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Database: UniProt
Entry: SMCA1_MOUSE
LinkDB: SMCA1_MOUSE
Original site: SMCA1_MOUSE 
ID   SMCA1_MOUSE             Reviewed;        1046 AA.
AC   Q6PGB8; B1AUP6; B1AUP7; Q8BSS1; Q91Y58;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 173.
DE   RecName: Full=Probable global transcription activator SNF2L1;
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P28370};
DE   AltName: Full=ATP-dependent helicase SMARCA1;
DE   AltName: Full=DNA-dependent ATPase SNF2L;
DE   AltName: Full=Nucleosome-remodeling factor subunit SNF2L;
DE   AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 1;
GN   Name=Smarca1; Synonyms=Snf2l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=11359880; DOI=10.1046/j.1471-4159.2001.00324.x;
RA   Lazzaro M.A., Picketts D.J.;
RT   "Cloning and characterization of the murine Imitation Switch (ISWI) genes:
RT   differential expression patterns suggest distinct developmental roles for
RT   Snf2h and Snf2l.";
RL   J. Neurochem. 77:1145-1156(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; 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=14609955; DOI=10.1093/emboj/cdg582;
RA   Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J.,
RA   Shiekhattar R.;
RT   "Isolation of human NURF: a regulator of Engrailed gene expression.";
RL   EMBO J. 22:6089-6100(2003).
RN   [6]
RP   INDUCTION.
RX   PubMed=16740656; DOI=10.1210/me.2005-0213;
RA   Lazzaro M.A., Pepin D., Pescador N., Murphy B.D., Vanderhyden B.C.,
RA   Picketts D.J.;
RT   "The imitation switch protein SNF2L regulates steroidogenic acute
RT   regulatory protein expression during terminal differentiation of ovarian
RT   granulosa cells.";
RL   Mol. Endocrinol. 20:2406-2417(2006).
CC   -!- FUNCTION: Helicase that possesses intrinsic ATP-dependent chromatin-
CC       remodeling activity (By similarity). ATPase activity is substrate-
CC       dependent, and is increased when nucleosomes are the substrate, but is
CC       also catalytically active when DNA alone is the substrate (By
CC       similarity). Catalytic subunit of ISWI chromatin-remodeling complexes,
CC       which form ordered nucleosome arrays on chromatin and facilitate access
CC       to DNA during DNA-templated processes such as DNA replication,
CC       transcription, and repair (By similarity). Within the ISWI chromatin-
CC       remodeling complexes, slides edge- and center-positioned histone
CC       octamers away from their original location on the DNA template (By
CC       similarity). Catalytic activity and histone octamer sliding propensity
CC       is regulated and determined by components of the ISWI chromatin-
CC       remodeling complexes (By similarity). The BAZ1A-, BAZ1B-, BAZ2A- and
CC       BAZ2B-containing ISWI chromatin-remodeling complexes regulate the
CC       spacing of nucleosomes along the chromatin and have the ability to
CC       slide mononucleosomes to the center of a DNA template (By similarity).
CC       The CECR2- and RSF1-containing ISWI chromatin-remodeling complexes do
CC       not have the ability to slide mononucleosomes to the center of a DNA
CC       template (By similarity). Within the NURF-1 and CERF-1 ISWI chromatin
CC       remodeling complexes, nucleosomes are the preferred substrate for its
CC       ATPase activity (By similarity). Within the NURF-1 ISWI chromatin-
CC       remodeling complex, binds to the promoters of En1 and En2 to positively
CC       regulate their expression and promote brain development (By
CC       similarity). May promote neurite outgrowth (By similarity). May be
CC       involved in the development of luteal cells (By similarity).
CC       {ECO:0000250|UniProtKB:P28370}.
CC   -!- SUBUNIT: May form homodimers (By similarity). Component of the ACF-1
CC       ISWI chromatin remodeling complex at least composed of SMARCA1 and
CC       BAZ1A, which regulates the spacing of histone octamers on the DNA
CC       template to facilitate access to DNA (By similarity). Within the
CC       complex interacts with BAZ1A; the interaction is direct (By
CC       similarity). Component of the WICH-1 ISWI chromatin remodeling complex
CC       at least composed of SMARCA1 and BAZ1B/WSTF (By similarity). Within the
CC       complex interacts with BAZ1B/WSTF (By similarity). Component of the
CC       NoRC-1 ISWI chromatin remodeling complex at least composed of SMARCA1
CC       and BAZ2A/TIP5 (By similarity). Within the complex interacts with
CC       BAZ2A/TIP5 (By similarity). Component of the BRF-1 ISWI chromatin
CC       remodeling complex at least composed of SMARCA1 and BAZ2B (By
CC       similarity). Within the complex interacts with BAZ2B (By similarity).
