PRDM5_HUMAN
ID PRDM5_HUMAN Reviewed; 630 AA.
AC Q9NQX1; Q0VAI9; Q0VAJ0; Q6NXQ7;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=PR domain zinc finger protein 5;
DE EC=2.1.1.-;
DE AltName: Full=PR domain-containing protein 5;
GN Name=PRDM5; Synonyms=PFM2;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=15077163; DOI=10.1038/sj.onc.1207615;
RA Deng Q., Huang S.;
RT "PRDM5 is silenced in human cancers and has growth suppressive
RT activities.";
RL Oncogene 23:4903-4910(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Brain;
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 TISSUE SPECIFICITY.
RX PubMed=17699856; DOI=10.1158/1078-0432.ccr-07-0305;
RA Watanabe Y., Toyota M., Kondo Y., Suzuki H., Imai T., Ohe-Toyota M.,
RA Maruyama R., Nojima M., Sasaki Y., Sekido Y., Hiratsuka H., Shinomura Y.,
RA Imai K., Itoh F., Tokino T.;
RT "PRDM5 identified as a target of epigenetic silencing in colorectal and
RT gastric cancer.";
RL Clin. Cancer Res. 13:4786-4794(2007).
RN [6]
RP FUNCTION, INTERACTION WITH EHMT2; GFI1 AND HDAC1, AND SUBCELLULAR LOCATION.
RX PubMed=17636019; DOI=10.1128/mcb.00762-07;
RA Duan Z., Person R.E., Lee H.-H., Huang S., Donadieu J., Badolato R.,
RA Grimes H.L., Papayannopoulou T., Horwitz M.S.;
RT "Epigenetic regulation of protein-coding and microRNA genes by the Gfi1-
RT interacting tumor suppressor PRDM5.";
RL Mol. Cell. Biol. 27:6889-6902(2007).
RN [7]
RP VARIANT BCS2 CYS-107, AND FUNCTION.
RX PubMed=21664999; DOI=10.1016/j.ajhg.2011.05.007;
RA Burkitt Wright E.M., Spencer H.L., Daly S.B., Manson F.D., Zeef L.A.,
RA Urquhart J., Zoppi N., Bonshek R., Tosounidis I., Mohan M., Madden C.,
RA Dodds A., Chandler K.E., Banka S., Au L., Clayton-Smith J., Khan N.,
RA Biesecker L.G., Wilson M., Rohrbach M., Colombi M., Giunta C., Black G.C.;
RT "Mutations in PRDM5 in brittle cornea syndrome identify a pathway
RT regulating extracellular matrix development and maintenance.";
RL Am. J. Hum. Genet. 88:767-777(2011).
CC -!- FUNCTION: Sequence-specific DNA-binding transcription factor. Represses
CC transcription at least in part by recruitment of the histone
CC methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1.
CC Regulates hematopoiesis-associated protein-coding and microRNA (miRNA)
CC genes. May regulate the expression of proteins involved in
CC extracellular matrix development and maintenance, including fibrillar
CC collagens, such as COL4A1 and COL11A1, connective tissue components,
CC such as HAPLN1, and molecules regulating cell migration and adhesion,
CC including EDIL3 and TGFB2. May cause G2/M arrest and apoptosis in
CC cancer cells. {ECO:0000269|PubMed:15077163,
CC ECO:0000269|PubMed:17636019, ECO:0000269|PubMed:21664999}.
CC -!- SUBUNIT: Interacts with EHMT2/G9A, GFI1 and HDAC1.
CC {ECO:0000269|PubMed:17636019}.
CC -!- INTERACTION:
CC Q9NQX1; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-4292031, EBI-744366;
CC Q9NQX1; Q99684: GFI1; NbExp=2; IntAct=EBI-4292031, EBI-949368;
CC Q9NQX1; Q13547: HDAC1; NbExp=3; IntAct=EBI-4292031, EBI-301834;
CC Q9NQX1-2; Q9NX46: ADPRS; NbExp=3; IntAct=EBI-12859340, EBI-718580;
CC Q9NQX1-2; P35523: CLCN1; NbExp=3; IntAct=EBI-12859340, EBI-10206780;
CC Q9NQX1-2; Q6NZ36-4: FAAP20; NbExp=3; IntAct=EBI-12859340, EBI-12013806;
CC Q9NQX1-2; Q9H4M3-2: FBXO44; NbExp=3; IntAct=EBI-12859340, EBI-12104696;
CC Q9NQX1-2; Q9Y272: RASD1; NbExp=3; IntAct=EBI-12859340, EBI-740818;
CC Q9NQX1-2; P29597: TYK2; NbExp=3; IntAct=EBI-12859340, EBI-1383454;
CC Q9NQX1-2; P32241: VIPR1; NbExp=3; IntAct=EBI-12859340, EBI-3917984;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15077163,
CC ECO:0000269|PubMed:17636019}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NQX1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQX1-2; Sequence=VSP_035654;
CC Name=3;
CC IsoId=Q9NQX1-3; Sequence=VSP_035652, VSP_035653;
CC Name=4;
CC IsoId=Q9NQX1-4; Sequence=VSP_035654, VSP_054395, VSP_054396;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in colon and
CC ovary. Tends to be silenced in breast, colorectal, gastric and liver
CC cancer tissues. {ECO:0000269|PubMed:15077163,
CC ECO:0000269|PubMed:17699856}.
