(data stored in ACNUC9552 zone)

SWISSPROT: B2CL1_RAT

ID   B2CL1_RAT               Reviewed;         233 AA.
AC   P53563; P70613; P70614; Q52KS0; Q62678; Q62836; Q64087; Q64128;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   30-AUG-2017, entry version 166.
DE   RecName: Full=Bcl-2-like protein 1;
DE            Short=Bcl2-L-1;
DE   AltName: Full=Apoptosis regulator Bcl-X;
GN   Name=Bcl2l1; Synonyms=Bclx, Blc2l;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS BCL-X(L) AND BCL-X(S)).
RC   TISSUE=Brain;
RA   Michaelidis T.M.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORM BCL-X(L)).
RC   TISSUE=Brain;
RA   Wesselingh S.L., David G.L., Choi S., Veliuona M., Hardwick J.M.;
RT   "Cloning and expression of rat bcl-x in cultured neurons.";
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(BETA)), AND
RP   FUNCTION.
RC   TISSUE=Thymus;
RX   PubMed=8662675; DOI=10.1074/jbc.271.22.13258;
RA   Shiraiwa N., Inohara N., Okada S., Yuzaki M., Shoji S., Ohta S.;
RT   "An additional form of rat Bcl-x, Bcl-xbeta, generated by an unspliced
RT   RNA, promotes apoptosis in promyeloid cells.";
RL   J. Biol. Chem. 271:13258-13265(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(S)), AND
RP   FUNCTION.
RC   STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX   PubMed=7828536; DOI=10.1210/endo.136.1.7828536;
RA   Tilly J.L., Tilly K.I., Kenton M.L., Johnson A.L.;
RT   "Expression of members of the Bcl-2 gene family in the immature rat
RT   ovary: equine chorionic gonadotropin-mediated inhibition of granulosa
RT   cell apoptosis is associated with decreased Bax and constitutive Bcl-2
RT   and Bcl-xlong messenger ribonucleic acid levels.";
RL   Endocrinology 136:232-241(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BCL-X(L)).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION IN SYNAPTIC VESICLE REGULATION, AND INTERACTION WITH DNM1L.
RX   PubMed=18250306; DOI=10.1073/pnas.0711647105;
RA   Li H., Chen Y., Jones A.F., Sanger R.H., Collis L.P., Flannery R.,
RA   McNay E.C., Yu T., Schwarzenbacher R., Bossy B., Bossy-Wetzel E.,
RA   Bennett M.V., Pypaert M., Hickman J.A., Smith P.J., Hardwick J.M.,
RA   Jonas E.A.;
RT   "Bcl-xL induces Drp1-dependent synapse formation in cultured
RT   hippocampal neurons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2169-2174(2008).
RN   [7]
RP   FUNCTION IN SYNAPTIC VESICLE REGULATION, INTERACTION WITH ATP5A1 AND
RP   ATP5B, AND SUBCELLULAR LOCATION.
RX   PubMed=21926988; DOI=10.1038/ncb2330;
RA   Alavian K.N., Li H., Collis L., Bonanni L., Zeng L., Sacchetti S.,
RA   Lazrove E., Nabili P., Flaherty B., Graham M., Chen Y., Messerli S.M.,
RA   Mariggio M.A., Rahner C., McNay E., Shore G.C., Smith P.J.,
RA   Hardwick J.M., Jonas E.A.;
RT   "Bcl-xL regulates metabolic efficiency of neurons through interaction
RT   with the mitochondrial F1FO ATP synthase.";
RL   Nat. Cell Biol. 13:1224-1233(2011).
RN   [8]
RP   FUNCTION IN SYNAPTIC VESICLE REGULATION, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH CLTA; DNM1L AND MFF.
