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Database: UniProt
Entry: P60900
LinkDB: P60900
Original site: P60900 
ID   PSA6_HUMAN              Reviewed;         246 AA.
AC   P60900; B2R7J9; B4DQR4; B4DXJ9; P34062; Q6IB60;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   02-JUN-2021, entry version 191.
DE   RecName: Full=Proteasome subunit alpha type-6;
DE   AltName: Full=27 kDa prosomal protein;
DE            Short=PROS-27;
DE            Short=p27K;
DE   AltName: Full=Macropain iota chain;
DE   AltName: Full=Multicatalytic endopeptidase complex iota chain;
DE   AltName: Full=Proteasome iota chain;
GN   Name=PSMA6; Synonyms=PROS27;
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=7681138; DOI=10.1007/bf00282801;
RA   Bey F., Pereira I.S., Coux O., Viegas-Pequignot E., Targa F.R.,
RA   Nothwang H.G., Dutrillaux B., Scherrer K.;
RT   "The prosomal RNA-binding protein p27K is a member of the alpha-type human
RT   prosomal gene family.";
RL   Mol. Gen. Genet. 237:193-205(1993).
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; 2 AND 3).
RC   TISSUE=Cerebellum, and Testis;
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=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, Lymph, Skeletal muscle, 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   PROTEIN SEQUENCE OF 12-43; 60-88; 105-116; 154-164; 172-181 AND 229-246,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Fetal brain cortex;
RA   Lubec G., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 26-246 (ISOFORM 1), AND PARTIAL PROTEIN
RP   SEQUENCE.
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   [9]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
RA   Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
RT   "Human proteasome subunits from 2-dimensional gels identified by partial
RT   sequencing.";
RL   Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
RN   [10]
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   [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   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   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-104, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [15]
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   [16]
RP   INTERACTION WITH ALKBH4.
RX   PubMed=23145062; DOI=10.1371/journal.pone.0049045;
RA   Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A.,
RA   Falnes P.O.;
RT   "Human ALKBH4 interacts with proteins associated with transcription.";
RL   PLoS ONE 7:E49045-E49045(2012).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-63 AND SER-64, 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   [18]
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   [19]
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   [20]
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   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-245, 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   [22]
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   [23]
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   [24]
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).
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       Interacts with ALKBH4 (PubMed:23145062). {ECO:0000269|PubMed:23145062,
CC       ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:26133119,
CC       ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
CC       ECO:0000269|PubMed:27493187}.
CC   -!- INTERACTION:
CC       P60900; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-357793, EBI-741210;
CC       P60900; Q8N9M1-2: C19orf47; NbExp=3; IntAct=EBI-357793, EBI-10979594;
CC       P60900; Q9BY67: CADM1; NbExp=3; IntAct=EBI-357793, EBI-5652260;
CC       P60900; P84090: ERH; NbExp=3; IntAct=EBI-357793, EBI-711389;
CC       P60900; P42858: HTT; NbExp=4; IntAct=EBI-357793, EBI-466029;
CC       P60900; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-357793, EBI-10172511;
CC       P60900; Q9BT23: LIMD2; NbExp=3; IntAct=EBI-357793, EBI-2805292;
CC       P60900; P62875: POLR2L; NbExp=3; IntAct=EBI-357793, EBI-359527;
CC       P60900; P25787: PSMA2; NbExp=5; IntAct=EBI-357793, EBI-603262;
CC       P60900; P25788: PSMA3; NbExp=10; IntAct=EBI-357793, EBI-348380;
CC       P60900; P25789: PSMA4; NbExp=5; IntAct=EBI-357793, EBI-359310;
CC       P60900; O14818: PSMA7; NbExp=11; IntAct=EBI-357793, EBI-603272;
CC       P60900; O43242: PSMD3; NbExp=3; IntAct=EBI-357793, EBI-357622;
CC       P60900; Q96K19: RNF170; NbExp=3; IntAct=EBI-357793, EBI-2130336;
CC       P60900; Q14D33: RTP5; NbExp=3; IntAct=EBI-357793, EBI-10217913;
CC       P60900; A2RU48: SMCO3; NbExp=3; IntAct=EBI-357793, EBI-10173195;
CC       P60900; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-357793, EBI-11139477;
CC       P60900; Q9HCM9: TRIM39; NbExp=3; IntAct=EBI-357793, EBI-739510;
CC       P60900; Q9HCM9-2: TRIM39; NbExp=5; IntAct=EBI-357793, EBI-11523450;
CC       P60900; Q6FI91: TSPYL; NbExp=3; IntAct=EBI-357793, EBI-723389;
CC       P60900; Q9Y5K5: UCHL5; NbExp=4; IntAct=EBI-357793, EBI-1051183;
CC       P60900; Q8NCP5: ZBTB44; NbExp=3; IntAct=EBI-357793, EBI-5658292;
CC       P60900; Q969J2: ZKSCAN4; NbExp=3; IntAct=EBI-357793, EBI-2818641;
CC       P60900; Q8TC21: ZNF596; NbExp=3; IntAct=EBI-357793, EBI-3923453;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}. Nucleus
CC       {ECO:0000269|PubMed:12181345}. Note=Colocalizes with TRIM5 in
CC       cytoplasmic bodies. {ECO:0000250|UniProtKB:Q9QUM9}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P60900-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P60900-2; Sequence=VSP_054587;
CC       Name=3;
CC         IsoId=P60900-3; Sequence=VSP_054586;
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; X59417; CAA42052.1; -; mRNA.
