DISP1_MOUSE
ID DISP1_MOUSE Reviewed; 1521 AA.
AC Q3TDN0; Q3UUL8; Q80ZZ8; Q8CGS3; Q8CIP6; Q8CIQ9; Q9CT62;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein dispatched homolog 1;
DE AltName: Full=Mdispa;
GN Name=Disp1; Synonyms=Disp, Dispa, Icb, Icbins;
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 1), FUNCTION, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF 571-ASP-ASP-572 AND ASP-1049.
RC STRAIN=129; TISSUE=Testis;
RX PubMed=12372301; DOI=10.1016/s0092-8674(02)00977-7;
RA Ma Y., Erkner A., Gong R., Yao S., Taipale J., Basler K., Beachy P.A.;
RT "Hedgehog-mediated patterning of the mammalian embryo requires transporter-
RT like function of dispatched.";
RL Cell 111:63-75(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=Swiss Webster; TISSUE=Embryo;
RX PubMed=12421714; DOI=10.1242/dev.00178;
RA Kawakami T., Kawcak T., Li Y.-J., Zhang W., Hu Y., Chuang P.-T.;
RT "Mouse dispatched mutants fail to distribute hedgehog proteins and are
RT defective in hedgehog signaling.";
RL Development 129:5753-5765(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, Embryo, and Hypothalamus;
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 [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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-1501 (ISOFORM 1), FUNCTION, MUTAGENESIS OF
RP CYS-829, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=12372258; DOI=10.1016/s0960-9822(02)01147-8;
RA Caspary T., Garcia-Garcia M.J., Huangfu D., Eggenschwiler J.T., Wyler M.R.,
RA Rakeman A.S., Alcorn H.L., Anderson K.V.;
RT "Mouse Dispatched homolog1 is required for long-range, but not juxtacrine,
RT Hh signaling.";
RL Curr. Biol. 12:1628-1632(2002).
RN [6]
RP FUNCTION, AND INTERACTION WITH SHH.
RX PubMed=22902404; DOI=10.1016/j.celrep.2012.07.010;
RA Tukachinsky H., Kuzmickas R.P., Jao C.Y., Liu J., Salic A.;
RT "Dispatched and scube mediate the efficient secretion of the cholesterol-
RT modified hedgehog ligand.";
RL Cell Rep. 2:308-320(2012).
CC -!- FUNCTION: Functions in hedgehog (Hh) signaling. Regulates the release
CC and extracellular accumulation of cholesterol-modified hedgehog
CC proteins and is hence required for effective production of the Hh
CC signal. Synergizes with SCUBE2 to cause an increase in SHH secretion
CC (PubMed:22902404). {ECO:0000269|PubMed:12372258,
CC ECO:0000269|PubMed:12372301, ECO:0000269|PubMed:12421714,
CC ECO:0000269|PubMed:22902404}.
CC -!- SUBUNIT: Interacts with SHH; via the cholesterol anchor of the dually
CC lipid-modified SHH (ShhNp) (PubMed:22902404).
CC {ECO:0000269|PubMed:22902404}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TDN0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TDN0-2; Sequence=VSP_029322, VSP_029323;
CC -!- DEVELOPMENTAL STAGE: Expression overlaps with the one of SHH and IHH
CC being restricted to tissues that require Hh signaling. PubMed:12372301,
CC reported a more ubiquitous expression which is detected throughout the
CC embryo at 7.5 dpc and is maintained during embryonic development.
CC {ECO:0000269|PubMed:12372258, ECO:0000269|PubMed:12372301,
CC ECO:0000269|PubMed:12421714}.
CC -!- DISRUPTION PHENOTYPE: Death at or soon after 9.5 dpc probably due to
CC abnormal embryonic turning and looping of the heart. Embryos also
CC display defects in development of the forebrain and branchial arches.
CC {ECO:0000269|PubMed:12421714}.
CC -!- SIMILARITY: Belongs to the dispatched family. {ECO:0000305}.
