RT4I1_HUMAN
ID RT4I1_HUMAN Reviewed; 396 AA.
AC Q8WWV3; Q8N9B3; Q8WZ66; Q9BRA4;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Reticulon-4-interacting protein 1, mitochondrial;
DE AltName: Full=NOGO-interacting mitochondrial protein;
DE Flags: Precursor;
GN Name=RTN4IP1; Synonyms=NIMP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain;
RA Jin W.-L., Hou B., Long M., Li R., Ju G.;
RT "Cloning and expression of the human NOGO-interacting mitochondrial
RT protein.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
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, AND SUBCELLULAR LOCATION.
RX PubMed=12067236; DOI=10.1046/j.1471-4159.2002.00788.x;
RA Hu W.-H., Hausmann O.N., Yan M.-S., Walters W.M., Wong P.K.Y., Bethea J.R.;
RT "Identification and characterization of a novel Nogo-interacting
RT mitochondrial protein (NIMP).";
RL J. Neurochem. 81:36-45(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER SER-40, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [8]
RP VARIANT OPA10 HIS-103, AND SUBCELLULAR LOCATION.
RX PubMed=26593267; DOI=10.1016/j.ajhg.2015.09.012;
RA Angebault C., Guichet P.O., Talmat-Amar Y., Charif M., Gerber S.,
RA Fares-Taie L., Gueguen N., Halloy F., Moore D., Amati-Bonneau P., Manes G.,
RA Hebrard M., Bocquet B., Quiles M., Piro-Megy C., Teigell M., Delettre C.,
RA Rossel M., Meunier I., Preising M., Lorenz B., Carelli V., Chinnery P.F.,
RA Yu-Wai-Man P., Kaplan J., Roubertie A., Barakat A., Bonneau D., Reynier P.,
RA Rozet J.M., Bomont P., Hamel C.P., Lenaers G.;
RT "Recessive mutations in RTN4IP1 cause isolated and syndromic optic
RT neuropathies.";
RL Am. J. Hum. Genet. 97:754-760(2015).
CC -!- FUNCTION: Plays a role in the regulation of retinal ganglion cell (RGC)
CC neurite outgrowth, and hence in the development of the inner retina and
CC optic nerve. Appears to be a potent inhibitor of regeneration following
CC spinal cord injury. {ECO:0000250|UniProtKB:Q924D0}.
CC -!- SUBUNIT: Interacts with RTN4, UQCRC1 and UQCRC2. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8WWV3; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-743502, EBI-2875816;
CC Q8WWV3; Q9BS16: CENPK; NbExp=3; IntAct=EBI-743502, EBI-6871750;
CC Q8WWV3; P78358: CTAG1B; NbExp=6; IntAct=EBI-743502, EBI-1188472;
CC Q8WWV3; Q8TAM6: ERMN; NbExp=3; IntAct=EBI-743502, EBI-2681068;
CC Q8WWV3; Q9UJY4: GGA2; NbExp=3; IntAct=EBI-743502, EBI-447646;
CC Q8WWV3; Q7Z353: HDX; NbExp=3; IntAct=EBI-743502, EBI-1052734;
CC Q8WWV3; Q9NX47: MARCHF5; NbExp=3; IntAct=EBI-743502, EBI-2341610;
CC Q8WWV3; Q12972-2: PPP1R8; NbExp=3; IntAct=EBI-743502, EBI-12252736;
CC Q8WWV3; Q9BRP8: PYM1; NbExp=3; IntAct=EBI-743502, EBI-2352802;
CC Q8WWV3; Q96CP1: RELA; NbExp=5; IntAct=EBI-743502, EBI-10489476;
CC Q8WWV3; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-743502, EBI-11984663;
CC Q8WWV3; Q9H7N4: SCAF1; NbExp=3; IntAct=EBI-743502, EBI-1222181;
CC Q8WWV3; Q9HAU4: SMURF2; NbExp=3; IntAct=EBI-743502, EBI-396727;
CC Q8WWV3; Q9BX66-7: SORBS1; NbExp=3; IntAct=EBI-743502, EBI-17775963;
CC Q8WWV3; Q9GZV5: WWTR1; NbExp=3; IntAct=EBI-743502, EBI-747743;
CC Q8WWV3; Q15942: ZYX; NbExp=5; IntAct=EBI-743502, EBI-444225;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:12067236, ECO:0000269|PubMed:26593267}.