CC -!- DISEASE: Brittle cornea syndrome 2 (BCS2) [MIM:614170]: A disorder
CC characterized by extreme corneal thinning resulting in corneal rupture
CC after minor trauma, blue sclerae, keratoconus or keratoglobus,
CC hyperelasticity of the skin, and hypermobile joints.
CC {ECO:0000269|PubMed:21664999}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AF272897; AAF78077.1; -; mRNA.
DR EMBL; AK056352; BAG51686.1; -; mRNA.
DR EMBL; AC025741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066942; AAH66942.1; -; mRNA.
DR EMBL; BC121037; AAI21038.1; -; mRNA.
DR EMBL; BC121038; AAI21039.1; -; mRNA.
DR CCDS; CCDS3716.1; -. [Q9NQX1-1]
DR CCDS; CCDS75187.1; -. [Q9NQX1-4]
DR CCDS; CCDS75188.1; -. [Q9NQX1-2]
DR RefSeq; NP_001287752.1; NM_001300823.1. [Q9NQX1-2]
DR RefSeq; NP_001287753.1; NM_001300824.1. [Q9NQX1-4]
DR RefSeq; NP_061169.2; NM_018699.3. [Q9NQX1-1]
DR PDB; 6XAZ; X-ray; 1.70 A; A/B=1-127.
DR PDBsum; 6XAZ; -.
DR AlphaFoldDB; Q9NQX1; -.
DR SMR; Q9NQX1; -.
DR BioGRID; 116287; 57.
DR IntAct; Q9NQX1; 49.
DR MINT; Q9NQX1; -.
DR STRING; 9606.ENSP00000264808; -.
DR MoonDB; Q9NQX1; Predicted.
DR GlyGen; Q9NQX1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NQX1; -.
DR PhosphoSitePlus; Q9NQX1; -.
DR SwissPalm; Q9NQX1; -.
DR BioMuta; PRDM5; -.
DR DMDM; 212276458; -.
DR MassIVE; Q9NQX1; -.
DR PaxDb; Q9NQX1; -.
DR PeptideAtlas; Q9NQX1; -.
DR PRIDE; Q9NQX1; -.
DR ProteomicsDB; 58796; -.
DR ProteomicsDB; 82218; -. [Q9NQX1-1]
DR ProteomicsDB; 82219; -. [Q9NQX1-2]
DR ProteomicsDB; 82220; -. [Q9NQX1-3]
DR Antibodypedia; 26690; 252 antibodies from 29 providers.
DR DNASU; 11107; -.
DR Ensembl; ENST00000264808.8; ENSP00000264808.3; ENSG00000138738.11. [Q9NQX1-1]
DR Ensembl; ENST00000394435.2; ENSP00000377955.2; ENSG00000138738.11. [Q9NQX1-3]
DR Ensembl; ENST00000428209.6; ENSP00000404832.2; ENSG00000138738.11. [Q9NQX1-2]
DR Ensembl; ENST00000515109.5; ENSP00000422309.1; ENSG00000138738.11. [Q9NQX1-4]
DR GeneID; 11107; -.
DR KEGG; hsa:11107; -.
DR MANE-Select; ENST00000264808.8; ENSP00000264808.3; NM_018699.4; NP_061169.2.
DR UCSC; uc003idn.4; human. [Q9NQX1-1]
DR CTD; 11107; -.
DR DisGeNET; 11107; -.
DR GeneCards; PRDM5; -.
DR HGNC; HGNC:9349; PRDM5.
DR HPA; ENSG00000138738; Low tissue specificity.
DR MalaCards; PRDM5; -.
DR MIM; 614161; gene.
DR MIM; 614170; phenotype.
DR neXtProt; NX_Q9NQX1; -.
DR OpenTargets; ENSG00000138738; -.
DR Orphanet; 90354; Brittle cornea syndrome.
DR PharmGKB; PA33717; -.
