PCID2_HUMAN
ID PCID2_HUMAN Reviewed; 399 AA.
AC Q5JVF3; A6NK09; Q3ZCX1; Q5TC57; Q5TC58; Q9H7K1; Q9HBZ7; Q9NUK6; Q9NVY1;
AC Q9NW44; Q9NWH3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=PCI domain-containing protein 2;
DE AltName: Full=CSN12-like protein;
GN Name=PCID2; ORFNames=HT004;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Embryo, Ovary, Placenta, Spleen, and Teratocarcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RA Peng Y., Li N., Jia J., Xu S., Han Z., Fu G., Chen Z.;
RT "A novel gene expressed in human hypothalamus.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Testis;
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 [5]
RP PROTEIN SEQUENCE OF 2-20; 83-93; 117-128 AND 250-259, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V.;
RL Submitted (JAN-2010) to UniProtKB.
RN [6]
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 [7]
RP IDENTIFICATION IN THE TREX-2 COMPLEX.
RX PubMed=22307388; DOI=10.1093/nar/gks059;
RA Jani D., Lutz S., Hurt E., Laskey R.A., Stewart M., Wickramasinghe V.O.;
RT "Functional and structural characterization of the mammalian TREX-2 complex
RT that links transcription with nuclear messenger RNA export.";
RL Nucleic Acids Res. 40:4562-4573(2012).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE TREX-2 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=23591820; DOI=10.1242/jcs.118000;
RA Umlauf D., Bonnet J., Waharte F., Fournier M., Stierle M., Fischer B.,
RA Brino L., Devys D., Tora L.;
RT "The human TREX-2 complex is stably associated with the nuclear pore
RT basket.";
RL J. Cell Sci. 126:2656-2667(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, 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 [10]
RP INTERACTION WITH BRCA2.
RX PubMed=24896180; DOI=10.1038/nature13374;
RA Bhatia V., Barroso S.I., Garcia-Rubio M.L., Tumini E., Herrera-Moyano E.,
RA Aguilera A.;
RT "BRCA2 prevents R-loop accumulation and associates with TREX-2 mRNA export
RT factor PCID2.";
RL Nature 511:362-365(2014).
CC -!- FUNCTION: Required for B-cell survival through the regulation of the
CC expression of cell-cycle checkpoint MAD2L1 protein during B cell
CC differentiation (By similarity). As a component of the TREX-2 complex,
CC involved in the export of mRNAs to the cytoplasm through the nuclear
CC pores (PubMed:22307388) (Probable). Binds and stabilizes BRCA2 and is
CC thus involved in the control of R-loop-associated DNA damage and
CC transcription-associated genomic instability. R-loop accumulation does
CC not increase in PCID2-depleted cells (PubMed:24896180).
CC {ECO:0000250|UniProtKB:Q8BFV2, ECO:0000269|PubMed:22307388,
CC ECO:0000269|PubMed:24896180, ECO:0000305|PubMed:23591820}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC)-associated TREX-2
CC complex (transcription and export complex 2), composed of at least
CC GANP, 2 copies of ENY2, PCID2, SEM1/DSS1, and either centrin CETN2 or
CC centrin CETN3. The TREX-2 complex also associates with ALYREF/ALY and
CC with the nucleoporin NUP153 (PubMed:22307388, PubMed:23591820).
CC Interacts with BRCA2 (PubMed:24896180). {ECO:0000269|PubMed:22307388,
CC ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:24896180}.
CC -!- INTERACTION:
CC Q5JVF3; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-1051701, EBI-747204;
CC Q5JVF3; Q96PV6: LENG8; NbExp=3; IntAct=EBI-1051701, EBI-739546;
CC Q5JVF3; P60896: SEM1; NbExp=3; IntAct=EBI-1051701, EBI-79819;
CC Q5JVF3-1; P60896: SEM1; NbExp=3; IntAct=EBI-15970419, EBI-79819;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23591820}. Nucleus,
CC nuclear pore complex {ECO:0000269|PubMed:23591820}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5JVF3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JVF3-2; Sequence=VSP_016843;
CC Name=3;
CC IsoId=Q5JVF3-3; Sequence=VSP_016845;
CC Name=4;
CC IsoId=Q5JVF3-4; Sequence=VSP_016844;
CC -!- SIMILARITY: Belongs to the CSN12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09695.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB15768.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK000888; BAA91407.1; -; mRNA.
