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Database: UniProt
Entry: P62195
LinkDB: P62195
Original site: P62195 
ID   PRS8_HUMAN              Reviewed;         406 AA.
AC   P62195; A8K3Z3; A8K763; O35051; O43208; P47210; P52915; P52916;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   02-JUN-2021, entry version 179.
DE   RecName: Full=26S proteasome regulatory subunit 8;
DE   AltName: Full=26S proteasome AAA-ATPase subunit RPT6;
DE   AltName: Full=Proteasome 26S subunit ATPase 5;
DE   AltName: Full=Proteasome subunit p45;
DE   AltName: Full=Thyroid hormone receptor-interacting protein 1;
DE            Short=TRIP1;
DE   AltName: Full=p45/SUG;
GN   Name=PSMC5; Synonyms=SUG1;
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).
RC   TISSUE=Hepatoma;
RX   PubMed=7729537; DOI=10.1016/0014-5793(95)00304-r;
RA   Akiyama K., Yokota K., Kagawa S., Shimbara N., Demartino G.N.,
RA   Slaughter C.A., Noda C., Tanaka K.;
RT   "cDNA cloning of a new putative ATPase subunit p45 of the human 26S
RT   proteasome, a homolog of yeast transcriptional factor Sug1p.";
RL   FEBS Lett. 363:151-156(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
RA   Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
RT   "Two classes of proteins dependent on either the presence or absence of
RT   thyroid hormone for interaction with the thyroid hormone receptor.";
RL   Mol. Endocrinol. 9:243-254(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Skeletal muscle;
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].
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung carcinoma;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-406.
RC   TISSUE=Brain;
RX   PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA   Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA   Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT   "Large-scale concatenation cDNA sequencing.";
RL   Genome Res. 7:353-358(1997).
RN   [7]
RP   FUNCTION.
RX   PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x;
RA   Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N., Yoshimura T.,
RA   Tanaka K., Ichihara A.;
RT   "Demonstration that a human 26S proteolytic complex consists of a
RT   proteasome and multiple associated protein components and hydrolyzes ATP
RT   and ubiquitin-ligated proteins by closely linked mechanisms.";
RL   Eur. J. Biochem. 206:567-578(1992).
RN   [8]
RP   INTERACTION WITH NDC80.
RX   PubMed=9295362; DOI=10.1074/jbc.272.38.24081;
RA   Chen Y., Sharp Z.D., Lee W.-H.;
RT   "HEC binds to the seventh regulatory subunit of the 26 S proteasome and
RT   modulates the proteolysis of mitotic cyclins.";
RL   J. Biol. Chem. 272:24081-24087(1997).
RN   [9]
RP   INTERACTION WITH NDC80.
RX   PubMed=10409732; DOI=10.1128/mcb.19.8.5417;
RA   Zheng L., Chen Y., Lee W.-H.;
RT   "Hec1p, an evolutionarily conserved coiled-coil protein, modulates
RT   chromosome segregation through interaction with SMC proteins.";
RL   Mol. Cell. Biol. 19:5417-5428(1999).
RN   [10]
RP   INTERACTION WITH PAAF1.
RX   PubMed=15831487; DOI=10.1128/mcb.25.9.3842-3853.2005;
RA   Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
RT   "Proteasomal ATPase-associated factor 1 negatively regulates proteasome
RT   activity by interacting with proteasomal ATPases.";
RL   Mol. Cell. Biol. 25:3842-3853(2005).
RN   [11]
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   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=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   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND IDENTIFICATION BY MASS
RP   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   [14]
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   [15]
RP   INTERACTION WITH TRIM5.
RX   PubMed=22078707; DOI=10.1186/1742-4690-8-93;
RA   Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
RA   Luban J., Campbell E.M.;
RT   "TRIM5alpha associates with proteasomal subunits in cells while in complex
RT   with HIV-1 virions.";
RL   Retrovirology 8:93-93(2011).
RN   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [17]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, ACETYLATION [LARGE SCALE
RP   ANALYSIS] AT MET-1 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP   SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [18]
RP   IDENTIFICATION IN A COMPLEX WITH USP49 AND RUVBL1.
RX   PubMed=23824326; DOI=10.1101/gad.211037.112;
RA   Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S.,
RA   Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M.,
RA   Giles K.E., Ma L., Wang H.;
RT   "USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA
RT   splicing.";
RL   Genes Dev. 27:1581-1595(2013).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [20]
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   [21]
RP   ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX   PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA   Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA   Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA   Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT   "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT   acetylation defects.";
RL   Hum. Mol. Genet. 24:1956-1976(2015).
