RM55_HUMAN
ID RM55_HUMAN Reviewed; 128 AA.
AC Q7Z7F7; Q5TBY3; Q5TBY6; Q6UWI8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=39S ribosomal protein L55, mitochondrial;
DE Short=L55mt;
DE Short=MRP-L55;
DE AltName: Full=Mitochondrial large ribosomal subunit protein bL31m {ECO:0000303|PubMed:27023846};
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL55 {ECO:0000303|PubMed:25838379};
DE Flags: Precursor;
GN Name=MRPL55; ORFNames=UNQ5835/PRO19675;
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 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP IDENTIFICATION.
RX PubMed=11551941; DOI=10.1074/jbc.m106510200;
RA Koc E.C., Burkhart W., Blackburn K., Moyer M.B., Schlatzer D.M.,
RA Moseley A., Spremulli L.L.;
RT "The large subunit of the mammalian mitochondrial ribosome. Analysis of the
RT complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:43958-43969(2001).
RN [5]
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 [6]
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 [7]
RP NOMENCLATURE.
RX PubMed=27023846; DOI=10.1146/annurev-biochem-060815-014343;
RA Greber B.J., Ban N.;
RT "Structure and function of the mitochondrial ribosome.";
RL Annu. Rev. Biochem. 85:103-132(2016).
RN [8] {ECO:0007744|PDB:3J9M}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBCELLULAR
RP LOCATION.
RX PubMed=25838379; DOI=10.1126/science.aaa1193;
RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.;
RT "Ribosome. The structure of the human mitochondrial ribosome.";
RL Science 348:95-98(2015).
RN [9] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=28892042; DOI=10.1038/nsmb.3464;
RA Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J.,
RA Amunts A., Ramakrishnan V.;
RT "Structures of the human mitochondrial ribosome in native states of
RT assembly.";
RL Nat. Struct. Mol. Biol. 24:866-869(2017).
CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC LSU) (PubMed:28892042, PubMed:25838379). Mature mammalian 55S
CC mitochondrial ribosomes consist of a small (28S) and a large (39S)
CC subunit. The 28S small subunit contains a 12S ribosomal RNA (12S mt-
CC rRNA) and 30 different proteins. The 39S large subunit contains a 16S
CC rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA (mt-
CC tRNA(Val)), which plays an integral structural role, and 52 different
CC proteins. {ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042,
CC ECO:0000305|PubMed:25838379}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379,
CC ECO:0000269|PubMed:28892042}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z7F7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z7F7-2; Sequence=VSP_022477;
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL55 family. {ECO:0000305}.
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DR EMBL; AY358771; AAQ89131.1; -; mRNA.
DR EMBL; AL136379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052806; AAH52806.1; -; mRNA.
DR CCDS; CCDS1567.1; -. [Q7Z7F7-1]
DR CCDS; CCDS44325.1; -. [Q7Z7F7-2]
DR RefSeq; NP_001308213.1; NM_001321284.1. [Q7Z7F7-1]
DR RefSeq; NP_852106.1; NM_181441.2. [Q7Z7F7-1]
DR RefSeq; NP_852119.1; NM_181454.2. [Q7Z7F7-1]
DR RefSeq; NP_852120.1; NM_181455.2. [Q7Z7F7-1]
DR RefSeq; NP_852121.1; NM_181456.2. [Q7Z7F7-1]
DR RefSeq; NP_852127.2; NM_181462.2. [Q7Z7F7-2]
DR RefSeq; NP_852128.1; NM_181463.2. [Q7Z7F7-1]
DR RefSeq; NP_852129.1; NM_181464.2. [Q7Z7F7-1]
DR RefSeq; NP_852130.1; NM_181465.2. [Q7Z7F7-1]
DR RefSeq; XP_005273116.1; XM_005273059.3. [Q7Z7F7-1]
DR RefSeq; XP_005273118.1; XM_005273061.4. [Q7Z7F7-1]
DR RefSeq; XP_005273119.1; XM_005273062.3. [Q7Z7F7-1]
DR RefSeq; XP_005273120.1; XM_005273063.4. [Q7Z7F7-1]
DR RefSeq; XP_011542396.1; XM_011544094.2.
DR RefSeq; XP_011542397.1; XM_011544095.2. [Q7Z7F7-1]
DR PDB; 3J9M; EM; 3.50 A; m=1-128.
DR PDB; 5OOL; EM; 3.06 A; m=1-128.
DR PDB; 5OOM; EM; 3.03 A; m=1-128.
DR PDB; 6I9R; EM; 3.90 A; m=1-128.
DR PDB; 6NU2; EM; 3.90 A; m=34-78.
DR PDB; 6NU3; EM; 4.40 A; m=1-128.
DR PDB; 6VLZ; EM; 2.97 A; m=1-128.
DR PDB; 6VMI; EM; 2.96 A; m=1-128.
DR PDB; 6ZM5; EM; 2.89 A; m=1-128.
DR PDB; 6ZM6; EM; 2.59 A; m=1-128.
DR PDB; 6ZS9; EM; 4.00 A; m=1-128.
