PSA5_HUMAN
ID PSA5_HUMAN Reviewed; 241 AA.
AC P28066; B2R8F6; B4E2V4; Q3T1C1; Q6IBF7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 3.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Proteasome subunit alpha type-5;
DE AltName: Full=Macropain zeta chain;
DE AltName: Full=Multicatalytic endopeptidase complex zeta chain;
DE AltName: Full=Proteasome zeta chain;
GN Name=PSMA5;
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).
RX PubMed=1888762; DOI=10.1016/0167-4838(91)90020-z;
RA DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z., Moomaw C.R.,
RA Dawson P.A., Slaughter C.A.;
RT "The primary structures of four subunits of the human, high-molecular-
RT weight proteinase, macropain (proteasome), are distinct but homologous.";
RL Biochim. Biophys. Acta 1079:29-38(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Trachea;
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=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 [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] (ISOFORM 1).
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 PROTEIN SEQUENCE OF 54-58; 67-73; 94-99 AND 120-128.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [8]
RP PROTEIN SEQUENCE OF 169-187.
RA Bienvenut W.V., Vuadens F., Crettaz D., Tissot J.-D., Quadroni M.;
RL Submitted (OCT-2003) to UniProtKB.
RN [9]
RP FUNCTION IN ANTIGEN PRESENTATION.
RX PubMed=8610016; DOI=10.1038/381166a0;
RA Groettrup M., Soza A., Eggers M., Kuehn L., Dick T.P., Schild H.,
RA Rammensee H.G., Koszinowski U.H., Kloetzel P.M.;
RT "A role for the proteasome regulator PA28alpha in antigen presentation.";
RL Nature 381:166-168(1996).
RN [10]
RP INDUCTION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11771738; DOI=10.1007/978-3-7091-6262-0_10;
RA Engidawork E., Juranville J.F., Fountoulakis M., Dierssen M., Lubec G.;
RT "Selective upregulation of the ubiquitin-proteasome proteolytic pathway
RT proteins, proteasome zeta chain and isopeptidase T in fetal Down
RT syndrome.";
RL J. Neural Transm. 61:117-130(2001).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=12181345; DOI=10.1091/mbc.e02-03-0122;
RA Lafarga M., Berciano M.T., Pena E., Mayo I., Castano J.G., Bohmann D.,
RA Rodrigues J.P., Tavanez J.P., Carmo-Fonseca M.;
RT "Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes,
RT ubiquitin, and protein substrates of proteasome.";
RL Mol. Biol. Cell 13:2771-2782(2002).
RN [12]
RP FUNCTION.
RX PubMed=15244466; DOI=10.1021/bm049957a;
RA Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.;
RT "20S proteasome prevents aggregation of heat-denatured proteins without
RT PA700 regulatory subcomplex like a molecular chaperone.";
RL Biomacromolecules 5:1465-1469(2004).
RN [13]
RP INTERACTION WITH PSMG1 AND PSMG2.
RX PubMed=16251969; DOI=10.1038/nature04106;
RA Hirano Y., Hendil K.B., Yashiroda H., Iemura S., Nagane R., Hioki Y.,
RA Natsume T., Tanaka K., Murata S.;
RT "A heterodimeric complex that promotes the assembly of mammalian 20S
RT proteasomes.";
RL Nature 437:1381-1385(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human 26S
RT proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-55, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP INDUCTION.
RX PubMed=19734940; DOI=10.1038/onc.2009.264;
RA Arlt A., Bauer I., Schafmayer C., Tepel J., Mueerkoester S.S., Brosch M.,
RA Roeder C., Kalthoff H., Hampe J., Moyer M.P., Foelsch U.R., Schaefer H.;
RT "Increased proteasome subunit protein expression and proteasome activity in
RT colon cancer relate to an enhanced activation of nuclear factor E2-related
RT factor 2 (Nrf2).";
RL Oncogene 28:3983-3996(2009).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-56, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
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 [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-56 AND SER-63, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27176742; DOI=10.1515/hsz-2016-0176;
RA Rut W., Drag M.;
RT "Human 20S proteasome activity towards fluorogenic peptides of various
RT chain lengths.";
RL Biol. Chem. 397:921-926(2016).