RN   [22]
RP   INTERACTION WITH ERCC6.
RX   PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA   Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA   Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT   "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT   B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT   Dynamics.";
RL   PLoS ONE 10:E0128558-E0128558(2015).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 318-395, AND STRUCTURE BY NMR OF
RP   320-395.
RG   Northeast structural genomics consortium (NESG);
RT   "Crystal structure of a domain of 26s proteasome regulatory subunit 8 from
RT   Homo sapiens. Northeast structural genomics consortium target ID HR3102A.";
RL   Submitted (JAN-2010) to the PDB data bank.
RN   [24]
RP   VARIANT [LARGE SCALE ANALYSIS] GLN-60.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [25]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-440, 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   [26]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS) OF 1-440, 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).
CC   -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       This complex plays a key role in the maintenance of protein homeostasis
CC       by removing misfolded or damaged proteins, which could impair cellular
CC       functions, and by removing proteins whose functions are no longer
CC       required. Therefore, the proteasome participates in numerous cellular
CC       processes, including cell cycle progression, apoptosis, or DNA damage
CC       repair. PSMC5 belongs to the heterohexameric ring of AAA (ATPases
CC       associated with diverse cellular activities) proteins that unfolds
CC       ubiquitinated target proteins that are concurrently translocated into a
CC       proteolytic chamber and degraded into peptides.
CC       {ECO:0000269|PubMed:1317798}.
CC   -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC       The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC       regulatory subunits (RP). The regulatory particle is made of a lid
CC       composed of 9 subunits, a base containing 6 ATPases including PSMC5 and
CC       few additional components (PubMed:27428775, PubMed:27342858). Component
CC       of a complex with USP49 and RUVBL1 (PubMed:23824326). Interacts with
CC       PRPF19. Interacts with TRIM5 (PubMed:22078707). Interacts with NDC80
CC       (PubMed:9295362, PubMed:10409732). Interacts with PAAF1
CC       (PubMed:15831487). Interacts, in vitro, with the thyroid hormone
CC       receptor (in a thyroid hormone T3-dependent manner) and with retinoid X
CC       receptor (RXR) (By similarity). Interacts with ERCC6 (PubMed:26030138).
CC       {ECO:0000250|UniProtKB:P62196, ECO:0000269|PubMed:10409732,
CC       ECO:0000269|PubMed:15831487, ECO:0000269|PubMed:22078707,
CC       ECO:0000269|PubMed:23824326, ECO:0000269|PubMed:26030138,
CC       ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
CC       ECO:0000269|PubMed:9295362}.
CC   -!- INTERACTION:
CC       P62195; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-357745, EBI-1642333;
CC       P62195; Q13515: BFSP2; NbExp=3; IntAct=EBI-357745, EBI-10229433;
CC       P62195; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-357745, EBI-749051;
CC       P62195; P19447: ERCC3; NbExp=4; IntAct=EBI-357745, EBI-1183307;
CC       P62195; P62508-3: ESRRG; NbExp=3; IntAct=EBI-357745, EBI-12001340;
CC       P62195; Q6FG41: FOS; NbExp=3; IntAct=EBI-357745, EBI-10198738;
CC       P62195; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-357745, EBI-3044087;
