ID   SKI3_HUMAN              Reviewed;        1564 AA.
AC   Q6PGP7; O15077; Q6PJI3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Superkiller complex protein 3 {ECO:0000305};
DE            Short=Ski3 {ECO:0000303|PubMed:32006463};
DE   AltName: Full=Tetratricopeptide repeat protein 37;
DE            Short=TPR repeat protein 37;
DE   AltName: Full=Tricho-hepatic-enteric syndrome protein {ECO:0000303|PubMed:20176027};
DE            Short=Thespin {ECO:0000303|PubMed:20176027};
GN   Name=SKIC3 {ECO:0000312|HGNC:HGNC:23639};
GN   Synonyms=KIAA0372 {ECO:0000303|PubMed:9205841}, TTC37
GN   {ECO:0000303|PubMed:21120949};
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 [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA   Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VII. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 4:141-150(1997).
RN   [2]
RP   SEQUENCE REVISION.
RA   Ohara O., Nagase T., Kikuno R., Nomura N.;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung carcinoma, and Melanoma;
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   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PAF1, AND IDENTIFICATION
RP   IN THE SKI COMPLEX.
RX   PubMed=16024656; DOI=10.1101/gad.1292105;
RA   Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H., Batra S.K.,
RA   Tempst P., Reinberg D.;
RT   "The human PAF complex coordinates transcription with events downstream of
RT   RNA synthesis.";
RL   Genes Dev. 19:1668-1673(2005).
RN   [5]
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   [6]
RP   TISSUE SPECIFICITY, VARIANTS 860-ASN--GLU-878 DEL; ASP-1077; ALA-1270 AND
RP   ARG-1485, AND ASSOCIATION WITH THES1.
RX   PubMed=21120949; DOI=10.1002/humu.21420;
RA   Fabre A., Martinez-Vinson C., Roquelaure B., Missirian C., Andre N.,
RA   Breton A., Lachaux A., Odul E., Colomb V., Lemale J., Cezard J.P.,
RA   Goulet O., Sarles J., Levy N., Badens C.;
RT   "Novel mutations in TTC37 associated with Tricho-Hepato-Enteric syndrome.";
RL   Hum. Mutat. 32:277-281(2011).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9]
RP   VARIANTS THES1 ARG-251; ASN-1283 AND SER-1505.
RX   PubMed=20176027; DOI=10.1053/j.gastro.2010.02.010;
RA   Hartley J.L., Zachos N.C., Dawood B., Donowitz M., Forman J., Pollitt R.J.,
RA   Morgan N.V., Tee L., Gissen P., Kahr W.H., Knisely A.S., Watson S.,
RA   Chitayat D., Booth I.W., Protheroe S., Murphy S., de Vries E., Kelly D.A.,
RA   Maher E.R.;
RT   "Mutations in TTC37 cause trichohepatoenteric syndrome (phenotypic diarrhea
RT   of infancy).";
RL   Gastroenterology 138:2388-2398(2010).
RN   [10]
RP   FUNCTION, AND IDENTIFICATION IN THE SKI COMPLEX.
RX   PubMed=32006463; DOI=10.1016/j.molcel.2020.01.011;
RA   Zinoviev A., Ayupov R.K., Abaeva I.S., Hellen C.U.T., Pestova T.V.;
RT   "Extraction of mRNA from stalled ribosomes by the Ski complex.";
RL   Mol. Cell 77:1340-1349(2020).
RN   [11] {ECO:0007744|PDB:7QDR, ECO:0007744|PDB:7QDS, ECO:0007744|PDB:7QDY, ECO:0007744|PDB:7QDZ}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) IN COMPLEX WITH SKIC2 AND
RP   SKIC8, FUNCTION, AND IDENTIFICATION IN THE SKI COMPLEX.
RX   PubMed=35120588; DOI=10.1016/j.molcel.2022.01.009;
RA   Koegel A., Keidel A., Bonneau F., Schaefer I.B., Conti E.;
RT   "The human SKI complex regulates channeling of ribosome-bound RNA to the
RT   exosome via an intrinsic gatekeeping mechanism.";
RL   Mol. Cell 82:756-769(2022).
