SRP19_HUMAN
ID SRP19_HUMAN Reviewed; 144 AA.
AC P09132; B2R4E9; D6RCQ5; Q05D77; Q96FG6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Signal recognition particle 19 kDa protein;
DE Short=SRP19;
GN Name=SRP19;
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), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2460823; DOI=10.1093/nar/16.20.9431;
RA Lingelbach K., Zwieb C., Webb J.R., Marshallsaz C., Hoben P., Walter P.,
RA Dobberstein B.;
RT "Isolation and characterization of a cDNA clone encoding the 19 kDa protein
RT of signal recognition particle (SRP): expression and binding to 7SL RNA.";
RL Nucleic Acids Res. 16:9431-9442(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Erythroblast;
RA Gubin A.N., Lee Y.T., Bouffard G.G., Miller J.L.;
RT "Gene expression in human erythroid precursor cells.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
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] (ISOFORMS 1 AND 2), AND VARIANT
RP THR-4.
RC TISSUE=Brain, 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 SUBCELLULAR LOCATION.
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 [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH IPO5; IPO7; IPO8; KPNB1 AND
RP TNPO1.
RX PubMed=11682607; DOI=10.1242/jcs.114.19.3479;
RA Dean K.A., von Ahsen O., Goerlich D., Fried H.M.;
RT "Signal recognition particle protein 19 is imported into the nucleus by
RT importin 8 (RanBP8) and transportin.";
RL J. Cell Sci. 114:3479-3485(2001).
RN [9]
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 [10]
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).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-128.
RX PubMed=11641499; DOI=10.1126/science.1063839;
RA Wild K., Sinning I., Cusack S.;
RT "Crystal structure of an early protein-RNA assembly complex of the signal
RT recognition particle.";
RL Science 294:598-601(2001).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 14-120 IN COMPLEX WITH SRP54 AND
RP 7SL RNA.
RX PubMed=12244299; DOI=10.1038/nsb843;
RA Kuglstatter A., Oubridge C., Nagai K.;
RT "Induced structural changes of 7SL RNA during the assembly of human signal
RT recognition particle.";
RL Nat. Struct. Biol. 9:740-744(2002).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 1-120 IN COMPLEX WITH 7SL RNA.
RX PubMed=20179341; DOI=10.1107/s0907444910000879;
RA Wild K., Bange G., Bozkurt G., Segnitz B., Hendricks A., Sinning I.;
RT "Structural insights into the assembly of the human and archaeal signal
RT recognition particles.";
RL Acta Crystallogr. D 66:295-303(2010).
RN [14] {ECO:0007744|PDB:4P3E}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 1-120 IN COMPLEX WITH SRP68 AND
RP 7SL RNA.
RX PubMed=24700861; DOI=10.1126/science.1249094;
RA Grotwinkel J.T., Wild K., Segnitz B., Sinning I.;
RT "SRP RNA remodeling by SRP68 explains its role in protein translocation.";
RL Science 344:101-104(2014).
RN [15] {ECO:0007744|PDB:5M73}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 11-118 IN COMPLEX WITH SRP68;
RP SRP72 AND 7SL RNA, AND RNA BINDING.
RX PubMed=27899666; DOI=10.1093/nar/gkw1124;
RA Becker M.M., Lapouge K., Segnitz B., Wild K., Sinning I.;
RT "Structures of human SRP72 complexes provide insights into SRP RNA
RT remodeling and ribosome interaction.";
RL Nucleic Acids Res. 45:470-481(2017).
RN [16] {ECO:0007744|PDB:7NFX}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF SIGNAL RECOGNITION
RP PARTICLE IN COMPLEX WITH RIBOSOME NASCENT CHAIN COMPLEX AND THE SRP
RP RECEPTOR.
RX PubMed=34020957; DOI=10.1126/sciadv.abg0942;
RA Lee J.H., Jomaa A., Jomaa A., Chung S., Hwang Fu Y.H., Qian R., Sun X.,
RA Hsieh H.H., Chandrasekar S., Bi X., Mattei S., Boehringer D., Weiss S.,
RA Ban N., Shan S.O.;
RT "Receptor compaction and GTPase rearrangement drive SRP-mediated
RT cotranslational protein translocation into the ER.";
RL Sci. Adv. 7:942-942(2021).
CC -!- FUNCTION: Component of the signal recognition particle (SRP) complex, a
CC ribonucleoprotein complex that mediates the cotranslational targeting
CC of secretory and membrane proteins to the endoplasmic reticulum (ER)
CC (By similarity). Binds directly to 7SL RNA (By similarity). Mediates
CC binding of SRP54 to the SRP complex (By similarity).