DR VEuPathDB; HostDB:ENSG00000138738; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG2461; Eukaryota.
DR GeneTree; ENSGT00940000158340; -.
DR HOGENOM; CLU_002678_75_0_1; -.
DR InParanoid; Q9NQX1; -.
DR OMA; IRTHTRX; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9NQX1; -.
DR TreeFam; TF106478; -.
DR PathwayCommons; Q9NQX1; -.
DR SignaLink; Q9NQX1; -.
DR BioGRID-ORCS; 11107; 6 hits in 1097 CRISPR screens.
DR ChiTaRS; PRDM5; human.
DR GenomeRNAi; 11107; -.
DR Pharos; Q9NQX1; Tbio.
DR PRO; PR:Q9NQX1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9NQX1; protein.
DR Bgee; ENSG00000138738; Expressed in calcaneal tendon and 126 other tissues.
DR ExpressionAtlas; Q9NQX1; baseline and differential.
DR Genevisible; Q9NQX1; HS.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IMP:UniProtKB.
DR GO; GO:0051567; P:histone H3-K9 methylation; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:ARUK-UCL.
DR GO; GO:1903053; P:regulation of extracellular matrix organization; IMP:ARUK-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd19190; PR-SET_PRDM5; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044415; PRDM5_PR-SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR017125; Znf_PRDM5-like.
DR Pfam; PF00096; zf-C2H2; 10.
DR PIRSF; PIRSF037162; PRDM; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 16.
DR SUPFAM; SSF57667; SSF57667; 8.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Chromatin regulator;
KW Disease variant; DNA-binding; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..630
FT /note="PR domain zinc finger protein 5"
FT /id="PRO_0000047761"
FT DOMAIN 8..124
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 167..190
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 199..221
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 234..256
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 262..287
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 295..317
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 320..342
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 348..370
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 376..398
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 404..426
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 432..455
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 461..483
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 489..511
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 517..539
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 545..567
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 573..595
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 602..625
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VAR_SEQ 101..111
FT /note="EGENIFYLAVE -> DKNLGPAEWRG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035652"
FT VAR_SEQ 112..630
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035653"
FT VAR_SEQ 218..248
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035654"
FT VAR_SEQ 515..532
FT /note="RPYQCPYCEKGFSKNDGL -> AVQVLRVQQGLQPEARPG (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054395"
FT VAR_SEQ 533..630
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054396"
FT VARIANT 107
FT /note="Y -> C (in BCS2; dbSNP:rs387907111)"
FT /evidence="ECO:0000269|PubMed:21664999"
FT /id="VAR_066393"
FT CONFLICT 261
FT /note="R -> K (in Ref. 1; AAF78077)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6XAZ"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:6XAZ"
FT STRAND 16..27
FT /evidence="ECO:0007829|PDB:6XAZ"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6XAZ"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:6XAZ"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:6XAZ"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6XAZ"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:6XAZ"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:6XAZ"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:6XAZ"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:6XAZ"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6XAZ"
SQ SEQUENCE 630 AA; 73090 MW; D16AF81AB5A34398 CRC64;
MLGMYVPDRF SLKSSRVQDG MGLYTARRVR KGEKFGPFAG EKRMPEDLDE NMDYRLMWEV
RGSKGEVLYI LDATNPRHSN WLRFVHEAPS QEQKNLAAIQ EGENIFYLAV EDIETDTELL
IGYLDSDMEA EEEEQQIMTV IKEGEVENSR RQSTAGRKDR LGCKEDYACP QCESSFTSED
ILAEHLQTLH QKPTEEKEFK CKNCGKKFPV KQALQRHVLQ CTAKSSLKES SRSFQCSVCN
SSFSSASSFE QHQETCRGDA RFVCKADSCG KRLKSKDALK RHQENVHTGD PKKKLICSVC
NKKCSSASSL QEHRKIHEIF DCQECMKKFI SANQLKRHMI THSEKRPYNC EICNKSFKRL
DQVGAHKVIH SEDKPYKCKL CGKGFAHRNV YKNHKKTHSE ERPFQCEECK ALFRTPFSLQ
RHLLIHNSER TFKCHHCDAT FKRKDTLNVH VQVVHERHKK YRCELCNKAF VTPSVLRSHK
KTHTGEKEKI CPYCGQKFAS SGTLRVHIRS HTGERPYQCP YCEKGFSKND GLKMHIRTHT
REKPYKCSEC SKAFSQKRGL DEHKRTHTGE KPFQCDVCDL AFSLKKMLIR HKMTHNPNRP
LAECQFCHKK FTRNDYLKVH MDNIHGVADS