CC   -!- FUNCTION: Component of the SKI complex, a multiprotein complex that
CC       assists the RNA-degrading exosome during the mRNA decay and quality-
CC       control pathways (PubMed:16024656, PubMed:32006463, PubMed:35120588).
CC       The SKI complex catalyzes mRNA extraction from 80S ribosomal complexes
CC       in the 3'-5' direction and channels mRNA to the cytosolic exosome for
CC       degradation (PubMed:32006463, PubMed:35120588). SKI-mediated extraction
CC       of mRNA from stalled ribosomes allow binding of the Pelota-HBS1L
CC       complex and subsequent ribosome disassembly by ABCE1 for ribosome
CC       recycling (PubMed:32006463). In the nucleus, the SKI complex associates
CC       with transcriptionally active genes in a manner dependent on PAF1
CC       complex (PAF1C) (PubMed:16024656). {ECO:0000269|PubMed:16024656,
CC       ECO:0000269|PubMed:32006463, ECO:0000269|PubMed:35120588}.
CC   -!- SUBUNIT: Component of the SKI complex which consists of SKIC2, SKIC3
CC       and SKIC8 (PubMed:16024656, PubMed:32006463, PubMed:35120588).
CC       Interacts with PAF1 (PubMed:16024656). {ECO:0000269|PubMed:16024656,
CC       ECO:0000269|PubMed:32006463, ECO:0000269|PubMed:35120588}.
CC   -!- INTERACTION:
CC       Q6PGP7; Q8N7H5: PAF1; NbExp=2; IntAct=EBI-6083436, EBI-2607770;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16024656}. Nucleus
CC       {ECO:0000269|PubMed:16024656}.
CC   -!- TISSUE SPECIFICITY: Widely expressed with the highest levels observed
CC       in vascular tissues, lymph node, pituitary, lung and intestine. Not
CC       expressed in the liver. {ECO:0000269|PubMed:21120949}.
CC   -!- DISEASE: Trichohepatoenteric syndrome 1 (THES1) [MIM:222470]: A
CC       syndrome characterized by intrauterine growth retardation, severe
CC       diarrhea in infancy requiring total parenteral nutrition, facial
CC       dysmorphism, immunodeficiency, and hair abnormalities, mostly
CC       trichorrhexis nodosa. Hepatic involvement contributes to the poor
CC       prognosis of affected patients. {ECO:0000269|PubMed:20176027}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the SKI3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA20827.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB002370; BAA20827.2; ALT_INIT; mRNA.
DR   EMBL; BC015163; AAH15163.1; -; mRNA.
DR   EMBL; BC056893; AAH56893.1; -; mRNA.
DR   CCDS; CCDS4072.1; -.
DR   RefSeq; NP_055454.1; NM_014639.3.
DR   PDB; 7QDR; EM; 3.70 A; B=1-1564.
DR   PDB; 7QDS; EM; 3.80 A; B=1-1564.
DR   PDB; 7QDY; EM; 3.10 A; B=1-1564.
DR   PDB; 7QDZ; EM; 3.60 A; B=1-1564.
DR   PDBsum; 7QDR; -.
DR   PDBsum; 7QDS; -.
DR   PDBsum; 7QDY; -.
DR   PDBsum; 7QDZ; -.
DR   AlphaFoldDB; Q6PGP7; -.
DR   EMDB; EMD-13923; -.
DR   EMDB; EMD-13925; -.
DR   EMDB; EMD-13927; -.
DR   EMDB; EMD-13928; -.
DR   SMR; Q6PGP7; -.
DR   BioGRID; 115010; 116.
DR   ComplexPortal; CPX-2736; SKI complex.
DR   CORUM; Q6PGP7; -.
DR   IntAct; Q6PGP7; 32.
DR   MINT; Q6PGP7; -.
DR   STRING; 9606.ENSP00000497948; -.
DR   GlyGen; Q6PGP7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6PGP7; -.
DR   PhosphoSitePlus; Q6PGP7; -.
DR   SwissPalm; Q6PGP7; -.
DR   BioMuta; TTC37; -.
DR   DMDM; 74758339; -.
DR   EPD; Q6PGP7; -.
DR   jPOST; Q6PGP7; -.
DR   MassIVE; Q6PGP7; -.
DR   MaxQB; Q6PGP7; -.
DR   PaxDb; 9606-ENSP00000351596; -.