RX   PubMed=23792689; DOI=10.1038/ncb2791;
RA   Li H., Alavian K.N., Lazrove E., Mehta N., Jones A., Zhang P.,
RA   Licznerski P., Graham M., Uo T., Guo J., Rahner C., Duman R.S.,
RA   Morrison R.S., Jonas E.A.;
RT   "A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics
RT   during endocytosis.";
RL   Nat. Cell Biol. 15:773-785(2013).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=9346936; DOI=10.1074/jbc.272.44.27886;
RA   Aritomi M., Kunishima N., Inohara N., Ishibashi Y., Ohta S.,
RA   Morikawa K.;
RT   "Crystal structure of rat Bcl-xL. Implications for the function of the
RT   Bcl-2 protein family.";
RL   J. Biol. Chem. 272:27886-27892(1997).
CC   -!- FUNCTION: Potent inhibitor of cell death. Inhibits activation of
CC       caspases. Appears to regulate cell death by blocking the voltage-
CC       dependent anion channel (VDAC) by binding to it and preventing the
CC       release of the caspase activator, CYC1, from the mitochondrial
CC       membrane. Also acts as a regulator of G2 checkpoint and
CC       progression to cytokinesis during mitosis.
CC   -!- FUNCTION: Isoform Bcl-X(L) also regulates presynaptic plasticity,
CC       including neurotransmitter release and recovery, number of axonal
CC       mitochondria as well as size and number of synaptic vesicle
CC       clusters. During synaptic stimulation, increases ATP availability
CC       from mitochondria through regulation of mitochondrial membrane ATP
CC       synthase F(1)F(0) activity and regulates endocytic vesicle
CC       retrieval in hippocampal neurons through association with DMN1L
CC       and stimulation of its GTPase activity in synaptic vesicles. May
CC       attenuate inflammation impairing NLRP1-inflammasome activation,
CC       hence CASP1 activation and IL1B release (By similarity).
CC       {ECO:0000250|UniProtKB:Q07817, ECO:0000269|PubMed:18250306,
CC       ECO:0000269|PubMed:21926988, ECO:0000269|PubMed:23792689,
CC       ECO:0000269|PubMed:7828536, ECO:0000269|PubMed:8662675}.
CC   -!- FUNCTION: Isoform Bcl-X(S) promotes apoptosis.
CC   -!- SUBUNIT: Homodimer. Isoform Bcl-X(L) forms heterodimers with BAX,
CC       BAK or BCL2. Heterodimerization with BAX does not seem to be
CC       required for anti-apoptotic activity. Interacts with BCL2L11.
CC       Interacts with BAD. Isoform Bcl-X(L) interacts with SIVA1 isoform
CC       1; the interaction inhibits the anti-apoptotic activity. Interacts
CC       with BECN1 and PGAM5. Isoform Bcl-X(L) interacts with IKZF3.
CC       Interacts with HEBP2. Isoform Bcl-X(L) interacts with BOP.
CC       Interacts with p53/TP53 and BBC3; interaction with BBC3 disrupts
CC       the interaction with p53/TP53. Isoform Bcl-X(L) interacts with
CC       DNM1L and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may form a
CC       complex in synaptic vesicles that also contains clathrin and MFF.
CC       Interacts with ATP5A and ATP5B; the interactions mediate the
CC       association of isoform Bcl-X(L) with the mitochondrial membrane
CC       ATP synthase F(1)F(0) ATP synthase. Interacts with VDAC1 (By
CC       similarity). Isoform Bcl-X(L) interacts (via the loop between
CC       motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with
CC       NLRP2, NLRP3, NLRP4, PYCARD, nor MEFV (By similarity). Interacts
CC       with BCL2L11 (via BH3) (By similarity).
CC       {ECO:0000250|UniProtKB:Q07817, ECO:0000250|UniProtKB:Q64373,
CC       ECO:0000269|PubMed:18250306, ECO:0000269|PubMed:21926988,
CC       ECO:0000269|PubMed:23792689}.
CC   -!- INTERACTION:
CC       O35303:Dnm1l; NbExp=2; IntAct=EBI-287204, EBI-1767447;
CC   -!- SUBCELLULAR LOCATION: Isoform Bcl-X(L): Mitochondrion inner
CC       membrane. Mitochondrion outer membrane. Mitochondrion matrix.
CC       Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane.