DR EMBL; AK001185; BAA91542.1; -; mRNA.
DR EMBL; AK001302; BAA91611.1; -; mRNA.
DR EMBL; AK002167; BAA92118.1; -; mRNA.
DR EMBL; AK023313; BAB14521.1; -; mRNA.
DR EMBL; AK024478; BAB15768.1; ALT_INIT; mRNA.
DR EMBL; AF183426; AAG09695.1; ALT_FRAME; mRNA.
DR EMBL; AL136221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016614; AAH16614.1; -; mRNA.
DR EMBL; BC031246; AAH31246.1; -; mRNA.
DR CCDS; CCDS58301.1; -. [Q5JVF3-2]
DR CCDS; CCDS58302.1; -. [Q5JVF3-4]
DR CCDS; CCDS9532.2; -. [Q5JVF3-1]
DR RefSeq; NP_001120674.1; NM_001127202.3. [Q5JVF3-1]
DR RefSeq; NP_001120675.1; NM_001127203.3. [Q5JVF3-1]
DR RefSeq; NP_001245142.1; NM_001258213.2. [Q5JVF3-2]
DR RefSeq; NP_001307584.1; NM_001320655.1. [Q5JVF3-2]
DR RefSeq; NP_001307585.1; NM_001320656.1. [Q5JVF3-4]
DR RefSeq; NP_001307586.1; NM_001320657.1.
DR RefSeq; NP_001307589.1; NM_001320660.1.
DR RefSeq; NP_060856.2; NM_018386.4. [Q5JVF3-1]
DR RefSeq; XP_016876153.1; XM_017020664.1. [Q5JVF3-2]
DR PDB; 3T5X; X-ray; 2.12 A; A=201-399.
DR PDBsum; 3T5X; -.
DR AlphaFoldDB; Q5JVF3; -.
DR SMR; Q5JVF3; -.
DR BioGRID; 120908; 64.
DR DIP; DIP-50497N; -.
DR IntAct; Q5JVF3; 25.
DR MINT; Q5JVF3; -.
DR GlyGen; Q5JVF3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5JVF3; -.
DR MetOSite; Q5JVF3; -.
DR PhosphoSitePlus; Q5JVF3; -.
DR SwissPalm; Q5JVF3; -.
DR BioMuta; PCID2; -.
DR DMDM; 85681034; -.
DR EPD; Q5JVF3; -.
DR jPOST; Q5JVF3; -.
DR MassIVE; Q5JVF3; -.
DR MaxQB; Q5JVF3; -.
DR PaxDb; Q5JVF3; -.
DR PeptideAtlas; Q5JVF3; -.
DR PRIDE; Q5JVF3; -.
DR ProteomicsDB; 63327; -. [Q5JVF3-1]
DR ProteomicsDB; 63328; -. [Q5JVF3-2]
DR ProteomicsDB; 63329; -. [Q5JVF3-3]
DR ProteomicsDB; 63330; -. [Q5JVF3-4]
DR Antibodypedia; 25858; 97 antibodies from 16 providers.
DR DNASU; 55795; -.
DR Ensembl; ENST00000246505.9; ENSP00000246505.5; ENSG00000126226.22. [Q5JVF3-4]
DR Ensembl; ENST00000337344.9; ENSP00000337405.4; ENSG00000126226.22. [Q5JVF3-1]
DR Ensembl; ENST00000375457.2; ENSP00000364606.2; ENSG00000126226.22. [Q5JVF3-2]
DR Ensembl; ENST00000375459.5; ENSP00000364608.1; ENSG00000126226.22. [Q5JVF3-2]
DR Ensembl; ENST00000375477.5; ENSP00000364626.1; ENSG00000126226.22. [Q5JVF3-1]
DR Ensembl; ENST00000375479.6; ENSP00000364628.2; ENSG00000126226.22. [Q5JVF3-1]
DR Ensembl; ENST00000622406.4; ENSP00000479494.1; ENSG00000126226.22. [Q5JVF3-4]
DR GeneID; 55795; -.
DR KEGG; hsa:55795; -.
DR MANE-Select; ENST00000337344.9; ENSP00000337405.4; NM_001127202.4; NP_001120674.1.
DR UCSC; uc058ylr.1; human. [Q5JVF3-1]
DR CTD; 55795; -.
DR DisGeNET; 55795; -.
DR GeneCards; PCID2; -.
DR HGNC; HGNC:25653; PCID2.