CC       P62195; Q15323: KRT31; NbExp=3; IntAct=EBI-357745, EBI-948001;
CC       P62195; O76015: KRT38; NbExp=6; IntAct=EBI-357745, EBI-1047263;
CC       P62195; Q6A162: KRT40; NbExp=5; IntAct=EBI-357745, EBI-10171697;
CC       P62195; Q9BRP4: PAAF1; NbExp=2; IntAct=EBI-357745, EBI-1056358;
CC       P62195; Q13371: PDCL; NbExp=16; IntAct=EBI-357745, EBI-5772890;
CC       P62195; Q53GL0: PLEKHO1; NbExp=10; IntAct=EBI-357745, EBI-949945;
CC       P62195; P35998: PSMC2; NbExp=11; IntAct=EBI-357745, EBI-359710;
CC       P62195; P43686: PSMC4; NbExp=15; IntAct=EBI-357745, EBI-743997;
CC       P62195; P62333: PSMC6; NbExp=14; IntAct=EBI-357745, EBI-357669;
CC       P62195; Q13200: PSMD2; NbExp=10; IntAct=EBI-357745, EBI-357648;
CC       P62195; P55036: PSMD4; NbExp=2; IntAct=EBI-357745, EBI-359318;
CC       P62195; P10826-2: RARB; NbExp=3; IntAct=EBI-357745, EBI-8583223;
CC       P62195; Q92753-1: RORB; NbExp=3; IntAct=EBI-357745, EBI-18560266;
CC       P62195; P51449: RORC; NbExp=3; IntAct=EBI-357745, EBI-3908771;
CC       P62195; Q96BD8: SKA1; NbExp=7; IntAct=EBI-357745, EBI-741854;
CC       P62195; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-357745, EBI-1105213;
CC       P62195; P48788: TNNI2; NbExp=3; IntAct=EBI-357745, EBI-7746394;
CC       P62195; P09493-10: TPM1; NbExp=3; IntAct=EBI-357745, EBI-12123928;
CC       P62195; P06753: TPM3; NbExp=3; IntAct=EBI-357745, EBI-355607;
CC       P62195; Q01831: XPC; NbExp=2; IntAct=EBI-357745, EBI-372610;
CC       P62195; P11275: Camk2a; Xeno; NbExp=4; IntAct=EBI-357745, EBI-2640645;
CC       P62195; P08413: Camk2b; Xeno; NbExp=3; IntAct=EBI-357745, EBI-916155;
CC       P62195; P03255-1; Xeno; NbExp=2; IntAct=EBI-357745, EBI-6692439;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P62195-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P62195-2; Sequence=VSP_045441;
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; D44467; BAA07919.1; -; mRNA.
DR   EMBL; L38810; AAC41735.1; -; mRNA.
DR   EMBL; AK290758; BAF83447.1; -; mRNA.
DR   EMBL; AK291878; BAF84567.1; -; mRNA.
DR   EMBL; AC015651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471109; EAW94270.1; -; Genomic_DNA.
DR   EMBL; CH471109; EAW94271.1; -; Genomic_DNA.
DR   EMBL; CH471109; EAW94272.1; -; Genomic_DNA.
DR   EMBL; BC001932; AAH01932.1; -; mRNA.
DR   EMBL; BC002367; AAH02367.3; -; mRNA.
DR   EMBL; AF035309; AAB88187.1; -; mRNA.
DR   CCDS; CCDS11645.1; -. [P62195-1]
DR   CCDS; CCDS56043.1; -. [P62195-2]
DR   PIR; S60343; S60343.
DR   PIR; S65536; S65536.
DR   RefSeq; NP_001186092.1; NM_001199163.1. [P62195-2]
DR   RefSeq; NP_002796.4; NM_002805.5. [P62195-1]
DR   PDB; 2KRK; NMR; -; A=320-395.
DR   PDB; 3KW6; X-ray; 2.10 A; A=318-395.
DR   PDB; 5GJQ; EM; 4.50 A; J=1-406.
DR   PDB; 5GJR; EM; 3.50 A; J/x=1-406.
DR   PDB; 5L4G; EM; 4.02 A; J=1-406.
DR   PDB; 5LN3; EM; 6.80 A; J=1-406.
DR   PDB; 5M32; EM; 3.80 A; h=38-392.
DR   PDB; 5T0C; EM; 3.80 A; AC/BC=1-406.
DR   PDB; 5T0G; EM; 4.40 A; C=9-406.
DR   PDB; 5T0H; EM; 6.80 A; C=9-406.
DR   PDB; 5T0I; EM; 8.00 A; C=9-406.
DR   PDB; 5T0J; EM; 8.00 A; C=9-406.
DR   PDB; 5VFP; EM; 4.20 A; C=11-402.
DR   PDB; 5VFQ; EM; 4.20 A; C=11-402.
DR   PDB; 5VFR; EM; 4.90 A; C=11-402.
DR   PDB; 5VFS; EM; 3.60 A; C=9-397.
DR   PDB; 5VFT; EM; 7.00 A; C=11-394.
DR   PDB; 5VFU; EM; 5.80 A; C=11-394.
DR   PDB; 5VGZ; EM; 3.70 A; C=11-128.
DR   PDB; 5VHF; EM; 5.70 A; C=11-395.
DR   PDB; 5VHH; EM; 6.10 A; C=11-395.
DR   PDB; 5VHI; EM; 6.80 A; C=11-395.
DR   PDB; 5VHJ; EM; 8.50 A; C=130-395.
DR   PDB; 5VHM; EM; 8.30 A; C=130-395.
DR   PDB; 5VHN; EM; 7.30 A; C=130-395.