CC       Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250}. Nucleus membrane
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Note=Localizes to the centrosome
CC       when phosphorylated at Ser-49 (By similarity). After neuronal
CC       stimulation, translocates from cytosol to synaptic vesicle and
CC       mitochondrion membrane in a calmodulin-dependent manner.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Bcl-X(L); Synonyms=Bcl-xL;
CC         IsoId=P53563-1; Sequence=Displayed;
CC       Name=Bcl-X(S); Synonyms=Bcl-xS;
CC         IsoId=P53563-2; Sequence=VSP_000520;
CC       Name=Bcl-X(beta);
CC         IsoId=P53563-3; Sequence=VSP_000521;
CC   -!- TISSUE SPECIFICITY: Expressed in most tissues. Bcl-X(beta) is
CC       specifically expressed in cerebellum, heart, and thymus. In the
CC       ovary, the predominant form is Bcl-X(L), with a small but
CC       detectable level of Bcl-X(S).
CC   -!- DOMAIN: The BH4 motif is required for anti-apoptotic activity. The
CC       BH1 and BH2 motifs are required for both heterodimerization with
CC       other Bcl-2 family members and for repression of cell death.
CC   -!- DOMAIN: The loop between motifs BH4 and BH3 is required for the
CC       interaction with NLRP1. {ECO:0000250|UniProtKB:Q07817}.
CC   -!- PTM: Proteolytically cleaved by caspases during apoptosis. The
CC       cleaved protein, lacking the BH4 motif, has pro-apoptotic activity
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated on Ser-62 by CDK1. This phosphorylation is
CC       partial in normal mitotic cells, but complete in G2-arrested cells
CC       upon DNA-damage, thus promoting subsequent apoptosis probably by
CC       triggering caspases-mediated proteolysis. Phosphorylated by PLK3,
CC       leading to regulate the G2 checkpoint and progression to
CC       cytokinesis during mitosis. Phosphorylation at Ser-49 appears
CC       during the S phase and G2, disappears rapidly in early mitosis
CC       during prometaphase, metaphase and early anaphase, and re-appears
CC       during telophase and cytokinesis (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC60701.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAC60702.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; X82537; CAA57886.1; -; Genomic_DNA.
DR   EMBL; X82537; CAA57887.1; -; Genomic_DNA.
DR   EMBL; U10579; AAA19257.1; -; Unassigned_DNA.
DR   EMBL; U72350; AAB17353.1; -; mRNA.
DR   EMBL; U72349; AAB17352.1; -; mRNA.
DR   EMBL; U34963; AAA77686.1; -; mRNA.
DR   EMBL; S76513; AAC60701.2; ALT_INIT; mRNA.
DR   EMBL; S78284; AAC60702.1; ALT_INIT; mRNA.
DR   EMBL; BC094213; AAH94213.1; -; mRNA.
DR   PIR; I67431; I67431.
DR   PIR; I67435; I67435.
DR   PIR; S51761; S51761.
DR   RefSeq; NP_001028842.1; NM_001033670.1. [P53563-1]
DR   RefSeq; NP_001028843.1; NM_001033671.1. [P53563-2]
DR   RefSeq; NP_113723.2; NM_031535.2.
DR   RefSeq; XP_006235327.1; XM_006235265.3. [P53563-1]
DR   UniGene; Rn.10323; -.
DR   PDB; 1AF3; X-ray; 2.50 A; A=1-196.
DR   PDB; 4QNQ; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-233.
DR   PDBsum; 1AF3; -.
DR   PDBsum; 4QNQ; -.
DR   DisProt; DP00449; -.
DR   ProteinModelPortal; P53563; -.
DR   SMR; P53563; -.
DR   BioGrid; 246998; 5.
DR   DIP; DIP-29698N; -.
DR   IntAct; P53563; 2.
DR   STRING; 10116.ENSRNOP00000043542; -.
DR   ChEMBL; CHEMBL1075182; -.
DR   iPTMnet; P53563; -.
DR   PhosphoSitePlus; P53563; -.
DR   SwissPalm; P53563; -.
