NPCL1_RAT
ID NPCL1_RAT Reviewed; 1331 AA.
AC Q6T3U3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=NPC1-like intracellular cholesterol transporter 1 {ECO:0000312|RGD:1303135};
DE Short=Npc1l1 {ECO:0000303|PubMed:15928087};
DE AltName: Full=Niemann-Pick C1-like protein 1 {ECO:0000303|PubMed:14976318};
DE Flags: Precursor;
GN Name=Npc1l1 {ECO:0000312|RGD:1303135};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley;
RX PubMed=14976318; DOI=10.1126/science.1093131;
RA Altmann S.W., Davis H.R. Jr., Zhu L.-J., Yao X., Hoos L.M., Tetzloff G.,
RA Iyer S.P.N., Maguire M., Golovko A., Zeng M., Wang L., Murgolo N.,
RA Graziano M.P.;
RT "Niemann-Pick C1 like 1 protein is critical for intestinal cholesterol
RT absorption.";
RL Science 303:1201-1204(2004).
RN [2]
RP SUBCELLULAR LOCATION, AND CHARACTERIZATION.
RX PubMed=15777641; DOI=10.1016/j.bbagen.2004.12.021;
RA Iyer S.P.N., Yao X., Crona J.H., Hoos L.M., Tetzloff G., Davis H.R. Jr.,
RA Graziano M.P., Altmann S.W.;
RT "Characterization of the putative native and recombinant rat sterol
RT transporter Niemann-Pick C1 Like 1 (NPC1L1) protein.";
RL Biochim. Biophys. Acta 1722:282-292(2005).
RN [3]
RP FUNCTION.
RX PubMed=15928087; DOI=10.1073/pnas.0500269102;
RA Garcia-Calvo M., Lisnock J., Bull H.G., Hawes B.E., Burnett D.A.,
RA Braun M.P., Crona J.H., Davis H.R. Jr., Dean D.C., Detmers P.A.,
RA Graziano M.P., Hughes M., MacIntyre D.E., Ogawa A., O'neill K.A.,
RA Iyer S.P.N., Shevell D.E., Smith M.M., Tang Y.S., Makarewicz A.M.,
RA Ujjainwalla F., Altmann S.W., Chapman K.T., Thornberry N.A.;
RT "The target of ezetimibe is Niemann-Pick C1-like 1 (NPC1L1).";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8132-8137(2005).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=17135346; DOI=10.1124/jpet.106.114181;
RA Yamanashi Y., Takada T., Suzuki H.;
RT "Niemann-Pick C1-like 1 overexpression facilitates ezetimibe-sensitive
RT cholesterol and beta-sitosterol uptake in CaCo-2 cells.";
RL J. Pharmacol. Exp. Ther. 320:559-564(2007).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=29880681; DOI=10.1126/science.aao6575;
RA Zhang Y.Y., Fu Z.Y., Wei J., Qi W., Baituola G., Luo J., Meng Y.J.,
RA Guo S.Y., Yin H., Jiang S.Y., Li Y.F., Miao H.H., Liu Y., Wang Y., Li B.L.,
RA Ma Y.T., Song B.L.;
RT "A LIMA1 variant promotes low plasma LDL cholesterol and decreases
RT intestinal cholesterol absorption.";
RL Science 360:1087-1092(2018).
CC -!- FUNCTION: Plays a major role in cholesterol homeostasis
CC (PubMed:17135346). Critical for the uptake of cholesterol across the
CC plasma membrane of the intestinal enterocyte (PubMed:17135346).
CC Involved in plant sterol absorption, it transports sitosterol, although
CC at lower rates than cholesterol (PubMed:17135346). Is the direct
CC molecular target of ezetimibe, a drug that inhibits cholesterol
CC absorption and is approved for the treatment of hypercholesterolemia
CC (PubMed:15928087). May have a function in the transport of multiple
CC lipids and their homeostasis, thereby influencing lipid metabolism
CC regulation (By similarity). May be involved in caveolin trafficking
CC from the plasma membrane (By similarity). Acts as a negative regulator
CC of NPC2 and down-regulates its expression and secretion by inhibiting
CC its maturation and accelerating its degradation (By similarity).