CC Note=Colocalizes with the endoplasmic reticulum HSPA5 at spots
CC corresponding to contacts with mitochondria.
CC {ECO:0000269|PubMed:26593267}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WWV3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WWV3-2; Sequence=VSP_015742;
CC Name=3; Synonyms=Short;
CC IsoId=Q8WWV3-3; Sequence=VSP_015743, VSP_015744;
CC -!- TISSUE SPECIFICITY: Widely expressed in mitochondria-enriched tissues.
CC Found in heart, muscle, kidney, liver, brain and placenta.
CC {ECO:0000269|PubMed:12067236}.
CC -!- DISEASE: Optic atrophy 10 with or without ataxia, intellectual
CC disability, and seizures (OPA10) [MIM:616732]: An autosomal recessive
CC disease characterized by progressive visual loss in association with
CC optic atrophy. Atrophy of the optic disk indicates a deficiency in the
CC number of nerve fibers which arise in the retina and converge to form
CC the optic disk, optic nerve, optic chiasm and optic tracts. OPA10
CC patients may also manifest mild ataxia, mild intellectual disability
CC and, rarely, generalized seizures. {ECO:0000269|PubMed:26593267}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; AF439711; AAL34525.1; -; mRNA.
DR EMBL; AY063761; AAL40856.1; -; mRNA.
DR EMBL; AK095207; BAC04499.1; -; mRNA.
DR EMBL; AL390074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006399; AAH06399.2; -; mRNA.
DR CCDS; CCDS5056.1; -. [Q8WWV3-1]
DR RefSeq; NP_001305675.1; NM_001318746.1. [Q8WWV3-2]
DR RefSeq; NP_116119.2; NM_032730.5. [Q8WWV3-1]
DR PDB; 2VN8; X-ray; 2.10 A; A/B=45-396.
DR PDBsum; 2VN8; -.
DR AlphaFoldDB; Q8WWV3; -.
DR SMR; Q8WWV3; -.
DR BioGRID; 124276; 88.
DR IntAct; Q8WWV3; 36.
DR MINT; Q8WWV3; -.
DR STRING; 9606.ENSP00000358059; -.
DR GlyGen; Q8WWV3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WWV3; -.
DR PhosphoSitePlus; Q8WWV3; -.
DR BioMuta; RTN4IP1; -.
DR DMDM; 76789669; -.
DR EPD; Q8WWV3; -.
DR jPOST; Q8WWV3; -.
DR MassIVE; Q8WWV3; -.
DR MaxQB; Q8WWV3; -.
DR PaxDb; Q8WWV3; -.
DR PeptideAtlas; Q8WWV3; -.
DR PRIDE; Q8WWV3; -.
DR ProteomicsDB; 74937; -. [Q8WWV3-1]
DR ProteomicsDB; 74938; -. [Q8WWV3-2]
DR ProteomicsDB; 74939; -. [Q8WWV3-3]
DR Antibodypedia; 32150; 244 antibodies from 23 providers.
DR DNASU; 84816; -.
DR Ensembl; ENST00000369063.8; ENSP00000358059.3; ENSG00000130347.13. [Q8WWV3-1]
DR GeneID; 84816; -.
DR KEGG; hsa:84816; -.
DR MANE-Select; ENST00000369063.8; ENSP00000358059.3; NM_032730.5; NP_116119.2.
DR UCSC; uc003prj.4; human. [Q8WWV3-1]
DR CTD; 84816; -.
DR DisGeNET; 84816; -.
DR GeneCards; RTN4IP1; -.
DR HGNC; HGNC:18647; RTN4IP1.
DR HPA; ENSG00000130347; Low tissue specificity.
DR MalaCards; RTN4IP1; -.