DR   PaxDb; P53563; -.
DR   PRIDE; P53563; -.
DR   Ensembl; ENSRNOT00000010762; ENSRNOP00000010762; ENSRNOG00000007946. [P53563-1]
DR   GeneID; 24888; -.
DR   KEGG; rno:24888; -.
DR   UCSC; RGD:2200; rat. [P53563-1]
DR   CTD; 598; -.
DR   RGD; 2200; Bcl2l1.
DR   eggNOG; KOG4728; Eukaryota.
DR   eggNOG; ENOG41123S0; LUCA.
DR   GeneTree; ENSGT00530000062935; -.
DR   InParanoid; P53563; -.
DR   KO; K04570; -.
DR   OMA; NGSPSWH; -.
DR   PhylomeDB; P53563; -.
DR   EvolutionaryTrace; P53563; -.
DR   PRO; PR:P53563; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000007946; -.
DR   ExpressionAtlas; P53563; baseline and differential.
DR   Genevisible; P53563; RN.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005740; C:mitochondrial envelope; IDA:RGD.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IDA:CAFA.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051400; F:BH domain binding; IPI:RGD.
DR   GO; GO:0030276; F:clathrin binding; IPI:CAFA.
DR   GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:RGD.
DR   GO; GO:0051020; F:GTPase binding; IPI:CAFA.
DR   GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:RGD.
DR   GO; GO:0032403; F:protein complex binding; IPI:RGD.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR   GO; GO:0008134; F:transcription factor binding; IPI:RGD.
DR   GO; GO:0007568; P:aging; IEP:RGD.
DR   GO; GO:0006915; P:apoptotic process; IEP:RGD.
DR   GO; GO:1905218; P:cellular response to astaxanthin; IEP:RGD.
DR   GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR   GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR   GO; GO:0035690; P:cellular response to drug; IEP:RGD.
DR   GO; GO:0036018; P:cellular response to erythropoietin; IEP:RGD.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR   GO; GO:1990646; P:cellular response to prolactin; IEP:RGD.
DR   GO; GO:1904579; P:cellular response to thapsigargin; IEP:RGD.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR   GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR   GO; GO:0000910; P:cytokinesis; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR   GO; GO:0007093; P:mitotic cell cycle checkpoint; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR   GO; GO:1900118; P:negative regulation of execution phase of apoptosis; ISS:UniProtKB.
DR   GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
DR   GO; GO:0001541; P:ovarian follicle development; IMP:RGD.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR   GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:CAFA.
DR   GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; IMP:CAFA.
DR   GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:CAFA.
DR   GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; IMP:CAFA.
DR   GO; GO:0042981; P:regulation of apoptotic process; IDA:RGD.
DR   GO; GO:1900452; P:regulation of long term synaptic depression; IMP:CAFA.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR   GO; GO:0036017; P:response to erythropoietin; IEP:RGD.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
DR   GO; GO:0002931; P:response to ischemia; IDA:RGD.
DR   GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR   GO; GO:0036466; P:synaptic vesicle recycling via endosome; IMP:CAFA.
DR   InterPro; IPR013279; Apop_reg_BclX.
DR   InterPro; IPR002475; Bcl2-like.
DR   InterPro; IPR004725; Bcl2/BclX.
DR   InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR   InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR   InterPro; IPR020728; Bcl2_BH3_motif_CS.
DR   InterPro; IPR003093; Bcl2_BH4.
DR   InterPro; IPR020731; Bcl2_BH4_motif_CS.
DR   InterPro; IPR026298; Blc2_fam.
DR   PANTHER; PTHR11256; PTHR11256; 1.
DR   PANTHER; PTHR11256:SF61; PTHR11256:SF61; 1.
DR   Pfam; PF00452; Bcl-2; 1.
DR   Pfam; PF02180; BH4; 1.
DR   PRINTS; PR01864; APOPREGBCLX.
DR   PRINTS; PR01862; BCL2FAMILY.
DR   SMART; SM00265; BH4; 1.
DR   SUPFAM; SSF56854; SSF56854; 1.