RN [28]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
RX PubMed=26133119; DOI=10.1038/ncomms8573;
RA da Fonseca P.C., Morris E.P.;
RT "Cryo-EM reveals the conformation of a substrate analogue in the human 20S
RT proteasome core.";
RL Nat. Commun. 6:7573-7573(2015).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), AND SUBUNIT.
RX PubMed=25599644; DOI=10.1016/j.str.2014.11.017;
RA Harshbarger W., Miller C., Diedrich C., Sacchettini J.;
RT "Crystal structure of the human 20S proteasome in complex with
RT carfilzomib.";
RL Structure 23:418-424(2015).
RN [30]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
RX PubMed=27428775; DOI=10.1038/nsmb.3273;
RA Huang X., Luan B., Wu J., Shi Y.;
RT "An atomic structure of the human 26S proteasome.";
RL Nat. Struct. Mol. Biol. 23:778-785(2016).
RN [31]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS), AND SUBUNIT.
RX PubMed=27342858; DOI=10.1073/pnas.1608050113;
RA Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
RA Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
RT "Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
RX PubMed=27493187; DOI=10.1126/science.aaf8993;
RA Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R.,
RA Stark H., Bourenkov G., Chari A.;
RT "The inhibition mechanism of human 20S proteasomes enables next-generation
RT inhibitor design.";
RL Science 353:594-598(2016).
RN [33]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH AKIRIN2,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=34711951; DOI=10.1038/s41586-021-04035-8;
RA de Almeida M., Hinterndorfer M., Brunner H., Grishkovskaya I., Singh K.,
RA Schleiffer A., Jude J., Deswal S., Kalis R., Vunjak M., Lendl T., Imre R.,
RA Roitinger E., Neumann T., Kandolf S., Schutzbier M., Mechtler K.,
RA Versteeg G.A., Haselbach D., Zuber J.;
RT "AKIRIN2 controls the nuclear import of proteasomes in vertebrates.";
RL Nature 599:491-496(2021).
CC -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC proteolytic degradation of most intracellular proteins. This complex
CC plays numerous essential roles within the cell by associating with
CC different regulatory particles. Associated with two 19S regulatory
CC particles, forms the 26S proteasome and thus participates in the ATP-
CC dependent degradation of ubiquitinated proteins. The 26S proteasome
CC plays a key role in the maintenance of protein homeostasis by removing
CC misfolded or damaged proteins that could impair cellular functions, and
CC by removing proteins whose functions are no longer required. Associated
CC with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC independent protein degradation. This type of proteolysis is required
CC in several pathways including spermatogenesis (20S-PA200 complex) or
CC generation of a subset of MHC class I-presented antigenic peptides
CC (20S-PA28 complex). {ECO:0000269|PubMed:15244466,
CC ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC complex made of 28 subunits that are arranged in four stacked rings.
CC The two outer rings are each formed by seven alpha subunits, and the
CC two inner rings are formed by seven beta subunits. The proteolytic
CC activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.
CC PSMA5 interacts directly with the PSMG1-PSMG2 heterodimer which
CC promotes 20S proteasome assembly. {ECO:0000269|PubMed:16251969,
CC ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:26133119,
CC ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
CC ECO:0000269|PubMed:27493187, ECO:0000269|PubMed:34711951}.
CC -!- INTERACTION:
CC P28066; O14818: PSMA7; NbExp=2; IntAct=EBI-355475, EBI-603272;
CC P28066; P55036: PSMD4; NbExp=2; IntAct=EBI-355475, EBI-359318;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345,
CC ECO:0000269|PubMed:34711951}. Nucleus {ECO:0000269|PubMed:12181345,
CC ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into
CC the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9.
CC {ECO:0000269|PubMed:34711951}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P28066-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28066-2; Sequence=VSP_046241;
CC -!- TISSUE SPECIFICITY: Expressed in fetal brain (at protein level).
CC {ECO:0000269|PubMed:11771738}.