DR MIM; 610502; gene.
DR MIM; 616732; phenotype.
DR neXtProt; NX_Q8WWV3; -.
DR OpenTargets; ENSG00000130347; -.
DR Orphanet; 98676; Autosomal recessive isolated optic atrophy.
DR PharmGKB; PA38619; -.
DR VEuPathDB; HostDB:ENSG00000130347; -.
DR eggNOG; KOG1198; Eukaryota.
DR GeneTree; ENSGT00880000138028; -.
DR HOGENOM; CLU_026673_3_3_1; -.
DR InParanoid; Q8WWV3; -.
DR OMA; TSWQALK; -.
DR OrthoDB; 727365at2759; -.
DR PhylomeDB; Q8WWV3; -.
DR TreeFam; TF313919; -.
DR PathwayCommons; Q8WWV3; -.
DR SignaLink; Q8WWV3; -.
DR BioGRID-ORCS; 84816; 85 hits in 1081 CRISPR screens.
DR ChiTaRS; RTN4IP1; human.
DR EvolutionaryTrace; Q8WWV3; -.
DR GenomeRNAi; 84816; -.
DR Pharos; Q8WWV3; Tbio.
DR PRO; PR:Q8WWV3; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8WWV3; protein.
DR Bgee; ENSG00000130347; Expressed in secondary oocyte and 153 other tissues.
DR ExpressionAtlas; Q8WWV3; baseline and differential.
DR Genevisible; Q8WWV3; HS.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0050773; P:regulation of dendrite development; ISS:UniProtKB.
DR CDD; cd08248; RTN4I1; 1.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR InterPro; IPR037397; RTN4I1.
DR Pfam; PF08240; ADH_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Neurogenesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:25944712"
FT CHAIN 41..396
FT /note="Reticulon-4-interacting protein 1, mitochondrial"
FT /id="PRO_0000042114"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015742"
FT VAR_SEQ 208..226
FT /note="VLILGASGGVGTFAIQVMK -> ISGKESIIAGHFSWPVAH (in
FT isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_015743"
FT VAR_SEQ 227..396
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_015744"
FT VARIANT 103
FT /note="R -> H (in OPA10; dbSNP:rs372054380)"
FT /evidence="ECO:0000269|PubMed:26593267"
FT /id="VAR_076369"
FT CONFLICT 65
FT /note="M -> V (in Ref. 1; AAL34525)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="N -> Y (in Ref. 1; AAL40856)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="N -> S (in Ref. 2; BAC04499)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="P -> S (in Ref. 1; AAL34525)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="M -> T (in Ref. 1; AAL40856)"
FT /evidence="ECO:0000305"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 73..83
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:2VN8"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:2VN8"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:2VN8"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:2VN8"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 304..311
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 313..333
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 347..358
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:2VN8"
FT HELIX 375..384
FT /evidence="ECO:0007829|PDB:2VN8"
FT STRAND 388..394
FT /evidence="ECO:0007829|PDB:2VN8"
SQ SEQUENCE 396 AA; 43590 MW; DF173BF75A86E39B CRC64;
MEFLKTCVLR RNACTAVCFW RSKVVQKPSV RRISTTSPRS TVMPAWVIDK YGKNEVLRFT
QNMMMPIIHY PNEVIVKVHA ASVNPIDVNM RSGYGATALN MKRDPLHVKI KGEEFPLTLG
RDVSGVVMEC GLDVKYFKPG DEVWAAVPPW KQGTLSEFVV VSGNEVSHKP KSLTHTQAAS
LPYVALTAWS AINKVGGLND KNCTGKRVLI LGASGGVGTF AIQVMKAWDA HVTAVCSQDA
SELVRKLGAD DVIDYKSGSV EEQLKSLKPF DFILDNVGGS TETWAPDFLK KWSGATYVTL
VTPFLLNMDR LGIADGMLQT GVTVGSKALK HFWKGVHYRW AFFMASGPCL DDIAELVDAG
KIRPVIEQTF PFSKVPEAFL KVERGHARGK TVINVV
