NAA50_MOUSE
ID NAA50_MOUSE Reviewed; 169 AA.
AC Q6PGB6; Q3TH79; Q3TK59; Q7TML2; Q80VE3; Q9D0Q8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=N-alpha-acetyltransferase 50;
DE EC=2.3.1.258 {ECO:0000250|UniProtKB:Q9GZZ1};
DE AltName: Full=N-acetyltransferase NAT13;
DE AltName: Full=N-epsilon-acetyltransferase 50 {ECO:0000250|UniProtKB:Q9GZZ1};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q9GZZ1};
DE AltName: Full=NatE catalytic subunit;
GN Name=Naa50 {ECO:0000312|MGI:MGI:1919367}; Synonyms=Mak3, Nat13;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Egg, Embryo, Kidney, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 5).
RC STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
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 [3]
RP INTERACTION WITH NAA35, AND SUBCELLULAR LOCATION.
RX PubMed=16484612; DOI=10.1161/01.res.0000214539.86593.7a;
RA Wenzlau J.M., Garl P.J., Simpson P., Stenmark K.R., West J., Artinger K.B.,
RA Nemenoff R.A., Weiser-Evans M.C.M.;
RT "Embryonic growth-associated protein is one subunit of a novel N-terminal
RT acetyltransferase complex essential for embryonic vascular development.";
RL Circ. Res. 98:846-855(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34 AND LYS-37, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: N-alpha-acetyltransferase that acetylates the N-terminus of
CC proteins that retain their initiating methionine (By similarity). Has a
CC broad substrate specificity: able to acetylate the initiator methionine
CC of most peptides, except for those with a proline in second position
CC (By similarity). Also displays N-epsilon-acetyltransferase activity by
CC mediating acetylation of the side chain of specific lysines on proteins
CC (By similarity). Autoacetylates in vivo (By similarity). The relevance
CC of N-epsilon-acetyltransferase activity is however unclear: able to
CC acetylate H4 in vitro, but this result has not been confirmed in vivo
CC (By similarity). Component of N-alpha-acetyltransferase complexes
CC containing NAA10 and NAA15, which has N-alpha-acetyltransferase
CC activity (By similarity). Does not influence the acetyltransferase
CC activity of NAA10 (By similarity). However, it negatively regulates the
CC N-alpha-acetyltransferase activity of the N-terminal acetyltransferase
CC A complex (also called the NatA complex) (By similarity). The
CC multiprotein complexes probably constitute the major contributor for N-
CC terminal acetylation at the ribosome exit tunnel, with NAA10
CC acetylating all amino termini that are devoid of methionine and NAA50
CC acetylating other peptides (By similarity). Required for sister
CC chromatid cohesion during mitosis by promoting binding of CDCA5/sororin
CC to cohesin: may act by counteracting the function of NAA10 (By
CC similarity). {ECO:0000250|UniProtKB:Q9GZZ1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein];
CC Xref=Rhea:RHEA:50564, Rhea:RHEA-COMP:12726, Rhea:RHEA-COMP:12727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133398, ChEBI:CHEBI:133399; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-seryl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein];
CC Xref=Rhea:RHEA:50568, Rhea:RHEA-COMP:12728, Rhea:RHEA-COMP:12729,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133400, ChEBI:CHEBI:133401; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-valyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein];
CC Xref=Rhea:RHEA:50572, Rhea:RHEA-COMP:12730, Rhea:RHEA-COMP:12731,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133402, ChEBI:CHEBI:133403; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-threonyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein];
CC Xref=Rhea:RHEA:50576, Rhea:RHEA-COMP:12732, Rhea:RHEA-COMP:12733,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133404, ChEBI:CHEBI:133405; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-lysyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein];
CC Xref=Rhea:RHEA:50580, Rhea:RHEA-COMP:12734, Rhea:RHEA-COMP:12735,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133406, ChEBI:CHEBI:133407; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein];
CC Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-
CC [protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-
CC COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase E (NatE) complex
CC at least composed of NAA10, NAA15 and NAA50 (By similarity). Interacts
CC with NAA10 (By similarity). Interacts with NAA15 (By similarity).
CC Predominantly interacts with NAA15 in the N-terminal acetyltransferase
CC A complex (NatA complex); the interactions reduce the acetylation
CC activity of the NatA complex (By similarity). Component of the N-
CC terminal acetyltransferase E (NatE)/HYPK complex at least composed of
CC NAA10, NAA15, NAA50 and HYPK (By similarity). Within the complex
CC interacts with NAA15 (By similarity). Its capacity to interact with the
CC NatA complex is reduced by HYPK (By similarity). Interacts with NAA35
CC (PubMed:16484612). {ECO:0000250|UniProtKB:Q9GZZ1,
CC ECO:0000269|PubMed:16484612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16484612}. Nucleus
CC {ECO:0000250|UniProtKB:Q9GZZ1}. Note=Localizes to the cytoplasm in
CC interphase cells. {ECO:0000250|UniProtKB:Q9GZZ1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6PGB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PGB6-2; Sequence=VSP_024749;
CC Name=3;
CC IsoId=Q6PGB6-3; Sequence=VSP_024750;
CC Name=4;
CC IsoId=Q6PGB6-4; Sequence=VSP_024748;
CC Name=5;
CC IsoId=Q6PGB6-5; Sequence=VSP_024749, VSP_024751;
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE40319.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK011160; BAB27439.1; -; mRNA.
