SALL4_MOUSE
ID SALL4_MOUSE Reviewed; 1067 AA.
AC Q8BX22; A2AV00; Q6S7E8; Q6S7E9; Q7TST6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Sal-like protein 4;
DE AltName: Full=Zinc finger protein SALL4;
GN Name=Sall4;
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] (ISOFORMS 1; 2 AND 3).
RA Ma Y., Di C., Kang Q., Lai R., Theus J., Chai L.;
RT "Characterization of the murine Okihiro syndrome gene (Sall4): sequence,
RT expression and alternative splicing.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 324-958.
RC STRAIN=129/Sv;
RA Kohlhase J., Kispert A., Heinrich M.;
RT "Cloning and expression of Sall4.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH NANOG.
RX PubMed=16840789; DOI=10.1074/jbc.c600122200;
RA Wu Q., Chen X., Zhang J., Loh Y.-H., Low T.-Y., Zhang W., Zhang W.,
RA Sze S.-K., Lim B., Ng H.-H.;
RT "Sall4 interacts with Nanog and co-occupies Nanog genomic sites in
RT embryonic stem cells.";
RL J. Biol. Chem. 281:24090-24094(2006).
RN [7]
RP DOMAIN.
RX PubMed=16545361; DOI=10.1016/j.ydbio.2006.02.009;
RA Sweetman D., Muensterberg A.;
RT "The vertebrate spalt genes in development and disease.";
RL Dev. Biol. 293:285-293(2006).
RN [8]
RP INTERACTION WITH NSD2, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19483677; DOI=10.1038/nature08086;
RA Nimura K., Ura K., Shiratori H., Ikawa M., Okabe M., Schwartz R.J.,
RA Kaneda Y.;
RT "A histone H3 lysine 36 trimethyltransferase links Nkx2-5 to Wolf-
RT Hirschhorn syndrome.";
RL Nature 460:287-291(2009).
CC -!- FUNCTION: Transcription factor with a key role in the maintenance and
CC self-renewal of embryonic and hematopoietic stem cells. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with POU5F1/OCT4 (By similarity). Interacts with
CC NANOG (PubMed:16840789). Interacts with BEND3 (By similarity).
CC Interacts with NSD2 (via PHD-type zinc fingers 1, 2 and 3)
CC (PubMed:19483677). {ECO:0000250|UniProtKB:Q9UJQ4,
CC ECO:0000269|PubMed:16840789, ECO:0000269|PubMed:19483677}.
CC -!- INTERACTION:
CC Q8BX22; Q9R190: Mta2; NbExp=3; IntAct=EBI-2312582, EBI-904134;
CC Q8BX22; Q7TSZ8: Nacc1; NbExp=4; IntAct=EBI-2312582, EBI-5691985;
CC Q8BX22; Q8BVE8-2: Nsd2; NbExp=3; IntAct=EBI-2312582, EBI-11518042;
CC Q8BX22; O70230: Znf143; NbExp=2; IntAct=EBI-2312582, EBI-5691478;
CC Q8BX22; Q9UHY1: NRBP1; Xeno; NbExp=2; IntAct=EBI-2312582, EBI-749731;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:19483677}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Sall4a;
CC IsoId=Q8BX22-1; Sequence=Displayed;
CC Name=2; Synonyms=Sall4b;
CC IsoId=Q8BX22-2; Sequence=VSP_021687;
CC Name=3; Synonyms=Sall4c;
CC IsoId=Q8BX22-3; Sequence=VSP_021686;
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryonic heart (at protein
CC level). {ECO:0000269|PubMed:19483677}.
CC -!- PTM: Sumoylation with both SUMO1 and SUMO2 regulates the stability,
CC subcellular localization, transcriptional activity, and may reduce
CC interaction with POU5F1/OCT4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sal C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AY463371; AAR91796.1; -; mRNA.
DR EMBL; AY463372; AAR91797.1; -; mRNA.
DR EMBL; AY463373; AAR91798.1; -; mRNA.
DR EMBL; AK049188; BAC33598.1; -; mRNA.
DR EMBL; AL929248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466551; EDL06559.1; -; Genomic_DNA.
DR EMBL; AJ488904; CAD32912.1; -; Genomic_DNA.
DR CCDS; CCDS17115.1; -. [Q8BX22-1]
DR CCDS; CCDS17116.1; -. [Q8BX22-2]
DR CCDS; CCDS17117.1; -. [Q8BX22-3]
DR RefSeq; NP_780512.2; NM_175303.4. [Q8BX22-1]
DR RefSeq; NP_958797.2; NM_201395.3. [Q8BX22-2]
DR RefSeq; NP_958798.2; NM_201396.3. [Q8BX22-3]
DR AlphaFoldDB; Q8BX22; -.
DR BioGRID; 221236; 72.
DR DIP; DIP-29926N; -.
DR IntAct; Q8BX22; 46.
DR MINT; Q8BX22; -.
DR STRING; 10090.ENSMUSP00000029061; -.
DR iPTMnet; Q8BX22; -.
DR PhosphoSitePlus; Q8BX22; -.
DR MaxQB; Q8BX22; -.
DR PaxDb; Q8BX22; -.
DR PeptideAtlas; Q8BX22; -.
DR PRIDE; Q8BX22; -.
DR ProteomicsDB; 256691; -. [Q8BX22-1]
DR ProteomicsDB; 256692; -. [Q8BX22-2]
DR ProteomicsDB; 256693; -. [Q8BX22-3]
DR Antibodypedia; 13868; 302 antibodies from 41 providers.
DR DNASU; 99377; -.
