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   27-MAR-2024, entry version 165.
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). Binds and stabilizes BRCA2 and is thus
CC       involved in the control of R-loop-associated DNA damage and
CC       transcription-associated genomic instability (PubMed:24896180). Blocks
CC       the activity of the SRCAP chromatin remodeling complex by interacting
CC       with SRCAP complex member ZNHIT1 and inhibiting its interaction with
CC       the complex (By similarity). This prevents the deposition of histone
CC       variant H2AZ1/H2A.Z at the nucleosomes of key lymphoid fate regulator
CC       genes which suppresses their expression and restricts lymphoid lineage
CC       commitment (By similarity). {ECO:0000250|UniProtKB:Q8BFV2,
CC       ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:24896180,
CC       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). Interacts with SRCAP chromatin
CC       remodeling complex component ZNHIT1; the interaction results in
CC       inhibition of SRCAP complex activity, preventing the deposition of
CC       histone variant H2AZ1/H2A.Z to lymphoid fate regulator genes and
CC       restricting lymphoid lineage commitment (By similarity).
CC       {ECO:0000250|UniProtKB:Q8BFV2, 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};
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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.
DR   PDB; 3T5X; X-ray; 2.12 A; A=201-399.
DR   PDBsum; 3T5X; -.
DR   AlphaFoldDB; Q5JVF3; -.
DR   SMR; Q5JVF3; -.
DR   BioGRID; 120908; 81.
DR   ComplexPortal; CPX-2477; TREX-2 transcription-export complex, CETN2 variant.
DR   ComplexPortal; CPX-7281; TREX-2 transcription-export complex, CETN3 variant.
DR   DIP; DIP-50497N; -.
DR   IntAct; Q5JVF3; 28.
DR   MINT; Q5JVF3; -.
DR   STRING; 9606.ENSP00000479494; -.
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   PeptideAtlas; Q5JVF3; -.
DR   ProteomicsDB; 63327; -. [Q5JVF3-1]
DR   ProteomicsDB; 63328; -. [Q5JVF3-2]
DR   ProteomicsDB; 63329; -. [Q5JVF3-3]
DR   ProteomicsDB; 63330; -. [Q5JVF3-4]
DR   Pumba; Q5JVF3; -.
DR   Antibodypedia; 25858; 116 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   AGR; HGNC:25653; -.
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; INRMFTL; -.
DR   OrthoDB; 1491at2759; -.
DR   PhylomeDB; Q5JVF3; -.
DR   TreeFam; TF106136; -.
DR   PathwayCommons; Q5JVF3; -.
DR   SignaLink; Q5JVF3; -.
DR   BioGRID-ORCS; 55795; 791 hits in 1167 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 187 other cell types or tissues.
DR   ExpressionAtlas; Q5JVF3; baseline and differential.
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:0070828; P:heterochromatin organization; ISS:UniProtKB.
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:0060633; P:negative regulation of transcription initiation by RNA polymerase II; 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:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB.
DR   GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; 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:0043488; P:regulation of mRNA stability; IMP:UniProtKB.
DR   GO; GO:0048536; P:spleen development; ISS:UniProtKB.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR045114; Csn12-like.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR12732:SF0; PCI DOMAIN-CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR12732; UNCHARACTERIZED PROTEASOME COMPONENT REGION PCI-CONTAINING; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00753; PAM; 1.
DR   PROSITE; PS50250; PCI; 1.
DR   Genevisible; Q5JVF3; HS.
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
//