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Database: UniProt
Entry: Q9UHB9
LinkDB: Q9UHB9
Original site: Q9UHB9 
ID   SRP68_HUMAN             Reviewed;         627 AA.
AC   Q9UHB9; B3KUU5; B3KWY7; G3V1U4; Q8NCJ4; Q8WUK2;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2003, sequence version 2.
DT   29-SEP-2021, entry version 180.
DE   RecName: Full=Signal recognition particle subunit SRP68;
DE            Short=SRP68;
DE   AltName: Full=Signal recognition particle 68 kDa protein;
GN   Name=SRP68;
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=10618370; DOI=10.1073/pnas.97.1.55;
RA   Politz J.C., Yarovoi S., Kilroy S.M., Gowda K., Zwieb C., Pederson T.;
RT   "Signal recognition particle components in the nucleolus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:55-60(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   TISSUE=Liver, Mammary gland, and Thymus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [7]
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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-452, 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   [9]
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   [10]
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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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   [13]
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   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Signal-recognition-particle assembly has a crucial role in
CC       targeting secretory proteins to the rough endoplasmic reticulum
CC       membrane. SRP68 binds the 7S RNA, SRP72 binds to this complex
CC       subsequently. This ribonucleoprotein complex might interact directly
CC       with the docking protein in the ER membrane and possibly participate in
CC       the elongation arrest function.
CC   -!- SUBUNIT: Signal recognition particle consists of a 7S RNA molecule of
CC       300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19,
CC       SRP14 and SRP9.
CC   -!- INTERACTION:
CC       Q9UHB9; P09132: SRP19; NbExp=2; IntAct=EBI-1048560, EBI-2680090;
CC       Q9UHB9-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12210563, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9UHB9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UHB9-2; Sequence=VSP_008347;
CC       Name=3;
CC         IsoId=Q9UHB9-3; Sequence=VSP_045132;
CC       Name=4;
CC         IsoId=Q9UHB9-4; Sequence=VSP_046944;
CC   -!- DOMAIN: The RNA-binding domain is located near the N-terminus.
CC   -!- SIMILARITY: Belongs to the SRP68 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Signal recognition particle entry;
CC       URL="https://en.wikipedia.org/wiki/Signal-recognition_particle";
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DR   EMBL; AF195951; AAF24308.1; -; mRNA.
DR   EMBL; AK074698; BAC11145.1; -; mRNA.
DR   EMBL; AK097962; BAG53557.1; -; mRNA.
DR   EMBL; AK126258; BAG54299.1; -; mRNA.
DR   EMBL; AC040980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471099; EAW89360.1; -; Genomic_DNA.
DR   EMBL; CH471099; EAW89362.1; -; Genomic_DNA.
DR   EMBL; BC020238; AAH20238.1; -; mRNA.
DR   CCDS; CCDS11738.1; -. [Q9UHB9-1]
DR   CCDS; CCDS58600.1; -. [Q9UHB9-3]
DR   CCDS; CCDS58601.1; -. [Q9UHB9-4]
DR   RefSeq; NP_001247431.1; NM_001260502.1. [Q9UHB9-4]
DR   RefSeq; NP_001247432.1; NM_001260503.1. [Q9UHB9-3]
DR   RefSeq; NP_055045.2; NM_014230.3. [Q9UHB9-1]
DR   PDB; 4P3E; X-ray; 3.50 A; C=47-254.
DR   PDB; 4P3F; X-ray; 1.70 A; A/B=47-254.
DR   PDB; 5M72; X-ray; 1.60 A; B=546-614.
DR   PDB; 5M73; X-ray; 3.40 A; C/G=60-254.
DR   PDB; 5WRV; X-ray; 1.70 A; A=509-614.
DR   PDB; 7NFX; EM; 3.20 A; u=1-627.
DR   PDBsum; 4P3E; -.
DR   PDBsum; 4P3F; -.
DR   PDBsum; 5M72; -.
DR   PDBsum; 5M73; -.