DR HPA; ENSG00000126226; Low tissue specificity.
DR MIM; 613713; gene.
DR neXtProt; NX_Q5JVF3; -.
DR OpenTargets; ENSG00000126226; -.
DR PharmGKB; PA144596397; -.
DR VEuPathDB; HostDB:ENSG00000126226; -.
DR GeneTree; ENSGT00390000001101; -.
DR HOGENOM; CLU_031567_2_0_1; -.
DR InParanoid; Q5JVF3; -.
DR OMA; TYLIPCH; -.
DR PhylomeDB; Q5JVF3; -.
DR TreeFam; TF106136; -.
DR PathwayCommons; Q5JVF3; -.
DR SignaLink; Q5JVF3; -.
DR BioGRID-ORCS; 55795; 755 hits in 1086 CRISPR screens.
DR ChiTaRS; PCID2; human.
DR GenomeRNAi; 55795; -.
DR Pharos; Q5JVF3; Tbio.
DR PRO; PR:Q5JVF3; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q5JVF3; protein.
DR Bgee; ENSG00000126226; Expressed in oocyte and 185 other tissues.
DR ExpressionAtlas; Q5JVF3; baseline and differential.
DR Genevisible; Q5JVF3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070390; C:transcription export complex 2; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:1905457; P:negative regulation of lymphoid progenitor cell differentiation; ISS:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1900049; P:regulation of histone exchange; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; IMP:UniProtKB.
DR GO; GO:0048536; P:spleen development; ISS:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR045114; Csn12-like.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12732; PTHR12732; 1.
DR Pfam; PF01399; PCI; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Translocation;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5"
FT CHAIN 2..399
FT /note="PCI domain-containing protein 2"
FT /id="PRO_0000121029"
FT DOMAIN 210..391
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..12
FT /note="MAHITINQYLQQ -> MRLTDVVQQL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016843"
FT VAR_SEQ 89
FT /note="Q -> QYPLSFMAAVPHRTHAVDYLGLETRKHWASCSFLQLERNDSVLEQKL
FT VSALSLGT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016844"
FT VAR_SEQ 92..114
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016845"
FT CONFLICT 74
FT /note="N -> D (in Ref. 4; AAH31246)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="I -> L (in Ref. 1; BAA91407)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="P -> L (in Ref. 2; AAG09695)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="K -> E (in Ref. 2; AAG09695)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="L -> M (in Ref. 1; BAA91407)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="F -> I (in Ref. 1; BAA91611)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="I -> T (in Ref. 1; BAA92118)"
FT /evidence="ECO:0000305"
FT HELIX 206..222
FT /evidence="ECO:0007829|PDB:3T5X"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:3T5X"
FT HELIX 245..261
FT /evidence="ECO:0007829|PDB:3T5X"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:3T5X"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:3T5X"
FT HELIX 280..288
FT /evidence="ECO:0007829|PDB:3T5X"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:3T5X"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:3T5X"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:3T5X"
FT HELIX 317..333
FT /evidence="ECO:0007829|PDB:3T5X"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:3T5X"
FT HELIX 340..349
FT /evidence="ECO:0007829|PDB:3T5X"
FT HELIX 357..369
FT /evidence="ECO:0007829|PDB:3T5X"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:3T5X"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:3T5X"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:3T5X"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:3T5X"
SQ SEQUENCE 399 AA; 46030 MW; 8D23273361F00E18 CRC64;
MAHITINQYL QQVYEAIDSR DGASCAELVS FKHPHVANPR LQMASPEEKC QQVLEPPYDE
MFAAHLRCTY AVGNHDFIEA YKCQTVIVQS FLRAFQAHKE ENWALPVMYA VALDLRVFAN
NADQQLVKKG KSKVGDMLEK AAELLMSCFR VCASDTRAGI EDSKKWGMLF LVNQLFKIYF
KINKLHLCKP LIRAIDSSNL KDDYSTAQRV TYKYYVGRKA MFDSDFKQAE EYLSFAFEHC
HRSSQKNKRM ILIYLLPVKM LLGHMPTVEL LKKYHLMQFA EVTRAVSEGN LLLLHEALAK
HEAFFIRCGI FLILEKLKII TYRNLFKKVY LLLKTHQLSL DAFLVALKFM QVEDVDIDEV
QCILANLIYM GHVKGYISHQ HQKLVVSKQN PFPPLSTVC