CC {ECO:0000250|UniProtKB:J9PAS6}.
CC -!- SUBUNIT: Component of a signal recognition particle complex that
CC consists of a 7SL RNA molecule of 300 nucleotides and 6 protein
CC subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9 (PubMed:12244299,
CC PubMed:20179341). Interacts with IPO5, IPO7, IPO8, KPNB1 and TNPO1.
CC Interactions with IPO8 and TNPO1 may be involved in SRP19 import into
CC the nucleus (PubMed:11682607). {ECO:0000269|PubMed:11682607,
CC ECO:0000269|PubMed:12244299, ECO:0000269|PubMed:20179341}.
CC -!- INTERACTION:
CC P09132; Q9UHB9: SRP68; NbExp=2; IntAct=EBI-2680090, EBI-1048560;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10618370,
CC ECO:0000269|PubMed:11682607}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:10618370, ECO:0000269|PubMed:11682607}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:11682607}. Note=Although the signal
CC recognition particle complex acts in the cytoplasm, it assembles at
CC least in part in the nucleus and/or the nucleolus. SRP19 nuclear import
CC may be mediated by IPO8/Imp8 and TPNO1/Trn.
CC {ECO:0000269|PubMed:11682607}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P09132-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09132-2; Sequence=VSP_042540;
CC Name=3;
CC IsoId=P09132-3; Sequence=VSP_044524;
CC -!- SIMILARITY: Belongs to the SRP19 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; X12791; CAA31280.1; -; mRNA.
DR EMBL; BU661702; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK311803; BAG34746.1; -; mRNA.
DR EMBL; AC008536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471086; EAW48999.1; -; Genomic_DNA.
DR EMBL; CH471086; EAW49000.1; -; Genomic_DNA.
DR EMBL; BC010947; AAH10947.1; -; mRNA.
DR EMBL; BC017830; AAH17830.1; -; mRNA.
DR CCDS; CCDS4108.1; -. [P09132-1]
DR CCDS; CCDS56375.1; -. [P09132-2]
DR CCDS; CCDS56376.1; -. [P09132-3]
DR PIR; S01700; S01700.
DR RefSeq; NP_001191122.1; NM_001204193.1. [P09132-2]
DR RefSeq; NP_001191123.1; NM_001204194.1.
DR RefSeq; NP_001191125.1; NM_001204196.1. [P09132-3]
DR RefSeq; NP_003126.1; NM_003135.2. [P09132-1]
DR PDB; 1JID; X-ray; 1.80 A; A=1-120.
DR PDB; 1MFQ; X-ray; 3.10 A; B=14-120.
DR PDB; 1RY1; EM; 12.00 A; B=14-120.
DR PDB; 2J37; EM; 8.00 A; B=14-120.
DR PDB; 3KTV; X-ray; 3.80 A; B/D=1-120.
DR PDB; 4P3E; X-ray; 3.50 A; B=1-120.
DR PDB; 5M73; X-ray; 3.40 A; B/F=11-118.
DR PDB; 7NFX; EM; 3.20 A; q=1-144.
DR PDB; 7QWQ; EM; 2.83 A; q=1-144.
DR PDBsum; 1JID; -.
DR PDBsum; 1MFQ; -.
DR PDBsum; 1RY1; -.
DR PDBsum; 2J37; -.
DR PDBsum; 3KTV; -.
DR PDBsum; 4P3E; -.
DR PDBsum; 5M73; -.
DR PDBsum; 7NFX; -.
DR PDBsum; 7QWQ; -.
DR AlphaFoldDB; P09132; -.
DR SMR; P09132; -.
DR BioGRID; 112606; 82.
DR DIP; DIP-41412N; -.
DR IntAct; P09132; 25.
DR MINT; P09132; -.
DR STRING; 9606.ENSP00000424870; -.
DR ChEMBL; CHEMBL4295704; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR GlyGen; P09132; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P09132; -.
DR PhosphoSitePlus; P09132; -.
DR SwissPalm; P09132; -.
DR BioMuta; SRP19; -.
DR DMDM; 115502457; -.
DR EPD; P09132; -.
DR jPOST; P09132; -.
DR MassIVE; P09132; -.
DR MaxQB; P09132; -.
DR PaxDb; P09132; -.
DR PeptideAtlas; P09132; -.
DR PRIDE; P09132; -.
DR ProteomicsDB; 13963; -.