DR   EMBL; CR456944; CAG33225.1; -; mRNA.
DR   EMBL; AK298920; BAG61026.1; -; mRNA.
DR   EMBL; AK302008; BAG63411.1; -; mRNA.
DR   EMBL; AK313011; BAG35846.1; -; mRNA.
DR   EMBL; AK316223; BAH14594.1; -; mRNA.
DR   EMBL; AL121594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL133163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471078; EAW65876.1; -; Genomic_DNA.
DR   EMBL; CH471078; EAW65877.1; -; Genomic_DNA.
DR   EMBL; BC002979; AAH02979.1; -; mRNA.
DR   EMBL; BC017882; AAH17882.1; -; mRNA.
DR   EMBL; BC022354; AAH22354.1; -; mRNA.
DR   EMBL; BC023659; AAH23659.1; -; mRNA.
DR   EMBL; BC070137; AAH70137.1; -; mRNA.
DR   EMBL; X61972; CAA43964.1; -; mRNA.
DR   CCDS; CCDS61437.1; -. [P60900-2]
DR   CCDS; CCDS61438.1; -. [P60900-3]
DR   CCDS; CCDS9655.1; -. [P60900-1]
DR   PIR; S30274; S30274.
DR   RefSeq; NP_001269161.1; NM_001282232.1. [P60900-3]
DR   RefSeq; NP_001269162.1; NM_001282233.1. [P60900-3]
DR   RefSeq; NP_001269163.1; NM_001282234.1. [P60900-2]
DR   RefSeq; NP_002782.1; NM_002791.2. [P60900-1]
DR   RefSeq; XP_016876957.1; XM_017021468.1. [P60900-3]
DR   PDB; 4R3O; X-ray; 2.60 A; A/O=2-245.
DR   PDB; 4R67; X-ray; 2.89 A; A/O/c/q=2-245.
DR   PDB; 5A0Q; EM; 3.50 A; A/O=1-246.
DR   PDB; 5GJQ; EM; 4.50 A; B/h=1-246.
DR   PDB; 5GJR; EM; 3.50 A; B/h=1-246.
DR   PDB; 5L4G; EM; 4.02 A; A/N=1-246.
DR   PDB; 5LE5; X-ray; 1.80 A; G/U=1-246.
DR   PDB; 5LEX; X-ray; 2.20 A; G/U=1-246.
DR   PDB; 5LEY; X-ray; 1.90 A; G/U=1-246.
DR   PDB; 5LEZ; X-ray; 2.19 A; G/U=1-246.
DR   PDB; 5LF0; X-ray; 2.41 A; G/U=1-246.
DR   PDB; 5LF1; X-ray; 2.00 A; G/U=1-246.
DR   PDB; 5LF3; X-ray; 2.10 A; G/U=1-246.
DR   PDB; 5LF4; X-ray; 1.99 A; G/U=1-246.
DR   PDB; 5LF6; X-ray; 2.07 A; G/U=1-246.
DR   PDB; 5LF7; X-ray; 2.00 A; G/U=1-246.
DR   PDB; 5LN3; EM; 6.80 A; A=1-246.
DR   PDB; 5M32; EM; 3.80 A; G/U=1-246.