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DR EMBL; AY150698; AAN52161.1; -; mRNA.
DR EMBL; AY150577; AAN64660.1; -; mRNA.
DR EMBL; AK004521; BAB23344.1; -; mRNA.
DR EMBL; AK138276; BAE23607.1; -; mRNA.
DR EMBL; AK170113; BAE41571.1; -; mRNA.
DR EMBL; BC043102; AAH43102.1; -; mRNA.
DR EMBL; BC059225; AAH59225.1; -; mRNA.
DR EMBL; AY144589; AAN08631.1; -; mRNA.
DR CCDS; CCDS56661.1; -. [Q3TDN0-1]
DR RefSeq; NP_001265147.1; NM_001278218.1. [Q3TDN0-1]
DR RefSeq; NP_001265148.1; NM_001278219.1. [Q3TDN0-1]
DR RefSeq; NP_001265149.1; NM_001278220.1. [Q3TDN0-1]
DR RefSeq; NP_081142.3; NM_026866.3. [Q3TDN0-1]
DR PDB; 7RPH; EM; 2.50 A; A=172-1521.
DR PDB; 7RPI; EM; 2.50 A; A=172-1521.
DR PDB; 7RPJ; EM; 3.20 A; A=172-1521.
DR PDB; 7RPK; EM; 2.70 A; A=172-1521.
DR PDBsum; 7RPH; -.
DR PDBsum; 7RPI; -.
DR PDBsum; 7RPJ; -.
DR PDBsum; 7RPK; -.
DR AlphaFoldDB; Q3TDN0; -.
DR SMR; Q3TDN0; -.
DR STRING; 10090.ENSMUSP00000003035; -.
DR TCDB; 2.A.6.9.2; the resistance-nodulation-cell division (rnd) superfamily.
DR GlyGen; Q3TDN0; 5 sites.
DR iPTMnet; Q3TDN0; -.
DR PhosphoSitePlus; Q3TDN0; -.
DR PaxDb; Q3TDN0; -.
DR PRIDE; Q3TDN0; -.
DR ProteomicsDB; 279774; -. [Q3TDN0-1]
DR ProteomicsDB; 279775; -. [Q3TDN0-2]
DR Antibodypedia; 34633; 148 antibodies from 32 providers.
DR Ensembl; ENSMUST00000003035; ENSMUSP00000003035; ENSMUSG00000030768. [Q3TDN0-1]
DR Ensembl; ENSMUST00000171366; ENSMUSP00000126742; ENSMUSG00000030768. [Q3TDN0-1]
DR Ensembl; ENSMUST00000195372; ENSMUSP00000141747; ENSMUSG00000030768. [Q3TDN0-1]
DR GeneID; 68897; -.
DR KEGG; mmu:68897; -.
DR UCSC; uc008ick.2; mouse. [Q3TDN0-1]
DR UCSC; uc008ico.2; mouse. [Q3TDN0-2]
DR CTD; 84976; -.
DR MGI; MGI:1916147; Disp1.
DR VEuPathDB; HostDB:ENSMUSG00000030768; -.
DR eggNOG; KOG3664; Eukaryota.
DR GeneTree; ENSGT00940000157407; -.
DR HOGENOM; CLU_004076_1_0_1; -.
DR InParanoid; Q3TDN0; -.
DR OMA; VYQAACC; -.
DR OrthoDB; 1156918at2759; -.
DR PhylomeDB; Q3TDN0; -.
DR TreeFam; TF324144; -.
DR BioGRID-ORCS; 68897; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Disp1; mouse.
DR PRO; PR:Q3TDN0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3TDN0; protein.
DR Bgee; ENSMUSG00000030768; Expressed in humerus cartilage element and 172 other tissues.
DR ExpressionAtlas; Q3TDN0; baseline and differential.
DR Genevisible; Q3TDN0; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IDA:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0060539; P:diaphragm development; ISO:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:MGI.
DR GO; GO:0007225; P:patched ligand maturation; IDA:MGI.