CC {ECO:0000250|UniProtKB:Q6T3U4, ECO:0000250|UniProtKB:Q9UHC9,
CC ECO:0000269|PubMed:15928087, ECO:0000269|PubMed:17135346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747,
CC ChEBI:CHEBI:16113; Evidence={ECO:0000269|PubMed:17135346};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sitosterol(out) = sitosterol(in); Xref=Rhea:RHEA:70723,
CC ChEBI:CHEBI:27693; Evidence={ECO:0000269|PubMed:17135346};
CC -!- SUBUNIT: Interacts with RAB11A, MYO5B and RAB11FIP2. Interaction with
CC RAB11A, MYO5B and RAB11FIP2 is required for proper transport to the
CC plasma membrane upon cholesterol depletion (By similarity). Interacts
CC with NPC2 (By similarity). Interacts with LIMA1 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q6T3U4}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:17135346}; Multi-pass membrane protein. Cell
CC membrane {ECO:0000269|PubMed:29880681}; Multi-pass membrane protein.
CC Note=Subfractionation of brush border membranes from proximal
CC enterocytes suggests considerable association with the apical membrane
CC fraction. Exists as a predominantly cell surface membrane expressed
CC protein. {ECO:0000269|PubMed:14976318}.
CC -!- TISSUE SPECIFICITY: Small intestine showed the highest level of
CC expression (PubMed:14976318). Expression in other tissues including
CC gall bladder, liver, testis and stomach is also observed
CC (PubMed:14976318). Along the duodenum-ileum axis, the levels vary in
CC different segments of the intestine with peak expression in the
CC proximal jejunum (PubMed:14976318). Protein expression is confined to
CC the enterocyte (PubMed:14976318). Discrete localization to the
CC epithelial layer bordering the luminal space along the crypt-villus
CC axis (PubMed:14976318). Protein expression in the enterocyte is
CC observed closest to the luminal space. Expression in enterocytes from
CC the proximal (jejunum) but not in the distal (ileum) region
CC (PubMed:14976318). {ECO:0000269|PubMed:14976318}.
CC -!- PTM: Highly glycosylated.
CC -!- SIMILARITY: Belongs to the patched family. {ECO:0000305}.
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DR EMBL; AY437867; AAR97888.1; -; mRNA.
DR RefSeq; NP_001002025.1; NM_001002025.1.
DR PDB; 6V3F; EM; 3.70 A; A=21-1331.
DR PDB; 6V3H; EM; 3.50 A; A=21-1331.
DR PDBsum; 6V3F; -.
DR PDBsum; 6V3H; -.
DR AlphaFoldDB; Q6T3U3; -.
DR SMR; Q6T3U3; -.
DR STRING; 10116.ENSRNOP00000065524; -.
DR BindingDB; Q6T3U3; -.
DR ChEMBL; CHEMBL5161; -.
DR DrugCentral; Q6T3U3; -.
DR GlyGen; Q6T3U3; 17 sites.
DR PaxDb; Q6T3U3; -.
DR PRIDE; Q6T3U3; -.
DR Ensembl; ENSRNOT00000075827; ENSRNOP00000065524; ENSRNOG00000049955.
DR GeneID; 432367; -.
DR KEGG; rno:432367; -.
DR CTD; 29881; -.
DR RGD; 1303135; Npc1l1.
DR eggNOG; KOG1933; Eukaryota.
DR GeneTree; ENSGT00940000159904; -.
DR HOGENOM; CLU_002359_0_0_1; -.
DR InParanoid; Q6T3U3; -.
DR OMA; VSLHCQN; -.
DR OrthoDB; 731120at2759; -.
DR PhylomeDB; Q6T3U3; -.
DR Reactome; R-RNO-8963678; Intestinal lipid absorption.
DR PRO; PR:Q6T3U3; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000049955; Expressed in jejunum and 6 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0044214; C:spanning component of plasma membrane; ISO:RGD.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:1901363; F:heterocyclic compound binding; IPI:RGD.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR GO; GO:0031489; F:myosin V binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0071501; P:cellular response to sterol depletion; ISO:RGD.