DR   PDB; 5T0C; EM; 3.80 A; AG/BG=2-246.
DR   PDB; 5T0G; EM; 4.40 A; G=2-246.
DR   PDB; 5T0H; EM; 6.80 A; G=2-246.
DR   PDB; 5T0I; EM; 8.00 A; G=2-246.
DR   PDB; 5T0J; EM; 8.00 A; G=2-246.
DR   PDB; 5VFO; EM; 3.50 A; G/g=5-244.
DR   PDB; 5VFP; EM; 4.20 A; G/g=5-244.
DR   PDB; 5VFQ; EM; 4.20 A; G/g=5-244.
DR   PDB; 5VFR; EM; 4.90 A; G/g=5-244.
DR   PDB; 5VFS; EM; 3.60 A; G/g=5-244.
DR   PDB; 5VFT; EM; 7.00 A; G/g=5-244.
DR   PDB; 5VFU; EM; 5.80 A; G/g=5-244.
DR   PDB; 6AVO; EM; 3.80 A; K/R=1-246.
DR   PDB; 6E5B; X-ray; 2.77 A; G/U=1-246.
DR   PDB; 6KWY; EM; 2.72 A; G/U=1-246.
DR   PDB; 6MSB; EM; 3.00 A; G/g=2-246.
DR   PDB; 6MSD; EM; 3.20 A; G/g=2-246.
DR   PDB; 6MSG; EM; 3.50 A; G/g=2-246.
DR   PDB; 6MSH; EM; 3.60 A; G/g=2-246.
DR   PDB; 6MSK; EM; 3.20 A; G/g=2-246.
DR   PDB; 6R70; EM; 3.50 A; G/U=2-245.
DR   PDB; 6REY; EM; 3.00 A; A/O=1-246.
DR   PDB; 6RGQ; EM; 2.60 A; A/O=1-246.
DR   PDB; 6WJD; EM; 4.80 A; G/g=2-246.
DR   PDB; 6WJN; EM; 5.70 A; G/g=5-244.
DR   PDB; 6XMJ; EM; 3.00 A; A=2-245.
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; 6MSG; -.
DR   PDBsum; 6MSH; -.
DR   PDBsum; 6MSK; -.
DR   PDBsum; 6R70; -.
DR   PDBsum; 6REY; -.
DR   PDBsum; 6RGQ; -.
DR   PDBsum; 6WJD; -.
DR   PDBsum; 6WJN; -.
DR   PDBsum; 6XMJ; -.
DR   SMR; P60900; -.
DR   BioGRID; 111660; 205.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P60900; -.
DR   DIP; DIP-29367N; -.
DR   IntAct; P60900; 78.
DR   MINT; P60900; -.
DR   STRING; 9606.ENSP00000261479; -.
DR   BindingDB; P60900; -.
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; T01.971; -.
DR   GlyGen; P60900; 1 site.
DR   iPTMnet; P60900; -.
DR   MetOSite; P60900; -.
DR   PhosphoSitePlus; P60900; -.
DR   SwissPalm; P60900; -.
DR   BioMuta; PSMA6; -.
DR   DMDM; 46397659; -.
DR   REPRODUCTION-2DPAGE; IPI00029623; -.
DR   SWISS-2DPAGE; P60900; -.
DR   UCD-2DPAGE; P60900; -.
DR   EPD; P60900; -.
DR   jPOST; P60900; -.
DR   MassIVE; P60900; -.
DR   MaxQB; P60900; -.
DR   PaxDb; P60900; -.
DR   PeptideAtlas; P60900; -.
DR   PRIDE; P60900; -.
DR   ProteomicsDB; 4898; -.
DR   ProteomicsDB; 5443; -.
DR   ProteomicsDB; 57236; -. [P60900-1]
DR   TopDownProteomics; P60900-1; -. [P60900-1]
DR   Antibodypedia; 155; 474 antibodies.
DR   DNASU; 5687; -.
DR   Ensembl; ENST00000261479; ENSP00000261479; ENSG00000100902. [P60900-1]
DR   Ensembl; ENST00000540871; ENSP00000444844; ENSG00000100902. [P60900-2]
DR   Ensembl; ENST00000555764; ENSP00000452566; ENSG00000100902. [P60900-3]
DR   Ensembl; ENST00000622405; ENSP00000479620; ENSG00000100902. [P60900-3]
DR   GeneID; 5687; -.