DR Ensembl; ENSMUST00000029061; ENSMUSP00000029061; ENSMUSG00000027547. [Q8BX22-1]
DR Ensembl; ENSMUST00000075044; ENSMUSP00000074556; ENSMUSG00000027547. [Q8BX22-3]
DR Ensembl; ENSMUST00000103074; ENSMUSP00000099363; ENSMUSG00000027547. [Q8BX22-2]
DR GeneID; 99377; -.
DR KEGG; mmu:99377; -.
DR UCSC; uc008obf.1; mouse. [Q8BX22-1]
DR UCSC; uc008obg.1; mouse. [Q8BX22-2]
DR UCSC; uc008obh.1; mouse. [Q8BX22-3]
DR CTD; 57167; -.
DR MGI; MGI:2139360; Sall4.
DR VEuPathDB; HostDB:ENSMUSG00000027547; -.
DR eggNOG; KOG1074; Eukaryota.
DR GeneTree; ENSGT00940000155384; -.
DR HOGENOM; CLU_087959_0_0_1; -.
DR InParanoid; Q8BX22; -.
DR OMA; YGRSSIH; -.
DR PhylomeDB; Q8BX22; -.
DR TreeFam; TF317003; -.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR BioGRID-ORCS; 99377; 4 hits in 59 CRISPR screens.
DR PRO; PR:Q8BX22; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BX22; protein.
DR Bgee; ENSMUSG00000027547; Expressed in primitive streak and 120 other tissues.
DR ExpressionAtlas; Q8BX22; baseline and differential.
DR Genevisible; Q8BX22; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000792; C:heterochromatin; 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:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IC:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0021915; P:neural tube development; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0009888; P:tissue development; IMP:MGI.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Oncogene; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1067
FT /note="Sal-like protein 4"
FT /id="PRO_0000261416"
FT ZN_FING 68..90
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT ECO:0000303|PubMed:16545361"
FT ZN_FING 387..409
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 415..437
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 573..595
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 601..623
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 633..655
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 880..902
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 908..930
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT MOD_RES 798
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 291
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 377
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 379
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 379
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 441
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 557
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 604
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 630
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 846
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 846
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 906
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 942
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT CROSSLNK 957
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJQ4"
FT VAR_SEQ 40..828
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_021686"
FT VAR_SEQ 386..829
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_021687"
FT CONFLICT 865
FT /note="P -> H (in Ref. 1; AAR91797)"
FT /evidence="ECO:0000305"
FT CONFLICT 950
FT /note="A -> V (in Ref. 1; AAR91797 and 5; CAD32912)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="S -> Y (in Ref. 1; AAR91796/AAR91798 and 2;
FT BAC33598)"
FT /evidence="ECO:0000305"
FT CONFLICT 997
FT /note="I -> T (in Ref. 1; AAR91797)"
FT /evidence="ECO:0000305"
FT CONFLICT 1022
FT /note="T -> M (in Ref. 1; AAR91797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1067 AA; 113110 MW; 23B92F488AAF53E5 CRC64;
MSRRKQAKPQ HINWEEGQGE QPQQLPSPDL AEALAAEEPG APVNSPGNCD EASEDSIPVK
RPRREDTHIC NKCCAEFFSL SEFMEHKKSC TKTPPVLIMN DSEGPVPSED FSRAALSHQL
GSPSNKDSLQ ENGSSSGDLK KLGTDSILYL KTEATQPSTP QDISYLPKGK VANTNVTLQA
LRGTKVAVNQ RGAEAPMAPM PAAQGIPWVL EQILCLQQQQ LQQIQLTEQI RVQVNMWAAH
ALHSGVAGAD TLKALSSHVS QQVSVSQQVS AAVALLSQKA SNPALSLDAL KQAKLPHASV
PSAASPLSSG LTSFTLKPDG TRVLPNFVSR LPSALLPQTP GSVLLQSPFS AVTLDQSKKG
KGKPQNLSAS ASVLDVKAKD EVVLGKHKCR YCPKVFGTDS SLQIHLRSHT GERPYVCPIC
GHRFTTKGNL KVHLQRHPEV KANPQLLAEF QDKGAVSAAS HYALPVPVPA DESSLSVDAE
PVPVTGTPSL GLPQKLTSGP NSRDLMGGSL PNDMQPGPSP ESEAGLPLLG VGMIHNPPKA
GGFQGTGAPE SGSETLKLQQ LVENIDKATT DPNECLICHR VLSCQSSLKM HYRTHTGERP
FQCKICGRAF STKGNLKTHL GVHRTNTTVK TQHSCPICQK KFTNAVMLQQ HIRMHMGGQI
PNTPLPESPC DFTAPEPVAV SENGSASGVC QDDAAEGMEA EEVCSQDVPS GPSTVSLPVP
SAHLASPSLG FSVLASLDTQ GKGALPALAL QRQSSRENSS LEGGDTGPAN DSSLLVGDQE
CQSRSPDATE TMCYQAVSPA NSQAGSVKSR SPEGHKAEGV ESCRVDTEGR TSLPPTFIRA
QPTFVKVEVP GTFVGPPSMP SGMPPLLASQ PQPRRQAKQH CCTRCGKNFS SASALQIHER
THTGEKPFVC NICGRAFTTK GNLKVHYMTH GANNNSARRG RKLAIENPMA ALSAEGKRAP
EVFSKELLSP AVSVDPASWN QYTSVLNGGL AMKTNEISVI QSGGIPTLPV SLGASSVVSN
GTISKLDGSQ TGVSMPMSGN GEKLAVPDGM AKHQFPHFLE ENKIAVS