CC       Component of the NURF-1 ISWI chromatin remodeling complex (also called
CC       the nucleosome-remodeling factor (NURF) complex) at least composed of
CC       SMARCA1, BPTF, RBBP4 and RBBP7 (By similarity). Within the complex
CC       interacts with BPTF (By similarity). Within the complex interacts with
CC       RBBP4 and RBBP7 (By similarity). Component of the CERF-1 ISWI chromatin
CC       remodeling complex (also called the CECR2-containing-remodeling factor
CC       (CERF) complex) at least composed of CECR2 and SMARCA1 (By similarity).
CC       Within the complex interacts with CECR2 (By similarity). Component of
CC       the RSF-1 ISWI chromatin remodeling complex at least composed of
CC       SMARCA1 and RSF1 (By similarity). Within the complex interacts with
CC       RSF1 (By similarity). Interacts with PRLR (By similarity). Interacts
CC       with ERCC6 (By similarity). {ECO:0000250|UniProtKB:P28370}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PGB8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PGB8-2; Sequence=VSP_020378;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in cortex, cerebellum,
CC       ovaries, testes, uterus and placenta. {ECO:0000269|PubMed:11359880,
CC       ECO:0000269|PubMed:14609955}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout the embryo at 9.5 dpc-15.5
CC       dpc. Brain expression increases during the first two weeks of postnatal
CC       development. {ECO:0000269|PubMed:11359880}.
CC   -!- INDUCTION: By ovulation in ovaries (at protein level).
CC       {ECO:0000269|PubMed:16740656}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK52453.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF325920; AAK52453.1; ALT_FRAME; mRNA.
DR   EMBL; AK030741; BAC27109.1; -; mRNA.
DR   EMBL; AL671903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC057115; AAH57115.1; -; mRNA.
DR   CCDS; CCDS30104.1; -. [Q6PGB8-1]
DR   CCDS; CCDS72374.1; -. [Q6PGB8-2]
DR   RefSeq; NP_001277637.1; NM_001290708.1. [Q6PGB8-2]
DR   RefSeq; NP_444353.3; NM_053123.4. [Q6PGB8-1]
DR   AlphaFoldDB; Q6PGB8; -.
DR   SMR; Q6PGB8; -.
DR   BioGRID; 220299; 7.
DR   ComplexPortal; CPX-454; CERF chromatin remodelling complex.
DR   ComplexPortal; CPX-694; NuRF chromatin remodeling complex.
DR   IntAct; Q6PGB8; 1.
DR   STRING; 10090.ENSMUSP00000099138; -.
DR   iPTMnet; Q6PGB8; -.
DR   PhosphoSitePlus; Q6PGB8; -.
DR   EPD; Q6PGB8; -.
DR   MaxQB; Q6PGB8; -.
DR   PaxDb; 10090-ENSMUSP00000086366; -.
DR   ProteomicsDB; 261430; -. [Q6PGB8-1]
DR   ProteomicsDB; 261431; -. [Q6PGB8-2]
DR   Pumba; Q6PGB8; -.
DR   Antibodypedia; 518; 241 antibodies from 27 providers.
DR   DNASU; 93761; -.
DR   Ensembl; ENSMUST00000077569.11; ENSMUSP00000076769.5; ENSMUSG00000031099.17. [Q6PGB8-1]
DR   Ensembl; ENSMUST00000088973.11; ENSMUSP00000086366.5; ENSMUSG00000031099.17. [Q6PGB8-1]
DR   Ensembl; ENSMUST00000101616.9; ENSMUSP00000099138.3; ENSMUSG00000031099.17. [Q6PGB8-2]
DR   GeneID; 93761; -.
DR   KEGG; mmu:93761; -.
DR   UCSC; uc009tbl.2; mouse. [Q6PGB8-1]
DR   UCSC; uc009tbm.2; mouse. [Q6PGB8-2]
DR   AGR; MGI:1935127; -.
DR   CTD; 6594; -.
DR   MGI; MGI:1935127; Smarca1.
DR   VEuPathDB; HostDB:ENSMUSG00000031099; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   GeneTree; ENSGT00940000157297; -.
DR   InParanoid; Q6PGB8; -.
DR   OMA; VHDYQFF; -.
DR   OrthoDB; 5482994at2759; -.
DR   PhylomeDB; Q6PGB8; -.
DR   TreeFam; TF300674; -.
DR   BRENDA; 2.7.11.17; 3474.
DR   BioGRID-ORCS; 93761; 2 hits in 83 CRISPR screens.
DR   ChiTaRS; Smarca1; mouse.
DR   PRO; PR:Q6PGB8; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q6PGB8; Protein.
DR   Bgee; ENSMUSG00000031099; Expressed in gonadal ridge and 229 other cell types or tissues.
DR   ExpressionAtlas; Q6PGB8; baseline and differential.
DR   Genevisible; Q6PGB8; MM.
DR   GO; GO:1904949; C:ATPase complex; ISO:MGI.
DR   GO; GO:0090537; C:CERF complex; ISO:MGI.