DR   PDB; 5VHO; EM; 8.30 A; C=130-395.
DR   PDB; 5VHP; EM; 7.90 A; C=130-395.
DR   PDB; 5VHQ; EM; 8.90 A; C=130-395.
DR   PDB; 5VHR; EM; 7.70 A; C=130-395.
DR   PDB; 5VHS; EM; 8.80 A; C=11-395.
DR   PDB; 6MSB; EM; 3.00 A; C=9-406.
DR   PDB; 6MSD; EM; 3.20 A; C=9-406.
DR   PDB; 6MSG; EM; 3.50 A; C=9-406.
DR   PDB; 6MSH; EM; 3.60 A; C=9-406.
DR   PDB; 6MSJ; EM; 3.30 A; C=9-406.
DR   PDB; 6MSK; EM; 3.20 A; C=9-406.
DR   PDB; 6WJD; EM; 4.80 A; C=9-406.
DR   PDB; 6WJN; EM; 5.70 A; C=11-402.
DR   PDBsum; 2KRK; -.
DR   PDBsum; 3KW6; -.
DR   PDBsum; 5GJQ; -.
DR   PDBsum; 5GJR; -.
DR   PDBsum; 5L4G; -.
DR   PDBsum; 5LN3; -.
DR   PDBsum; 5M32; -.
DR   PDBsum; 5T0C; -.
DR   PDBsum; 5T0G; -.
DR   PDBsum; 5T0H; -.
DR   PDBsum; 5T0I; -.
DR   PDBsum; 5T0J; -.
DR   PDBsum; 5VFP; -.
DR   PDBsum; 5VFQ; -.
DR   PDBsum; 5VFR; -.
DR   PDBsum; 5VFS; -.
DR   PDBsum; 5VFT; -.
DR   PDBsum; 5VFU; -.
DR   PDBsum; 5VGZ; -.
DR   PDBsum; 5VHF; -.
DR   PDBsum; 5VHH; -.
DR   PDBsum; 5VHI; -.
DR   PDBsum; 5VHJ; -.
DR   PDBsum; 5VHM; -.
DR   PDBsum; 5VHN; -.
DR   PDBsum; 5VHO; -.
DR   PDBsum; 5VHP; -.
DR   PDBsum; 5VHQ; -.
DR   PDBsum; 5VHR; -.
DR   PDBsum; 5VHS; -.
DR   PDBsum; 6MSB; -.
DR   PDBsum; 6MSD; -.
DR   PDBsum; 6MSG; -.
DR   PDBsum; 6MSH; -.
DR   PDBsum; 6MSJ; -.
DR   PDBsum; 6MSK; -.
DR   PDBsum; 6WJD; -.
DR   PDBsum; 6WJN; -.
DR   BMRB; P62195; -.
DR   SMR; P62195; -.
DR   BioGRID; 111678; 335.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P62195; -.
DR   DIP; DIP-36645N; -.
DR   IntAct; P62195; 150.
DR   MINT; P62195; -.
DR   STRING; 9606.ENSP00000310572; -.
DR   ChEMBL; CHEMBL2364701; -.
DR   GlyGen; P62195; 1 site.
DR   iPTMnet; P62195; -.
DR   MetOSite; P62195; -.
DR   PhosphoSitePlus; P62195; -.
DR   SwissPalm; P62195; -.
DR   BioMuta; PSMC5; -.
DR   DMDM; 49065819; -.
DR   EPD; P62195; -.
DR   jPOST; P62195; -.
DR   MassIVE; P62195; -.
DR   MaxQB; P62195; -.
DR   PaxDb; P62195; -.
DR   PeptideAtlas; P62195; -.
DR   PRIDE; P62195; -.
DR   ProteomicsDB; 1859; -.
DR   ProteomicsDB; 57371; -. [P62195-1]
DR   Antibodypedia; 18742; 304 antibodies.
DR   DNASU; 5705; -.
DR   Ensembl; ENST00000310144; ENSP00000310572; ENSG00000087191. [P62195-1]
DR   Ensembl; ENST00000375812; ENSP00000364970; ENSG00000087191. [P62195-2]
DR   Ensembl; ENST00000580864; ENSP00000462495; ENSG00000087191. [P62195-2]
DR   Ensembl; ENST00000581882; ENSP00000463938; ENSG00000087191. [P62195-2]
DR   GeneID; 5705; -.
DR   KEGG; hsa:5705; -.
DR   UCSC; uc002jcb.4; human. [P62195-1]
DR   CTD; 5705; -.