DR PDB; 6ZSA; EM; 4.00 A; m=1-128.
DR PDB; 6ZSB; EM; 4.50 A; m=1-128.
DR PDB; 6ZSC; EM; 3.50 A; m=1-128.
DR PDB; 6ZSD; EM; 3.70 A; m=1-128.
DR PDB; 6ZSE; EM; 5.00 A; m=1-128.
DR PDB; 6ZSG; EM; 4.00 A; m=1-128.
DR PDB; 7A5F; EM; 4.40 A; m3=1-128.
DR PDB; 7A5G; EM; 4.33 A; m3=1-128.
DR PDB; 7A5H; EM; 3.30 A; m=1-128.
DR PDB; 7A5I; EM; 3.70 A; m3=1-128.
DR PDB; 7A5J; EM; 3.10 A; m=1-128.
DR PDB; 7A5K; EM; 3.70 A; m3=1-128.
DR PDB; 7L08; EM; 3.49 A; m=1-128.
DR PDB; 7L20; EM; 3.15 A; m=1-128.
DR PDB; 7O9K; EM; 3.10 A; m=1-128.
DR PDB; 7O9M; EM; 2.50 A; m=1-128.
DR PDB; 7ODR; EM; 2.90 A; m=1-128.
DR PDB; 7ODS; EM; 3.10 A; m=1-128.
DR PDB; 7ODT; EM; 3.10 A; m=1-128.
DR PDB; 7OF0; EM; 2.20 A; m=1-128.
DR PDB; 7OF2; EM; 2.70 A; m=1-128.
DR PDB; 7OF3; EM; 2.70 A; m=1-128.
DR PDB; 7OF4; EM; 2.70 A; m=1-128.
DR PDB; 7OF5; EM; 2.90 A; m=1-128.
DR PDB; 7OF6; EM; 2.60 A; m=1-128.
DR PDB; 7OF7; EM; 2.50 A; m=1-128.
DR PDB; 7OG4; EM; 3.80 A; m=1-128.
DR PDB; 7OI7; EM; 3.50 A; m=1-128.
DR PDB; 7OI8; EM; 3.50 A; m=1-128.
DR PDB; 7OI9; EM; 3.30 A; m=1-128.
DR PDB; 7OIA; EM; 3.20 A; m=1-128.
DR PDB; 7OIB; EM; 3.30 A; m=1-128.
DR PDB; 7OIC; EM; 3.10 A; m=1-128.
DR PDB; 7OID; EM; 3.70 A; m=1-128.
DR PDB; 7OIE; EM; 3.50 A; m=1-128.
DR PDB; 7PD3; EM; 3.40 A; m=1-128.
DR PDBsum; 3J9M; -.
DR PDBsum; 5OOL; -.
DR PDBsum; 5OOM; -.
DR PDBsum; 6I9R; -.
DR PDBsum; 6NU2; -.
DR PDBsum; 6NU3; -.
DR PDBsum; 6VLZ; -.
DR PDBsum; 6VMI; -.
DR PDBsum; 6ZM5; -.
DR PDBsum; 6ZM6; -.
DR PDBsum; 6ZS9; -.
DR PDBsum; 6ZSA; -.
DR PDBsum; 6ZSB; -.
DR PDBsum; 6ZSC; -.
DR PDBsum; 6ZSD; -.
DR PDBsum; 6ZSE; -.
DR PDBsum; 6ZSG; -.
DR PDBsum; 7A5F; -.
DR PDBsum; 7A5G; -.
DR PDBsum; 7A5H; -.
DR PDBsum; 7A5I; -.
DR PDBsum; 7A5J; -.
DR PDBsum; 7A5K; -.
DR PDBsum; 7L08; -.
DR PDBsum; 7L20; -.
DR PDBsum; 7O9K; -.
DR PDBsum; 7O9M; -.
DR PDBsum; 7ODR; -.
DR PDBsum; 7ODS; -.
DR PDBsum; 7ODT; -.
DR PDBsum; 7OF0; -.
DR PDBsum; 7OF2; -.
DR PDBsum; 7OF3; -.
DR PDBsum; 7OF4; -.
DR PDBsum; 7OF5; -.
DR PDBsum; 7OF6; -.
DR PDBsum; 7OF7; -.
DR PDBsum; 7OG4; -.
DR PDBsum; 7OI7; -.
DR PDBsum; 7OI8; -.
DR PDBsum; 7OI9; -.
DR PDBsum; 7OIA; -.
DR PDBsum; 7OIB; -.
DR PDBsum; 7OIC; -.
DR PDBsum; 7OID; -.
DR PDBsum; 7OIE; -.
DR PDBsum; 7PD3; -.
DR AlphaFoldDB; Q7Z7F7; -.
DR SMR; Q7Z7F7; -.
DR BioGRID; 126105; 135.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q7Z7F7; -.
DR IntAct; Q7Z7F7; 37.
DR MINT; Q7Z7F7; -.
DR STRING; 9606.ENSP00000403614; -.
DR GlyGen; Q7Z7F7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z7F7; -.
DR PhosphoSitePlus; Q7Z7F7; -.
