27.
DR   ComplexPortal; CPX-2877; Nucleolar ribonuclease P complex.
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; 9606-ENSP00000409799; -.
DR   PeptideAtlas; Q9H633; -.
DR   ProteomicsDB; 63919; -.
DR   ProteomicsDB; 80953; -. [Q9H633-1]
DR   ProteomicsDB; 80954; -. [Q9H633-2]
DR   ProteomicsDB; 80955; -. [Q9H633-3]
DR   Pumba; Q9H633; -.
DR   Antibodypedia; 34965; 64 antibodies from 15 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   AGR; HGNC:21300; -.
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   OrthoDB; 5482220at2759; -.
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; 741 hits in 1134 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 99 other cell types or tissues.
DR   ExpressionAtlas; Q9H633; baseline and differential.
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   Gene3D; 6.20.50.20; -; 1.
DR   InterPro; IPR007175; Rpr2/Snm1/Rpp21.
DR   PANTHER; PTHR14742:SF0; RIBONUCLEASE P PROTEIN SUBUNIT P21; 1.
DR   PANTHER; PTHR14742; RIBONUCLEASE P SUBUNIT P21; 1.
DR   Pfam; PF04032; Rpr2; 1.
DR   Genevisible; Q9H633; HS.
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
//