DR   PDBsum; 5WRV; -.
DR   PDBsum; 7NFX; -.
DR   SMR; Q9UHB9; -.
DR   BioGRID; 112608; 126.
DR   DIP; DIP-50905N; -.
DR   IntAct; Q9UHB9; 55.
DR   MINT; Q9UHB9; -.
DR   STRING; 9606.ENSP00000312066; -.
DR   TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR   GlyGen; Q9UHB9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UHB9; -.
DR   PhosphoSitePlus; Q9UHB9; -.
DR   SwissPalm; Q9UHB9; -.
DR   BioMuta; SRP68; -.
DR   DMDM; 37154869; -.
DR   EPD; Q9UHB9; -.
DR   jPOST; Q9UHB9; -.
DR   MassIVE; Q9UHB9; -.
DR   PaxDb; Q9UHB9; -.
DR   PeptideAtlas; Q9UHB9; -.
DR   PRIDE; Q9UHB9; -.
DR   ProteomicsDB; 32444; -.
DR   ProteomicsDB; 3735; -.
DR   ProteomicsDB; 84303; -. [Q9UHB9-1]
DR   ProteomicsDB; 84304; -. [Q9UHB9-2]
DR   Antibodypedia; 19656; 135 antibodies.
DR   DNASU; 6730; -.
DR   Ensembl; ENST00000307877; ENSP00000312066; ENSG00000167881. [Q9UHB9-1]
DR   Ensembl; ENST00000539137; ENSP00000446136; ENSG00000167881. [Q9UHB9-4]
DR   Ensembl; ENST00000602720; ENSP00000473613; ENSG00000167881. [Q9UHB9-3]
DR   GeneID; 6730; -.
DR   KEGG; hsa:6730; -.
DR   UCSC; uc002jqj.3; human. [Q9UHB9-1]
DR   CTD; 6730; -.
DR   DisGeNET; 6730; -.
DR   GeneCards; SRP68; -.
DR   HGNC; HGNC:11302; SRP68.
DR   HPA; ENSG00000167881; Low tissue specificity.
DR   MIM; 604858; gene.
DR   neXtProt; NX_Q9UHB9; -.
DR   OpenTargets; ENSG00000167881; -.
DR   PharmGKB; PA36126; -.
DR   VEuPathDB; HostDB:ENSG00000167881; -.
DR   eggNOG; KOG2460; Eukaryota.
DR   GeneTree; ENSGT00390000011856; -.
DR   HOGENOM; CLU_084496_0_0_1; -.
DR   InParanoid; Q9UHB9; -.
DR   OMA; DERFIHI; -.
DR   OrthoDB; 1019762at2759; -.
DR   PhylomeDB; Q9UHB9; -.
DR   TreeFam; TF105779; -.
DR   PathwayCommons; Q9UHB9; -.
DR   Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   SIGNOR; Q9UHB9; -.
DR   BioGRID-ORCS; 6730; 615 hits in 1023 CRISPR screens.
DR   ChiTaRS; SRP68; human.
DR   GenomeRNAi; 6730; -.
DR   Pharos; Q9UHB9; Tbio.
DR   PRO; PR:Q9UHB9; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9UHB9; protein.
DR   Bgee; ENSG00000167881; Expressed in gastrocnemius and 216 other tissues.
DR   ExpressionAtlas; Q9UHB9; baseline and differential.
DR   Genevisible; Q9UHB9; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR   GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; TAS:ProtInc.
DR   GO; GO:0005840; C:ribosome; TAS:ProtInc.
DR   GO; GO:0048500; C:signal recognition particle; IDA:CAFA.
DR   GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:UniProtKB.
DR   GO; GO:0008312; F:7S RNA binding; IMP:CAFA.
DR   GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0005047; F:signal recognition particle binding; IPI:UniProtKB.
DR   GO; GO:0042493; P:response to drug; IDA:UniProtKB.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR   CDD; cd15481; SRP68-RBD; 1.