DR EMBL; AK135658; BAE22602.1; -; mRNA.
DR EMBL; AK145345; BAE26378.1; -; mRNA.
DR EMBL; AK156791; BAE33858.1; -; mRNA.
DR EMBL; AK167141; BAE39286.1; -; mRNA.
DR EMBL; AK168394; BAE40319.1; ALT_SEQ; mRNA.
DR EMBL; BC046283; AAH46283.1; -; mRNA.
DR EMBL; BC055846; AAH55846.1; -; mRNA.
DR EMBL; BC057117; AAH57117.1; -; mRNA.
DR CCDS; CCDS28183.1; -. [Q6PGB6-2]
DR CCDS; CCDS84236.1; -. [Q6PGB6-1]
DR RefSeq; NP_001334168.1; NM_001347239.1. [Q6PGB6-1]
DR RefSeq; NP_082384.1; NM_028108.3. [Q6PGB6-2]
DR AlphaFoldDB; Q6PGB6; -.
DR BMRB; Q6PGB6; -.
DR SMR; Q6PGB6; -.
DR BioGRID; 215162; 32.
DR IntAct; Q6PGB6; 32.
DR MINT; Q6PGB6; -.
DR STRING; 10090.ENSMUSP00000070140; -.
DR iPTMnet; Q6PGB6; -.
DR PhosphoSitePlus; Q6PGB6; -.
DR EPD; Q6PGB6; -.
DR MaxQB; Q6PGB6; -.
DR PaxDb; Q6PGB6; -.
DR PeptideAtlas; Q6PGB6; -.
DR PRIDE; Q6PGB6; -.
DR ProteomicsDB; 252638; -. [Q6PGB6-1]
DR ProteomicsDB; 252639; -. [Q6PGB6-2]
DR ProteomicsDB; 252640; -. [Q6PGB6-3]
DR ProteomicsDB; 252641; -. [Q6PGB6-4]
DR ProteomicsDB; 252642; -. [Q6PGB6-5]
DR Antibodypedia; 32596; 167 antibodies from 27 providers.
DR DNASU; 72117; -.
DR Ensembl; ENSMUST00000063520; ENSMUSP00000070140; ENSMUSG00000022698. [Q6PGB6-2]
DR Ensembl; ENSMUST00000063542; ENSMUSP00000067361; ENSMUSG00000022698. [Q6PGB6-3]
DR Ensembl; ENSMUST00000159514; ENSMUSP00000125517; ENSMUSG00000022698. [Q6PGB6-4]
DR Ensembl; ENSMUST00000161326; ENSMUSP00000124291; ENSMUSG00000022698. [Q6PGB6-1]
DR GeneID; 72117; -.
DR KEGG; mmu:72117; -.
DR UCSC; uc007zgy.1; mouse. [Q6PGB6-2]
DR UCSC; uc007zgz.1; mouse. [Q6PGB6-4]
DR UCSC; uc007zha.1; mouse. [Q6PGB6-1]
DR UCSC; uc012afx.1; mouse. [Q6PGB6-3]
DR CTD; 80218; -.
DR MGI; MGI:1919367; Naa50.
DR VEuPathDB; HostDB:ENSMUSG00000022698; -.
DR eggNOG; KOG3138; Eukaryota.
DR GeneTree; ENSGT00390000009110; -.
DR HOGENOM; CLU_013985_5_3_1; -.
DR InParanoid; Q6PGB6; -.
DR OMA; IVETKEH; -.
DR OrthoDB; 1536763at2759; -.
DR PhylomeDB; Q6PGB6; -.
DR TreeFam; TF314841; -.
DR BioGRID-ORCS; 72117; 23 hits in 71 CRISPR screens.
DR ChiTaRS; Naa50; mouse.
DR PRO; PR:Q6PGB6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q6PGB6; protein.
DR Bgee; ENSMUSG00000022698; Expressed in ear vesicle and 230 other tissues.
DR Genevisible; Q6PGB6; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031415; C:NatA complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0052858; F:peptidyl-lysine acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0071962; P:mitotic sister chromatid cohesion, centromeric; ISS:UniProtKB.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISS:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Alternative splicing; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..169
FT /note="N-alpha-acetyltransferase 50"
FT /id="PRO_0000284903"
FT DOMAIN 6..155
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 138..141
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT ACT_SITE 73
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT ACT_SITE 112
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT BINDING 77..90
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT BINDING 117..126
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 37
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 110
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT MOD_RES 140
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT VAR_SEQ 1..3
FT /note="MKG -> MPGTVGHEH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024748"
FT VAR_SEQ 4
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_024749"
FT VAR_SEQ 49..88
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024750"
FT VAR_SEQ 101..169
FT /note="EKDGTFDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYKRIEPADAHVLQK
FT NLKVPSGQNAETQKTDN -> GWMDGWMDGWMDGRASEIVEIPCLFLGYQFPKQSKSKL
FT RSLVLSTFTLMDKLQRALAKRRGHK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024751"
SQ SEQUENCE 169 AA; 19414 MW; 153A8021B745347C CRC64;
MKGSRIELGD VTPHNIKQLK RLNQVIFPVS YNDKFYKDVL EVGELAKLAY FNDIAVGAVC
CRVDHSQNQK RLYIMTLGCL APYRRLGIGT KMLNHVLNIC EKDGTFDNIY LHVQISNESA
IDFYRKFGFE IIETKKNYYK RIEPADAHVL QKNLKVPSGQ NAETQKTDN