CC -!- INDUCTION: Up-regulated in colon cancer cell lines. Up-regulated in
CC fetal Down syndrome (DS) brain (at protein level). May be the target of
CC the transcriptional activator NFE2L2. {ECO:0000269|PubMed:11771738,
CC ECO:0000269|PubMed:19734940}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; X61970; CAA43962.1; -; mRNA.
DR EMBL; CR456847; CAG33128.1; -; mRNA.
DR EMBL; AK304448; BAG65266.1; -; mRNA.
DR EMBL; AK313351; BAG36153.1; -; mRNA.
DR EMBL; AL356735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56381.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56383.1; -; Genomic_DNA.
DR EMBL; BC102018; AAI02019.1; -; mRNA.
DR EMBL; BC102019; AAI02020.1; -; mRNA.
DR EMBL; BC102020; AAI02021.1; -; mRNA.
DR EMBL; BC103751; AAI03752.1; -; mRNA.
DR CCDS; CCDS55619.1; -. [P28066-2]
DR CCDS; CCDS799.1; -. [P28066-1]
DR PIR; S17521; S17521.
DR RefSeq; NP_001186701.1; NM_001199772.1. [P28066-2]
DR RefSeq; NP_001186702.1; NM_001199773.1. [P28066-2]
DR RefSeq; NP_001186703.1; NM_001199774.1. [P28066-2]
DR RefSeq; NP_002781.2; NM_002790.3. [P28066-1]
DR PDB; 4R3O; X-ray; 2.60 A; E/S=8-241.
DR PDB; 4R67; X-ray; 2.89 A; E/S/g/u=8-241.
DR PDB; 5A0Q; EM; 3.50 A; E/S=1-241.
DR PDB; 5GJQ; EM; 4.50 A; F/l=1-241.
DR PDB; 5GJR; EM; 3.50 A; F/l=1-241.
DR PDB; 5L4G; EM; 4.02 A; E/R=1-241.
DR PDB; 5LE5; X-ray; 1.80 A; D/R=1-241.
DR PDB; 5LEX; X-ray; 2.20 A; D/R=1-241.
DR PDB; 5LEY; X-ray; 1.90 A; D/R=1-241.
DR PDB; 5LEZ; X-ray; 2.19 A; D/R=1-241.
DR PDB; 5LF0; X-ray; 2.41 A; D/R=1-241.
DR PDB; 5LF1; X-ray; 2.00 A; D/R=1-241.
DR PDB; 5LF3; X-ray; 2.10 A; D/R=1-241.
DR PDB; 5LF4; X-ray; 1.99 A; D/R=1-241.
DR PDB; 5LF6; X-ray; 2.07 A; D/R=1-241.
DR PDB; 5LF7; X-ray; 2.00 A; D/R=1-241.
DR PDB; 5LN3; EM; 6.80 A; E=1-241.
DR PDB; 5M32; EM; 3.80 A; D/R=1-241.
DR PDB; 5T0C; EM; 3.80 A; AK/BK=2-241.
DR PDB; 5T0G; EM; 4.40 A; K=2-241.
DR PDB; 5T0H; EM; 6.80 A; K=2-241.
DR PDB; 5T0I; EM; 8.00 A; K=2-241.
DR PDB; 5T0J; EM; 8.00 A; K=2-241.
DR PDB; 5VFO; EM; 3.50 A; K/k=8-241.
DR PDB; 5VFP; EM; 4.20 A; K/k=8-241.
DR PDB; 5VFQ; EM; 4.20 A; K/k=8-241.
DR PDB; 5VFR; EM; 4.90 A; K/k=8-241.
DR PDB; 5VFS; EM; 3.60 A; K/k=8-241.
DR PDB; 5VFT; EM; 7.00 A; K/k=8-241.
DR PDB; 5VFU; EM; 5.80 A; K/k=8-241.
DR PDB; 6AVO; EM; 3.80 A; H/M=1-241.
DR PDB; 6E5B; X-ray; 2.77 A; D/R=1-241.
DR PDB; 6KWY; EM; 2.72 A; D/R=1-241.
DR PDB; 6MSB; EM; 3.00 A; K/k=2-241.
DR PDB; 6MSD; EM; 3.20 A; K/k=2-241.