DR   Gene3D; 1.10.3450.40; -; 1.
DR   InterPro; IPR026258; SRP68.
DR   InterPro; IPR034652; SRP68-RBD.
DR   InterPro; IPR038253; SRP68_N_sf.
DR   PANTHER; PTHR12860; PTHR12860; 1.
DR   Pfam; PF16969; SRP68; 1.
DR   PIRSF; PIRSF038995; SRP68; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm; Nucleus;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding;
KW   Signal recognition particle.
FT   CHAIN           1..627
FT                   /note="Signal recognition particle subunit SRP68"
FT                   /id="PRO_0000135227"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18088087"
FT   MOD_RES         241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         452
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         1..339
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045132"
FT   VAR_SEQ         84..121
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046944"
FT   VAR_SEQ         256..286
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_008347"
FT   CONFLICT        15..19
FT                   /note="Missing (in Ref. 1; AAF24308)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        27..29
FT                   /note="Missing (in Ref. 1; AAF24308)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        174
FT                   /note="E -> K (in Ref. 1; AAF24308)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        534..535
FT                   /note="DA -> ES (in Ref. 1; AAF24308)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        606
FT                   /note="K -> E (in Ref. 2; BAG54299)"
FT                   /evidence="ECO:0000305"
FT   HELIX           62..72
FT                   /evidence="ECO:0007829|PDB:4P3F"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:4P3F"
FT   HELIX           80..103
FT                   /evidence="ECO:0007829|PDB:4P3F"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:4P3F"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:4P3F"
FT   HELIX           122..143
FT                   /evidence="ECO:0007829|PDB:4P3F"
FT   TURN            145..147
FT                   /evidence="ECO:0007829|PDB:4P3E"
FT   HELIX           151..172
FT                   /evidence="ECO:0007829|PDB:4P3F"
FT   HELIX           180..200
FT                   /evidence="ECO:0007829|PDB:4P3F"
FT   HELIX           204..222
FT                   /evidence="ECO:0007829|PDB:4P3F"
FT   HELIX           227..251
FT                   /evidence="ECO:0007829|PDB:4P3F"
FT   HELIX           593..597
FT                   /evidence="ECO:0007829|PDB:5M72"
FT   HELIX           604..606
FT                   /evidence="ECO:0007829|PDB:5M72"
SQ   SEQUENCE   627 AA;  70730 MW;  6EF582892D300B2D CRC64;
     MAAEKQVPGG GGGGGSGGGG GSGGGGSGGG RGAGGEENKE NERPSAGSKA NKEFGDSLSL
     EILQIIKESQ QQHGLRHGDF QRYRGYCSRR QRRLRKTLNF KMGNRHKFTG KKVTEELLTD
     NRYLLLVLMD AERAWSYAMQ LKQEANTEPR KRFHLLSRLR KAVKHAEELE RLCESNRVDA
     KTKLEAQAYT AYLSGMLRFE HQEWKAAIEA FNKCKTIYEK LASAFTEEQA VLYNQRVEEI
     SPNIRYCAYN IGDQSAINEL MQMRLRSGGT EGLLAEKLEA LITQTRAKQA ATMSEVEWRG
     RTVPVKIDKV RIFLLGLADN EAAIVQAESE ETKERLFESM LSECRDAIQV VREELKPDQK
     QRDYILEGEP GKVSNLQYLH SYLTYIKLST AIKRNENMAK GLQRALLQQQ PEDDSKRSPR
     PQDLIRLYDI ILQNLVELLQ LPGLEEDKAF QKEIGLKTLV FKAYRCFFIA QSYVLVKKWS
     EALVLYDRVL KYANEVNSDA GAFKNSLKDL PDVQELITQV RSEKCSLQAA AILDANDAHQ
     TETSSSQVKD NKPLVERFET FCLDPSLVTK QANLVHFPPG FQPIPCKPLF FDLALNHVAF
     PPLEDKLEQK TKSGLTGYIK GIFGFRS
//
DBGET integrated database retrieval system