DR GO; GO:0015833; P:peptide transport; IDA:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR Pfam; PF02460; Patched; 2.
DR PROSITE; PS50156; SSD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1521
FT /note="Protein dispatched homolog 1"
FT /id="PRO_0000310694"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 717..737
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 986..1006
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1008..1028
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1038..1058
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1081..1101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1109..1129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 485..657
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 329..345
FT /note="IRSHPQFSDLCQRTTAV -> VCKTQLKSIQHNKVMLR (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029322"
FT VAR_SEQ 346..1521
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029323"
FT MUTAGEN 571..572
FT /note="DD->AA: Loss of function; when associated with A-
FT 1049."
FT /evidence="ECO:0000269|PubMed:12372301"
FT MUTAGEN 571..572
FT /note="DD->NN: Loss of function; when associated with N-
FT 1049."
FT /evidence="ECO:0000269|PubMed:12372301"
FT MUTAGEN 829
FT /note="C->F: In icb; loss of function."
FT /evidence="ECO:0000269|PubMed:12372258"
FT MUTAGEN 1049
FT /note="D->A: Loss of function; when associated with 571-A-
FT A-572."
FT /evidence="ECO:0000269|PubMed:12372301"
FT MUTAGEN 1049
FT /note="D->N: Loss of function; when associated with 571-N-
FT N-572."
FT /evidence="ECO:0000269|PubMed:12372301"
FT CONFLICT 292
FT /note="C -> W (in Ref. 3; BAE23607)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="K -> M (in Ref. 1; AAN52161)"
FT /evidence="ECO:0000305"
FT CONFLICT 949
FT /note="I -> V (in Ref. 3; BAE23607)"
FT /evidence="ECO:0000305"
FT CONFLICT 1309
FT /note="S -> N (in Ref. 1; AAN52161 and 2; AAN64660)"
FT /evidence="ECO:0000305"
FT CONFLICT 1431
FT /note="K -> E (in Ref. 1; AAN52161, 2; AAN64660 and 3;
FT BAE41571)"
FT /evidence="ECO:0000305"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 188..208
FT /evidence="ECO:0007829|PDB:7RPH"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 228..241
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 254..261
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:7RPK"
FT TURN 285..288
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 315..328
FT /evidence="ECO:0007829|PDB:7RPH"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:7RPI"
FT HELIX 353..360
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 371..389
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:7RPJ"
FT HELIX 398..403
FT /evidence="ECO:0007829|PDB:7RPK"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 422..429
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 450..460
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 464..470
FT /evidence="ECO:0007829|PDB:7RPH"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 479..489
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 495..501
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 504..521
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 524..547
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 556..560
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 561..568
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 571..586
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:7RPJ"
FT HELIX 592..620
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 624..626
FT /evidence="ECO:0007829|PDB:7RPJ"
FT HELIX 627..647