DR   KEGG; hsa:5687; -.
DR   UCSC; uc001wtd.5; human. [P60900-1]
DR   CTD; 5687; -.
DR   DisGeNET; 5687; -.
DR   GeneCards; PSMA6; -.
DR   HGNC; HGNC:9535; PSMA6.
DR   HPA; ENSG00000100902; Low tissue specificity.
DR   MalaCards; PSMA6; -.
DR   MIM; 602855; gene.
DR   neXtProt; NX_P60900; -.
DR   OpenTargets; ENSG00000100902; -.
DR   PharmGKB; PA33880; -.
DR   VEuPathDB; HostDB:ENSG00000100902.10; -.
DR   eggNOG; KOG0182; Eukaryota.
DR   GeneTree; ENSGT00550000074807; -.
DR   HOGENOM; CLU_035750_6_0_1; -.
DR   InParanoid; P60900; -.
DR   PhylomeDB; P60900; -.
DR   TreeFam; TF106210; -.
DR   PathwayCommons; P60900; -.
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-68827; CDT1 association with the CDC6:ORC:origin 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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SIGNOR; P60900; -.
DR   BioGRID-ORCS; 5687; 782 hits in 969 CRISPR screens.
DR   ChiTaRS; PSMA6; human.
DR   GeneWiki; PSMA6; -.
DR   GenomeRNAi; 5687; -.
DR   Pharos; P60900; Tbio.
DR   PRO; PR:P60900; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; P60900; protein.
DR   Bgee; ENSG00000100902; Expressed in testis and 125 other tissues.
DR   ExpressionAtlas; P60900; baseline and differential.
DR   Genevisible; P60900; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0030016; C:myofibril; ISS:BHF-UCL.
DR   GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR   GO; GO:0005844; C:polysome; IDA:BHF-UCL.
DR   GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR   GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:UniProtKB.
DR   GO; GO:0030017; C:sarcomere; ISS:BHF-UCL.
DR   GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0051059; F:NF-kappaB binding; IPI:BHF-UCL.
DR   GO; GO:0035639; F:purine ribonucleoside triphosphate binding; NAS:BHF-UCL.
DR   GO; GO:0003723; F:RNA binding; IDA:BHF-UCL.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0036388; P:pre-replicative complex assembly; TAS:Reactome.
DR   GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR   GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IMP:BHF-UCL.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR   GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
DR   GO; GO:0050727; P:regulation of inflammatory response; IC:BHF-UCL.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
DR   CDD; cd03754; proteasome_alpha_type_6; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR034642; Proteasome_subunit_alpha6.
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..246
FT                   /note="Proteasome subunit alpha type-6"
FT                   /id="PRO_0000124130"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         63
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         102
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         104
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         159
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QUM9"
FT   CARBOHYD        5
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..79
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054586"
FT   VAR_SEQ         1..25
FT                   /note="MSRGSSAGFDRHITIFSPEGRLYQV -> MAGLRR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054587"
FT   CONFLICT        59
FT                   /note="K -> C (in Ref. 8; CAA43964)"
FT                   /evidence="ECO:0000305"
FT   TURN            8..12
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          18..20
FT                   /evidence="ECO:0007829|PDB:5VFO"
FT   HELIX           23..34
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          38..42
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          49..53
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:5LF0"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          76..82
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           84..105
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           111..125
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          128..131
FT                   /evidence="ECO:0007829|PDB:4R3O"
FT   STRAND          135..144
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   TURN            145..147
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          148..154
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:4R3O"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:5A0Q"
FT   STRAND          163..169
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           172..185
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          191..193
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           194..206
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          215..219
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          228..230
FT                   /evidence="ECO:0007829|PDB:6E5B"
FT   HELIX           232..243
FT                   /evidence="ECO:0007829|PDB:5LE5"
SQ   SEQUENCE   246 AA;  27399 MW;  94D1FD3C0A7CC72A CRC64;
     MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI VTQKKVPDKL
     LDSSTVTHLF KITENIGCVM TGMTADSRSQ VQRARYEAAN WKYKYGYEIP VDMLCKRIAD
     ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ VYKCDPAGYY CGFKATAAGV KQTESTSFLE
     KKVKKKFDWT FEQTVETAIT CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV
     ALAERD
//
DBGET integrated database retrieval system