DR PDB; 6MSE; EM; 3.30 A; Y=170-218.
DR PDB; 6MSG; EM; 3.50 A; K/k=2-241.
DR PDB; 6MSH; EM; 3.60 A; K/k=2-241.
DR PDB; 6MSJ; EM; 3.30 A; K/k=2-241.
DR PDB; 6MSK; EM; 3.20 A; K/k=2-241.
DR PDB; 6R70; EM; 3.50 A; D/R=9-241.
DR PDB; 6REY; EM; 3.00 A; E/S=1-241.
DR PDB; 6RGQ; EM; 2.60 A; E/S=1-241.
DR PDB; 6WJD; EM; 4.80 A; K/k=2-241.
DR PDB; 6WJN; EM; 5.70 A; K/k=8-241.
DR PDB; 6XMJ; EM; 3.00 A; E=8-241.
DR PDB; 7AWE; X-ray; 2.29 A; E/S=9-240.
DR PDB; 7B12; X-ray; 2.43 A; E/s=9-240.
DR PDB; 7LXV; EM; 3.40 A; D/R=1-241.
DR PDB; 7NHT; EM; 2.80 A; D=1-241.
DR PDB; 7PG9; EM; 3.70 A; E/S=1-241.
DR PDB; 7V5G; EM; 4.47 A; S/Z=1-241.
DR PDB; 7V5M; EM; 3.88 A; E/S=1-241.
DR PDBsum; 4R3O; -.
DR PDBsum; 4R67; -.
DR PDBsum; 5A0Q; -.
DR PDBsum; 5GJQ; -.
DR PDBsum; 5GJR; -.
DR PDBsum; 5L4G; -.
DR PDBsum; 5LE5; -.
DR PDBsum; 5LEX; -.
DR PDBsum; 5LEY; -.
DR PDBsum; 5LEZ; -.
DR PDBsum; 5LF0; -.
DR PDBsum; 5LF1; -.
DR PDBsum; 5LF3; -.
DR PDBsum; 5LF4; -.
DR PDBsum; 5LF6; -.
DR PDBsum; 5LF7; -.
DR PDBsum; 5LN3; -.
DR PDBsum; 5M32; -.
DR PDBsum; 5T0C; -.
DR PDBsum; 5T0G; -.
DR PDBsum; 5T0H; -.
DR PDBsum; 5T0I; -.
DR PDBsum; 5T0J; -.
DR PDBsum; 5VFO; -.
DR PDBsum; 5VFP; -.
DR PDBsum; 5VFQ; -.
DR PDBsum; 5VFR; -.
DR PDBsum; 5VFS; -.
DR PDBsum; 5VFT; -.
DR PDBsum; 5VFU; -.
DR PDBsum; 6AVO; -.
DR PDBsum; 6E5B; -.
DR PDBsum; 6KWY; -.
DR PDBsum; 6MSB; -.
DR PDBsum; 6MSD; -.
DR PDBsum; 6MSE; -.
DR PDBsum; 6MSG; -.
DR PDBsum; 6MSH; -.
DR PDBsum; 6MSJ; -.
DR PDBsum; 6MSK; -.
DR PDBsum; 6R70; -.
DR PDBsum; 6REY; -.
DR PDBsum; 6RGQ; -.
DR PDBsum; 6WJD; -.
DR PDBsum; 6WJN; -.
DR PDBsum; 6XMJ; -.
DR PDBsum; 7AWE; -.
DR PDBsum; 7B12; -.
DR PDBsum; 7LXV; -.
DR PDBsum; 7NHT; -.
DR PDBsum; 7PG9; -.
DR PDBsum; 7V5G; -.
DR PDBsum; 7V5M; -.
DR AlphaFoldDB; P28066; -.
DR SMR; P28066; -.
DR BioGRID; 111659; 204.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P28066; -.
DR DIP; DIP-29368N; -.
DR IntAct; P28066; 66.
DR MINT; P28066; -.
DR STRING; 9606.ENSP00000271308; -.
DR BindingDB; P28066; -.
DR ChEMBL; CHEMBL2364701; -.