DR   DisGeNET; 5705; -.
DR   GeneCards; PSMC5; -.
DR   HGNC; HGNC:9552; PSMC5.
DR   HPA; ENSG00000087191; Low tissue specificity.
DR   MIM; 601681; gene.
DR   neXtProt; NX_P62195; -.
DR   NIAGADS; ENSG00000087191; -.
DR   OpenTargets; ENSG00000087191; -.
DR   PharmGKB; PA33897; -.
DR   VEuPathDB; HostDB:ENSG00000087191.12; -.
DR   eggNOG; KOG0728; Eukaryota.
DR   GeneTree; ENSGT01020000230346; -.
DR   HOGENOM; CLU_000688_2_0_1; -.
DR   InParanoid; P62195; -.
DR   OMA; MALDTFF; -.
DR   OrthoDB; 571919at2759; -.
DR   PhylomeDB; P62195; -.
DR   PathwayCommons; P62195; -.
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; P62195; -.
DR   BioGRID-ORCS; 5705; 587 hits in 969 CRISPR screens.
DR   ChiTaRS; PSMC5; human.
DR   EvolutionaryTrace; P62195; -.
DR   GeneWiki; PSMC5; -.
DR   GenomeRNAi; 5705; -.
DR   Pharos; P62195; Tbio.
DR   PRO; PR:P62195; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P62195; protein.
DR   Bgee; ENSG00000087191; Expressed in testis and 245 other tissues.
DR   ExpressionAtlas; P62195; baseline and differential.
DR   Genevisible; P62195; HS.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0031597; C:cytosolic proteasome complex; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0031595; C:nuclear proteasome complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR   GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR   GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
DR   GO; GO:0036402; F:proteasome-activating ATPase activity; IEA:InterPro.
DR   GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR   GO; GO:0031531; F:thyrotropin-releasing hormone receptor binding; IPI:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IDA:GO_Central.
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:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
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:0043069; P:negative regulation of programmed cell death; NAS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
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:0090261; P:positive regulation of inclusion body assembly; IEA:Ensembl.
DR   GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
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: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:0006357; P:regulation of transcription by RNA polymerase II; IDA:GO_Central.
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   InterPro; IPR005937; 26S_Psome_P45-like.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01242; 26Sp45; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Proteasome;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:25489052,
FT                   ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..406
FT                   /note="26S proteasome regulatory subunit 8"
FT                   /id="PRO_0000084721"
FT   NP_BIND         190..197
FT                   /note="ATP"
FT                   /evidence="ECO:0000255"
FT   REGION          186..406
FT                   /note="May mediate interaction with PRPF9"
FT                   /evidence="ECO:0000250|UniProtKB:P62196"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:25489052,
FT                   ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         222
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         1..8
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045441"
FT   VARIANT         60
FT                   /note="R -> Q (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035901"
FT   VARIANT         258
FT                   /note="R -> W (in dbSNP:rs11543211)"
FT                   /id="VAR_048119"
FT   CONFLICT        61
FT                   /note="E -> R (in Ref. 1; BAA07919)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127..128
FT                   /note="LP -> ML (in Ref. 6; AAB88187)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        266
FT                   /note="D -> S (in Ref. 2; AAC41735)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="T -> Q (in Ref. 2; AAC41735)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        300
FT                   /note="I -> M (in Ref. 2; AAC41735)"
FT                   /evidence="ECO:0000305"
FT   HELIX           322..333
FT                   /evidence="ECO:0007829|PDB:3KW6"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:3KW6"
FT   HELIX           344..349
FT                   /evidence="ECO:0007829|PDB:3KW6"
FT   HELIX           356..372
FT                   /evidence="ECO:0007829|PDB:3KW6"
FT   STRAND          376..378
FT                   /evidence="ECO:0007829|PDB:3KW6"
FT   HELIX           380..391
FT                   /evidence="ECO:0007829|PDB:3KW6"
FT   MOD_RES         P62195-2:1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   406 AA;  45626 MW;  29C6410C4A85A7F7 CRC64;
     MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN ELNAKVRLLR
     EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD KNIDINDVTP NCRVALRNDS
     YTLHKILPNK VDPLVSLMMV EKVPDSTYEM IGGLDKQIKE IKEVIELPVK HPELFEALGI
     AQPKGVLLYG PPGTGKTLLA RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE
     HAPSIIFMDE IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI
     LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL MPGASGAEVK
     GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS IKKLWK
//
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