DR   GO; GO:0000785; C:chromatin; IDA:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0016589; C:NURF complex; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; ISO:MGI.
DR   GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; ISS:HGNC.
DR   GO; GO:0030182; P:neuron differentiation; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:HGNC.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:HGNC.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:2000177; P:regulation of neural precursor cell proliferation; IMP:MGI.
DR   CDD; cd18065; DEXHc_SMARCA1; 1.
DR   CDD; cd00167; SANT; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 1.20.5.1190; iswi atpase; 1.
DR   Gene3D; 1.10.1040.30; ISWI, HAND domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR015194; ISWI_HAND-dom.
DR   InterPro; IPR036306; ISWI_HAND-dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR015195; SLIDE.
DR   InterPro; IPR044755; SMARCA1_N.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; ISW-1; 1.
DR   Pfam; PF09110; HAND; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF09111; SLIDE; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; ATP-binding; Chromatin regulator;
KW   Coiled coil; DNA-binding; Helicase; Hydrolase; Isopeptide bond;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..1046
FT                   /note="Probable global transcription activator SNF2L1"
FT                   /id="PRO_0000249246"
FT   DOMAIN          199..364
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          494..645
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          847..899
FT                   /note="SANT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   DOMAIN          950..1014
FT                   /note="SANT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   REGION          27..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          819..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1025..1046
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1003..1037
FT                   /evidence="ECO:0000255"
FT   MOTIF           315..318
FT                   /note="DEAH box"
FT   BINDING         212..219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P28370"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P28370"
FT   MOD_RES         946
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P28370"
FT   CROSSLNK        654
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P28370"
FT   CROSSLNK        720
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P28370"
FT   CROSSLNK        742
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P28370"
FT   VAR_SEQ         1040..1046
FT                   /note="VKFSAFS -> SQKRKAESATESSGRKDVKKVKS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11359880"
FT                   /id="VSP_020378"
FT   CONFLICT        53
FT                   /note="G -> A (in Ref. 1; AAK52453 and 2; BAC27109)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94
FT                   /note="D -> A (in Ref. 1; AAK52453)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        459
FT                   /note="Q -> H (in Ref. 2; BAC27109)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1046 AA;  121715 MW;  11D60F70FE466FC5 CRC64;
     MEPDTATEAA TVAVSDARAT VVVVEDEQPG PSTFKEEGAA AAATEGTTAT EKGEKKEKIT
     SPFQLKLAAK ASKSEKEMDP EYEEKMVNMP LKADRAKRFE FLLKQTELFA HFIQPSAQKS
     PTSPLNMKLA RPRVKKDDKQ SLISVGDYRH RRTEQEEDEE LLSESRKTSN VCVRFEVSPS
     YVKGGPLRDY QIRGLNWLIS LYENGVNGIL ADEMGLGKTL QTIALLGYLK HYRNIPGPHM
     VLVPKSTLHN WMNEFKRWVP SLRVICFVGD KDVRAAFIRD EMMPGEWDVC VTSYEMVIKE
     KSVFKKFHWR YLVIDEAHRI KNEKSKLSEI VREFKSTNRL LLTGTPLQNN LHELWALLNF
     LLPDVFNSAD DFDSWFDTKN CLGDQKLVER LHAVLKPFLL RRIKTDVEKS LPPKKEIKIY
     LGLSKMQREW YTKILMKDID VLNSSGKMDK MRLLNILMQL RKCCNHPYLF DGAEPGPPYT
     TDEHIVGNSG KMVALDKLLA RIKEQGSRVL IFSQMTRLLD ILEDYCMWRG YEYSRLDGQT
     PHEEREEAID AFNAPNSSKF IFMLSTRAGG LGINLASADV VILYDSDWNP QVDLQAMDRA
     HRIGQKKPVR VFRLITDNTV EERIVERAEI KLRLDSIVIQ QGRLIDQQSN KLAKEEMLQM
     IRHGATHVFA CKESELTDED IVTILERGEK KTAEMNERMQ KMGESSLRNF RMDLEQSLYK
     FEGEDYREKQ KLGTVEWIEP PKRERKANYA VDAYFREALR VSEPKIPKAP RPPKQPNVQD
     FQFFPPRLFE LLEKEILYYR KTIGYKVPRN PEIPNPAIAQ REEQKKIDGA EPLTPQETEE
     KDKLLTQGFT NWTKRDFNQF IKANEKYGRD DIDNIAREVE GKSPEEVMEY SAVFWERCNE
     LQDIEKIMAQ IERGEARIQR RISIKKALDA KIARYKAPFH QLRIQYGTSK GKNYTEEEDR
     FLICMLHKMG FDRENVYEEL RQCVRNAPQF RFDWFIKSRT AMEFQRRCNT LISLIEKENM
     EIEERERAEK KKRATKTPMV KFSAFS
//
DBGET integrated database retrieval system