DR ProteomicsDB; 52203; -. [P09132-1]
DR ProteomicsDB; 52204; -. [P09132-2]
DR Antibodypedia; 13558; 180 antibodies from 30 providers.
DR DNASU; 6728; -.
DR Ensembl; ENST00000282999.7; ENSP00000282999.3; ENSG00000153037.15. [P09132-2]
DR Ensembl; ENST00000505459.6; ENSP00000424870.1; ENSG00000153037.15. [P09132-1]
DR Ensembl; ENST00000515463.1; ENSP00000425562.1; ENSG00000153037.15. [P09132-3]
DR GeneID; 6728; -.
DR KEGG; hsa:6728; -.
DR MANE-Select; ENST00000505459.6; ENSP00000424870.1; NM_003135.3; NP_003126.1.
DR UCSC; uc003kqb.3; human. [P09132-1]
DR CTD; 6728; -.
DR DisGeNET; 6728; -.
DR GeneCards; SRP19; -.
DR HGNC; HGNC:11300; SRP19.
DR HPA; ENSG00000153037; Low tissue specificity.
DR MalaCards; SRP19; -.
DR MIM; 182175; gene.
DR neXtProt; NX_P09132; -.
DR OpenTargets; ENSG00000153037; -.
DR PharmGKB; PA36124; -.
DR VEuPathDB; HostDB:ENSG00000153037; -.
DR eggNOG; KOG3198; Eukaryota.
DR GeneTree; ENSGT00390000004950; -.
DR HOGENOM; CLU_2621387_0_0_1; -.
DR InParanoid; P09132; -.
DR OMA; CVENPTH; -.
DR OrthoDB; 1552706at2759; -.
DR PhylomeDB; P09132; -.
DR TreeFam; TF106248; -.
DR PathwayCommons; P09132; -.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR SignaLink; P09132; -.
DR SIGNOR; P09132; -.
DR BioGRID-ORCS; 6728; 755 hits in 1085 CRISPR screens.
DR ChiTaRS; SRP19; human.
DR EvolutionaryTrace; P09132; -.
DR GenomeRNAi; 6728; -.
DR Pharos; P09132; Tbio.
DR PRO; PR:P09132; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P09132; protein.
DR Bgee; ENSG00000153037; Expressed in adenohypophysis and 104 other tissues.
DR ExpressionAtlas; P09132; baseline and differential.
DR Genevisible; P09132; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
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; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006613; P:cotranslational protein targeting to membrane; TAS:ProtInc.
DR GO; GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; IBA:GO_Central.
DR DisProt; DP00570; -.
DR Gene3D; 3.30.56.30; -; 1.
DR InterPro; IPR002778; Signal_recog_particle_SRP19.
DR InterPro; IPR036521; SRP19-like_sf.
DR PANTHER; PTHR17453; PTHR17453; 1.
DR Pfam; PF01922; SRP19; 1.
DR SUPFAM; SSF69695; SSF69695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..144
FT /note="Signal recognition particle 19 kDa protein"
FT /id="PRO_0000135197"
FT REGION 117..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 15..144
FT /note="FICIYPAYLNNKKTIAEGRRIPISKAVENPTATEIQDVCSAVGLNVFLEKNK
FT MYSREWNRDVQYRGRVRVQLKQEDGSLCLVQFPSRKSVMLYAAEMIPKLKTRTQKTGGA
FT DQSLQQGEGSKKGKGKKKK -> LLKILQLQRFKMYVQQLDLTYFLRKIKCTLENGIVM
FT SNTEAESGSSSNRKMGASALYSSHHVSQ (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_044524"
FT VAR_SEQ 101..144
FT /note="RKSVMLYAAEMIPKLKTRTQKTGGADQSLQQGEGSKKGKGKKKK -> HYTL
FT SLTSGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042540"
FT VARIANT 4
FT /note="A -> T (in dbSNP:rs17855423)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027800"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1JID"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:1JID"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:1JID"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:1JID"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1JID"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1JID"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:1JID"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1JID"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1JID"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1JID"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4P3E"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1MFQ"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:1JID"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1JID"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:1MFQ"
SQ SEQUENCE 144 AA; 16156 MW; E25F661972338CAE CRC64;
MACAAARSPA DQDRFICIYP AYLNNKKTIA EGRRIPISKA VENPTATEIQ DVCSAVGLNV
FLEKNKMYSR EWNRDVQYRG RVRVQLKQED GSLCLVQFPS RKSVMLYAAE MIPKLKTRTQ
KTGGADQSLQ QGEGSKKGKG KKKK