DR GO; GO:0006695; P:cholesterol biosynthetic process; ISO:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0070508; P:cholesterol import; IDA:UniProtKB.
DR GO; GO:0030301; P:cholesterol transport; ISO:RGD.
DR GO; GO:0030299; P:intestinal cholesterol absorption; ISO:RGD.
DR GO; GO:0042157; P:lipoprotein metabolic process; ISO:RGD.
DR GO; GO:0014850; P:response to muscle activity; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0015918; P:sterol transport; IBA:GO_Central.
DR GO; GO:0051180; P:vitamin transport; IDA:UniProtKB.
DR InterPro; IPR004765; NPC1-like.
DR InterPro; IPR032190; NPC1_N.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR Pfam; PF16414; NPC1_N; 1.
DR Pfam; PF02460; Patched; 1.
DR Pfam; PF12349; Sterol-sensing; 1.
DR TIGRFAMs; TIGR00917; 2A060601; 1.
DR PROSITE; PS50156; SSD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cholesterol metabolism; Disulfide bond;
KW Glycoprotein; Lipid metabolism; Membrane; Reference proteome; Signal;
KW Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1331
FT /note="NPC1-like intracellular cholesterol transporter 1"
FT /id="PRO_0000023268"
FT TOPO_DOM 21..282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..632
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 633..653
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 654..665
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 666..686
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 687..696
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..742
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 743..763
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 764..776
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 777..797
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 798..846
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 847..867
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 868..1113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1114..1134
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1135..1142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1143..1163
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1164..1165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1166..1186
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1187..1206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1207..1227
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1228..1242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1243..1263
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1264..1331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 632..797
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 909
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 917
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1038
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1076
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..90
FT /evidence="ECO:0000250|UniProtKB:Q9UHC9"
FT DISULFID 38..56
FT /evidence="ECO:0000250|UniProtKB:Q9UHC9"
FT DISULFID 77..125
FT /evidence="ECO:0000250|UniProtKB:Q9UHC9"
FT DISULFID 91..129
FT /evidence="ECO:0000250|UniProtKB:Q9UHC9"
FT DISULFID 113..254
FT /evidence="ECO:0000250|UniProtKB:Q9UHC9"
FT DISULFID 116..172
FT /evidence="ECO:0000250|UniProtKB:Q9UHC9"
FT DISULFID 189..197
FT /evidence="ECO:0000250|UniProtKB:Q9UHC9"
FT DISULFID 243..259
FT /evidence="ECO:0000250|UniProtKB:Q9UHC9"
FT DISULFID 256..263
FT /evidence="ECO:0000250|UniProtKB:Q9UHC9"
FT DISULFID 471..485
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 525..542
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 920..925
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 967..1025
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 981..990
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:6V3H"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:6V3H"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 114..129
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 152..161
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:6V3H"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 283..311
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 333..350
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 352..367
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 368..372
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 389..401
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 406..416
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 438..452
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:6V3H"
FT TURN 459..462
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 490..494
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 505..509
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 518..527
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 552..555
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 564..566
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 569..576