DR BioMuta; MRPL55; -.
DR DMDM; 74750237; -.
DR EPD; Q7Z7F7; -.
DR jPOST; Q7Z7F7; -.
DR MassIVE; Q7Z7F7; -.
DR MaxQB; Q7Z7F7; -.
DR PaxDb; Q7Z7F7; -.
DR PeptideAtlas; Q7Z7F7; -.
DR PRIDE; Q7Z7F7; -.
DR ProteomicsDB; 69531; -. [Q7Z7F7-1]
DR ProteomicsDB; 69532; -. [Q7Z7F7-2]
DR TopDownProteomics; Q7Z7F7-1; -. [Q7Z7F7-1]
DR Antibodypedia; 34660; 82 antibodies from 19 providers.
DR DNASU; 128308; -.
DR Ensembl; ENST00000295008.8; ENSP00000295008.4; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000336300.9; ENSP00000337361.5; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000336520.8; ENSP00000337342.3; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000348259.9; ENSP00000338189.5; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000366733.5; ENSP00000355694.1; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000366734.5; ENSP00000355695.1; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000366735.5; ENSP00000355696.1; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000366736.5; ENSP00000355697.1; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000366738.5; ENSP00000355699.1; ENSG00000162910.19. [Q7Z7F7-2]
DR Ensembl; ENST00000366739.5; ENSP00000355700.1; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000366740.5; ENSP00000355701.1; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000366741.5; ENSP00000355702.1; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000366742.5; ENSP00000355703.1; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000366744.5; ENSP00000355705.1; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000366746.7; ENSP00000355707.3; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000366747.7; ENSP00000355708.3; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000391867.8; ENSP00000375740.3; ENSG00000162910.19. [Q7Z7F7-1]
DR Ensembl; ENST00000430433.5; ENSP00000403614.1; ENSG00000162910.19. [Q7Z7F7-2]
DR GeneID; 128308; -.
DR KEGG; hsa:128308; -.
DR MANE-Select; ENST00000336520.8; ENSP00000337342.3; NM_181463.3; NP_852128.1.
DR UCSC; uc001hrz.5; human. [Q7Z7F7-1]
DR CTD; 128308; -.
DR GeneCards; MRPL55; -.
DR HGNC; HGNC:16686; MRPL55.
DR HPA; ENSG00000162910; Low tissue specificity.
DR MIM; 611859; gene.
DR neXtProt; NX_Q7Z7F7; -.
DR OpenTargets; ENSG00000162910; -.
DR PharmGKB; PA30988; -.
DR VEuPathDB; HostDB:ENSG00000162910; -.
DR eggNOG; KOG4616; Eukaryota.
DR GeneTree; ENSGT00390000010309; -.
DR HOGENOM; CLU_139855_0_0_1; -.
DR InParanoid; Q7Z7F7; -.
DR OMA; NNAWRAS; -.
DR OrthoDB; 1553019at2759; -.
DR PhylomeDB; Q7Z7F7; -.
DR TreeFam; TF320422; -.
DR PathwayCommons; Q7Z7F7; -.
DR Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR SignaLink; Q7Z7F7; -.
DR SIGNOR; Q7Z7F7; -.
DR BioGRID-ORCS; 128308; 416 hits in 1087 CRISPR screens.
DR ChiTaRS; MRPL55; human.
DR GeneWiki; MRPL55; -.
DR GenomeRNAi; 128308; -.
DR Pharos; Q7Z7F7; Tdark.
DR PRO; PR:Q7Z7F7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7Z7F7; protein.
DR Bgee; ENSG00000162910; Expressed in apex of heart and 159 other tissues.
DR ExpressionAtlas; Q7Z7F7; baseline and differential.
DR Genevisible; Q7Z7F7; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; ISS:UniProtKB.
DR Gene3D; 6.20.130.20; -; 1.
DR InterPro; IPR018615; Ribosomal_L55_mit.
DR InterPro; IPR044884; Ribosomal_L55_sf.
DR PANTHER; PTHR34095; PTHR34095; 1.
DR Pfam; PF09776; Mitoc_L55; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Mitochondrion; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..128
FT /note="39S ribosomal protein L55, mitochondrial"
FT /id="PRO_0000273099"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZ83"
FT VAR_SEQ 9
FT /note="G -> GLAASSWLGGQNASDHSLWLLRKPRGSSCPGTGHQLC (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_022477"
FT VARIANT 24
FT /note="R -> C (in dbSNP:rs822730)"
FT /id="VAR_030082"
FT VARIANT 42
FT /note="R -> H (in dbSNP:rs35265990)"
FT /id="VAR_052045"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:5OOM"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5OOL"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5OOL"
SQ SEQUENCE 128 AA; 15128 MW; A7808C869855C994 CRC64;
MAAVGSLLGR LRQSTVKATG PALRRLHTSS WRADSSRASL TRVHRQAYAR LYPVLLVKQD
GSTIHIRYRE PRRMLAMPID LDTLSPEERR ARLRKREAQL QSRKEYEQEL SDDLHVERYR
QFWTRTKK