DR ChEMBL; CHEMBL3831201; -.
DR DrugBank; DB08515; (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE.
DR MEROPS; T01.975; -.
DR GlyGen; P28066; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P28066; -.
DR MetOSite; P28066; -.
DR PhosphoSitePlus; P28066; -.
DR SwissPalm; P28066; -.
DR BioMuta; PSMA5; -.
DR DMDM; 38258905; -.
DR DOSAC-COBS-2DPAGE; P28066; -.
DR REPRODUCTION-2DPAGE; IPI00291922; -.
DR SWISS-2DPAGE; P28066; -.
DR EPD; P28066; -.
DR jPOST; P28066; -.
DR MassIVE; P28066; -.
DR MaxQB; P28066; -.
DR PaxDb; P28066; -.
DR PeptideAtlas; P28066; -.
DR PRIDE; P28066; -.
DR ProteomicsDB; 54441; -. [P28066-1]
DR ProteomicsDB; 5854; -.
DR TopDownProteomics; P28066-1; -. [P28066-1]
DR Antibodypedia; 20062; 464 antibodies from 33 providers.
DR DNASU; 5686; -.
DR Ensembl; ENST00000271308.9; ENSP00000271308.4; ENSG00000143106.13. [P28066-1]
DR Ensembl; ENST00000538610.5; ENSP00000440618.1; ENSG00000143106.13. [P28066-2]
DR GeneID; 5686; -.
DR KEGG; hsa:5686; -.
DR MANE-Select; ENST00000271308.9; ENSP00000271308.4; NM_002790.4; NP_002781.2.
DR UCSC; uc001dxn.4; human. [P28066-1]
DR CTD; 5686; -.
DR DisGeNET; 5686; -.
DR GeneCards; PSMA5; -.
DR HGNC; HGNC:9534; PSMA5.
DR HPA; ENSG00000143106; Low tissue specificity.
DR MIM; 176844; gene.
DR neXtProt; NX_P28066; -.
DR OpenTargets; ENSG00000143106; -.
DR PharmGKB; PA33879; -.
DR VEuPathDB; HostDB:ENSG00000143106; -.
DR eggNOG; KOG0176; Eukaryota.
DR GeneTree; ENSGT00550000074958; -.
DR HOGENOM; CLU_035750_4_2_1; -.
DR InParanoid; P28066; -.
DR OMA; FQVEYAR; -.
DR PhylomeDB; P28066; -.
DR TreeFam; TF106211; -.
DR PathwayCommons; P28066; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P28066; -.
DR SIGNOR; P28066; -.
DR BioGRID-ORCS; 5686; 799 hits in 1095 CRISPR screens.
DR ChiTaRS; PSMA5; human.
DR GeneWiki; PSMA5; -.
DR GenomeRNAi; 5686; -.
DR Pharos; P28066; Tbio.
DR PRO; PR:P28066; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P28066; protein.
DR Bgee; ENSG00000143106; Expressed in oocyte and 206 other tissues.
DR ExpressionAtlas; P28066; baseline and differential.
DR Genevisible; P28066; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR CDD; cd03753; proteasome_alpha_type_5; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR033812; Proteasome_alpha_type_5.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Glycoprotein; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome.
FT CHAIN 1..241
FT /note="Proteasome subunit alpha type-5"
FT /id="PRO_0000124117"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2U1"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 198
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046241"
FT CONFLICT 27
FT /note="A -> D (in Ref. 1; CAA43962)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="V -> L (in Ref. 1; CAA43962)"
FT /evidence="ECO:0000305"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5VFO"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:7AWE"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:6XMJ"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 85..103
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:5LE5"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5LF6"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:5LE5"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:6REY"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:5A0Q"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6RGQ"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:5LE5"
SQ SEQUENCE 241 AA; 26411 MW; 5610CDA00469120A CRC64;
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV EKRITSPLME
PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW FTYNETMTVE SVTQAVSNLA
LQFGEEDADP GAMSRPFGVA LLFGGVDEKG PQLFHMDPSG TFVQCDARAI GSASEGAQSS
LQEVYHKSMT LKEAIKSSLI ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD
I