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 585..606
FT /evidence="ECO:0007829|PDB:6V3H"
FT TURN 608..610
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 611..616
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 620..625
FT /evidence="ECO:0007829|PDB:6V3H"
FT TURN 626..632
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 633..636
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 638..650
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 655..659
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 660..663
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 666..689
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 696..699
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 702..723
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 732..761
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 767..787
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 790..803
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 827..834
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 836..840
FT /evidence="ECO:0007829|PDB:6V3H"
FT TURN 843..845
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 846..863
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 873..876
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 883..893
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 899..904
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 910..912
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 913..917
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 930..938
FT /evidence="ECO:0007829|PDB:6V3H"
FT TURN 941..943
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 946..948
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 953..961
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 963..965
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 968..970
FT /evidence="ECO:0007829|PDB:6V3H"
FT TURN 975..978
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 979..981
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 987..989
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 992..995
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 999..1001
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1006..1016
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1029..1032
FT /evidence="ECO:0007829|PDB:6V3H"
FT TURN 1033..1036
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 1037..1040
FT /evidence="ECO:0007829|PDB:6V3H"
FT TURN 1041..1043
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 1044..1054
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1060..1081
FT /evidence="ECO:0007829|PDB:6V3H"
FT STRAND 1093..1096
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1100..1103
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1104..1107
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1109..1131
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1136..1160
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1166..1178
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1180..1191
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1198..1226
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1227..1230
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1234..1239
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1241..1256
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1258..1266
FT /evidence="ECO:0007829|PDB:6V3H"
FT HELIX 1272..1281
FT /evidence="ECO:0007829|PDB:6V3H"
SQ SEQUENCE 1331 AA; 146415 MW; 2E10EF2E3A337F70 CRC64;
MAAAWLGWLL WALLLSAAQG ELYTPKHEAG VCTFYEECGK NPELSGGLTS LSNVSCLSNT
PARHVTGEHL ALLQRICPRL YNGPNTTFAC CSTKQLLSLE SSMSITKALL TRCPACSDNF
VSLHCHNTCS PDQSLFINVT RVVERGAGEP PAVVAYEAFY QRSFAEKAYE SCSQVRIPAA
ASLAVGSMCG VYGSALCNAQ RWLNFQGDTG NGLAPLDITF HLLEPGQALP DGIQPLNGKI
APCNESQGDD SAVCSCQDCA ASCPVIPPPE ALRPSFYMGR MPGWLALIII FTAVFVLLSA
VLVRLRVVSN RNKNKAEGPQ EAPKLPHKHK LSPHTILGRF FQNWGTRVAS WPLTVLALSF
IVVIALAAGL TFIELTTDPV ELWSAPKSQA RKEKSFHDEH FGPFFRTNQI FVTARNRSSY
KYDSLLLGSK NFSGILSLDF LLELLELQER LRHLQVWSPE AERNISLQDI CYAPLNPYNT
SLSDCCVNSL LQYFQNNRTL LMLTANQTLN GQTSLVDWKD HFLYCANAPL TFKDGTSLAL
SCMADYGAPV FPFLAVGGYQ GTDYSEAEAL IITFSLNNYP ADDPRMAQAK LWEEAFLKEM
ESFQRNTSDK FQVAFSAERS LEDEINRTTI QDLPVFAVSY IIVFLYISLA LGSYSRCSRV
AVESKATLGL GGVIVVLGAV LAAMGFYSYL GVPSSLVIIQ VVPFLVLAVG ADNIFIFVLE
YQRLPRMPGE QREAHIGRTL GSVAPSMLLC SLSEAICFFL GALTPMPAVR TFALTSGLAI
ILDFLLQMTA FVALLSLDSK RQEASRPDVL CCFSTRKLPP PKEKEGLLLR FFRKIYAPFL
LHRFIRPVVM LLFLTLFGAN LYLMCNINVG LDQELALPKD SYLIDYFLFL NRYLEVGPPV
YFVTTSGFNF SSEAGMNATC SSAGCKSFSL TQKIQYASEF PDQSYVAIAA SSWVDDFIDW
LTPSSSCCRL YIRGPHKDEF CPSTDTSFNC LKNCMNRTLG PVRPTAEQFH KYLPWFLNDP
PNIRCPKGGL AAYRTSVNLS SDGQVIASQF MAYHKPLRNS QDFTEALRAS RLLAANITAD
LRKVPGTDPN FEVFPYTISN VFYQQYLTVL PEGIFTLALC FVPTFVVCYL LLGLDMCSGI
LNLLSIIMIL VDTIGLMAVW GISYNAVSLI NLVTAVGMSV EFVSHITRSF AVSTKPTRLE
RAKDATVFMG SAVFAGVAMT NFPGILILGF AQAQLIQIFF FRLNLLITLL GLLHGLVFLP
VVLSYLGPDV NQALVQEEKL ASEAAVAPEP SCPQYPSPAD ADANVNYGFA PELAHGANAA
RSSLPKSDQK F