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 650..661
FT /evidence="ECO:0007829|PDB:7RPH"
FT TURN 662..664
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 682..705
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 707..714
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 716..735
FT /evidence="ECO:0007829|PDB:7RPH"
FT TURN 736..738
FT /evidence="ECO:0007829|PDB:7RPJ"
FT HELIX 747..749
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 758..764
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 766..768
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 771..778
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 782..791
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 816..818
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 819..833
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 846..849
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 850..858
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 866..871
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 881..898
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 909..912
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 918..930
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 935..953
FT /evidence="ECO:0007829|PDB:7RPH"
FT TURN 958..962
FT /evidence="ECO:0007829|PDB:7RPH"
FT STRAND 964..966
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 970..1001
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 1004..1027
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 1034..1060
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 1066..1093
FT /evidence="ECO:0007829|PDB:7RPH"
FT TURN 1094..1097
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 1101..1122
FT /evidence="ECO:0007829|PDB:7RPH"
FT HELIX 1124..1132
FT /evidence="ECO:0007829|PDB:7RPH"
FT TURN 1136..1139
FT /evidence="ECO:0007829|PDB:7RPH"
SQ SEQUENCE 1521 AA; 170130 MW; 7B1E9A0F7873BB30 CRC64;
MAVISGSDSV LLSNGSISTS TSNPSPLSPS DGDLPAQHLG PRETPRTKAS PNGCLQLNGT
VKSSFLPLDN QRTPQTPTQC CHPCPYHHPV SSHSNHQECH PEAGLAASPA LASCRMQPHS
EYSASLCPNH SPVYQAAHCL QPSPSFCLHH PWPDHFQHQP VRQHLTIIRP SRPFKFPRSY
AALLADWPVV VLGMCTLLIV VCALVGVLVP ELPDFSDPLL GFEPRGTTIG QRLVTWNNMM
RNTGYKATLA NYPYKYAEEQ ARSHRDDRWS DDHHERERRE VDWNFQKDSF FCDVPSDGYS
RVVFASAGGE TLWNLPAIKS MCDVDNSRIR SHPQFSDLCQ RTTAVSCCPS WTLGNYIAIL
NNRSSCQKIV ERDVSHTLKL LRTCAKHYQN GTLGPDCWDK AARRKDQLKC TNVPRKCTKY
NAVYQILHYL VDKDFMTPKT ADYAVPALKY SMLFSPTEKG ESMMNIYLDN FENWNSSDGI
TTVTGIEFGI KHSLFQDYLL MDTVYPAIAI AIVLLIMCVY TKSMFITLMT MFAIISSLIV
SYFLYRVVFN FEFFPFMNLT ALIILVGIGA DDAFVLCDVW NYTKFDKPRA ETSEAVSVTL
QHAALSMFVT SFTTAAAFYA NYVSNITAIR CFGVYAGTAI LVNYVLMVTW LPAVIVLHER
YLLNIFTCFR KPQPQAYDKS CWAVLCQKCR RVLFAVSEAS RIFFEKVLPC IVIKFRYLWL
IWFLALTVGG AYIVCVNPKM KLPSLELSEF QVFRSSHPFE RYDAEFKKLF MFERVHHGEE
LHMPITVIWG VSPEDSGDPL NPKSKGELTL DSTFNIASPA SQAWILHFCQ KLRNQTFFHQ
TEQQDFTSCF IETFKQWMEN QDCDEPALYP CCSHCSFPYK QEVFELCIKK AIMELDRSTG
YHLNNKTPGP RFDINDTIRA VVLEFQSTFL FTLAYEKMQQ FYKEVDSWIS HELSSAPEGL
SRGWFVSNLE FYDLQDSLSD GTLIAMGLSV AVAFSVMLLT TWNIIISLYA IVSIAGTIFV
TVGSLVLLGW ELNVLESVTI SVAVGLSVDF AVHYGVAYRL APDPDREGKV IFSLSRMGSA
IAMAALTTFV AGAMMMPSTV LAYTQLGTFM MLVMCVSWAF ATFFFQCLCR CLGPQGTCGQ
IPFPTKLQCS PFSHTLSARP GDRGPSKTHA ASAYSVDARG QKSQLEHEFY ELQPLASHSC
TSSEKTTYEE PHTCSEFFNG QAKNLRMPVP AAYSSELTKS PSSEPGSALL QSCLEQDTVC
HFSLNPRCNC RDAYTHLQYG LPEIHCQQMG DSLCHKCAST AGGFVQIQSS VAPLKASHQA
AEGLLHPAQH MLPPGMQNSR PRNFFLHSVQ HFQAQENLGR TSTHSTDERL PRTAELSPPP
SDSRSTESFQ RACCHPENNQ RRLCKSRDPG DTEGSGGTKS KVSGLPNQTD KEEKQVEPSL
LQTDETVNSE HLNHNESNFT FSHLPGEAGC RSCPNSPQSC RSIMRSKCGT EDCQTPNLEA
NVPAVPTHSD LSGESLLIKT L