DR   TIGRFAMs; TIGR00865; bcl-2; 1.
DR   PROSITE; PS50062; BCL2_FAMILY; 1.
DR   PROSITE; PS01080; BH1; 1.
DR   PROSITE; PS01258; BH2; 1.
DR   PROSITE; PS01259; BH3; 1.
DR   PROSITE; PS01260; BH4_1; 1.
DR   PROSITE; PS50063; BH4_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P53563.
DR   SWISS-2DPAGE; P53563.
KW   3D-structure; Alternative splicing; Apoptosis; Cell junction;
KW   Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW   Endocytosis; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Mitochondrion outer membrane; Nucleus; Phosphoprotein;
KW   Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN         1    233       Bcl-2-like protein 1.
FT                                /FTId=PRO_0000143065.
FT   TRANSMEM    210    226       Helical. {ECO:0000255}.
FT   MOTIF         4     24       BH4.
FT   MOTIF        86    100       BH3.
FT   MOTIF       129    148       BH1.
FT   MOTIF       180    195       BH2.
FT   MOD_RES      49     49       Phosphoserine; by PLK3.
FT                                {ECO:0000250|UniProtKB:Q07817}.
FT   MOD_RES      62     62       Phosphoserine; by CDK1.
FT                                {ECO:0000250|UniProtKB:Q07817}.
FT   VAR_SEQ     126    188       Missing (in isoform Bcl-X(S)).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_000520.
FT   VAR_SEQ     189    233       DTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSL
FT                                FSRK -> VRTTPLVCPPLVCLSSVEIPNCPFWSPGMVVED
FT                                IDYSGDIPGLL (in isoform Bcl-X(beta)).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_000521.
FT   CONFLICT      6      6       R -> Q (in Ref. 1; CAA57886/CAA57887).
FT                                {ECO:0000305}.
FT   CONFLICT     12     12       F -> S (in Ref. 2; AAA19257).
FT                                {ECO:0000305}.
FT   CONFLICT     64     64       A -> E (in Ref. 2; AAA19257).
FT                                {ECO:0000305}.
FT   CONFLICT     81     81       I -> L (in Ref. 4; AAA77686/AAC60701/
FT                                AAC60702). {ECO:0000305}.
FT   CONFLICT    119    119       A -> V (in Ref. 4; AAA77686/AAC60701/
FT                                AAC60702). {ECO:0000305}.
FT   CONFLICT    143    144       FF -> SS (in Ref. 4; AAA77686/AAC60701).
FT                                {ECO:0000305}.
FT   CONFLICT    199    199       A -> T (in Ref. 4; AAA77686/AAC60701/
FT                                AAC60702). {ECO:0000305}.
FT   CONFLICT    201    201       A -> P (in Ref. 4; AAA77686/AAC60701/
FT                                AAC60702). {ECO:0000305}.
FT   HELIX         2     19       {ECO:0000244|PDB:4QNQ}.
FT   TURN         25     28       {ECO:0000244|PDB:1AF3}.
FT   HELIX        82    100       {ECO:0000244|PDB:4QNQ}.
FT   HELIX       102    111       {ECO:0000244|PDB:4QNQ}.
FT   TURN        116    118       {ECO:0000244|PDB:4QNQ}.
FT   HELIX       119    130       {ECO:0000244|PDB:4QNQ}.
FT   TURN        131    133       {ECO:0000244|PDB:4QNQ}.
FT   HELIX       137    156       {ECO:0000244|PDB:4QNQ}.
FT   HELIX       162    177       {ECO:0000244|PDB:4QNQ}.
FT   HELIX       179    184       {ECO:0000244|PDB:4QNQ}.
FT   HELIX       187    196       {ECO:0000244|PDB:4QNQ}.
SQ   SEQUENCE   233 AA;  26158 MW;  2B62B6C63864BC8F CRC64;
     MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEE TEPERETPSA INGNPSWHLA
     DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY
     QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIASWM ATYLNDHLEP
     WIQENGGWDT FVDLYGNNAA AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK
//

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