DR   PeptideAtlas; Q6PGP7; -.
DR   ProteomicsDB; 67118; -.
DR   Pumba; Q6PGP7; -.
DR   Antibodypedia; 48952; 30 antibodies from 16 providers.
DR   DNASU; 9652; -.
DR   Ensembl; ENST00000358746.7; ENSP00000351596.3; ENSG00000198677.13.
DR   Ensembl; ENST00000649566.1; ENSP00000497948.1; ENSG00000198677.13.
DR   GeneID; 9652; -.
DR   KEGG; hsa:9652; -.
DR   MANE-Select; ENST00000358746.7; ENSP00000351596.3; NM_014639.4; NP_055454.1.
DR   UCSC; uc003klb.4; human.
DR   AGR; HGNC:23639; -.
DR   CTD; 9652; -.
DR   DisGeNET; 9652; -.
DR   GeneCards; SKIC3; -.
DR   GeneReviews; SKIC3; -.
DR   HGNC; HGNC:23639; SKIC3.
DR   HPA; ENSG00000198677; Low tissue specificity.
DR   MalaCards; SKIC3; -.
DR   MIM; 222470; phenotype.
DR   MIM; 614589; gene.
DR   neXtProt; NX_Q6PGP7; -.
DR   OpenTargets; ENSG00000198677; -.
DR   Orphanet; 84064; Syndromic diarrhea.
DR   PharmGKB; PA162407226; -.
DR   VEuPathDB; HostDB:ENSG00000198677; -.
DR   eggNOG; KOG1127; Eukaryota.
DR   GeneTree; ENSGT00390000016407; -.
DR   HOGENOM; CLU_003788_1_0_1; -.
DR   InParanoid; Q6PGP7; -.
DR   OMA; CQWELDP; -.
DR   OrthoDB; 3076611at2759; -.
DR   PhylomeDB; Q6PGP7; -.
DR   TreeFam; TF323569; -.
DR   PathwayCommons; Q6PGP7; -.
DR   Reactome; R-HSA-429958; mRNA decay by 3' to 5' exoribonuclease.
DR   SignaLink; Q6PGP7; -.
DR   BioGRID-ORCS; 9652; 40 hits in 1159 CRISPR screens.
DR   ChiTaRS; TTC37; human.
DR   GenomeRNAi; 9652; -.
DR   Pharos; Q6PGP7; Tbio.
DR   PRO; PR:Q6PGP7; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q6PGP7; Protein.
DR   Bgee; ENSG00000198677; Expressed in calcaneal tendon and 208 other cell types or tissues.
DR   ExpressionAtlas; Q6PGP7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0055087; C:Ski complex; IDA:UniProtKB.
DR   GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IDA:UniProtKB.
DR   GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 8.
DR   InterPro; IPR039226; Ski3/TTC37.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR15704; SUPERKILLER 3 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR15704:SF7; TETRATRICOPEPTIDE REPEAT PROTEIN 37; 1.
DR   Pfam; PF13432; TPR_16; 2.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF13181; TPR_8; 2.
DR   SMART; SM00028; TPR; 14.
DR   SUPFAM; SSF81901; HCP-like; 2.
DR   SUPFAM; SSF48452; TPR-like; 5.
DR   PROSITE; PS50005; TPR; 12.
DR   PROSITE; PS50293; TPR_REGION; 5.
DR   Genevisible; Q6PGP7; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW   TPR repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..1564
FT                   /note="Superkiller complex protein 3"
FT                   /id="PRO_0000251722"
FT   REPEAT          6..39
FT                   /note="TPR 1"
FT   REPEAT          40..73
FT                   /note="TPR 2"
FT   REPEAT          272..305
FT                   /note="TPR 3"
FT   REPEAT          307..339
FT                   /note="TPR 4"
FT   REPEAT          386..419
FT                   /note="TPR 5"
FT   REPEAT          420..453
FT                   /note="TPR 6"
FT   REPEAT          455..492
FT                   /note="TPR 7"
FT   REPEAT          493..527
FT                   /note="TPR 8"
FT   REPEAT          564..597
FT                   /note="TPR 9"
FT   REPEAT          598..631
FT                   /note="TPR 10"
FT   REPEAT          633..665
FT                   /note="TPR 11"
FT   REPEAT          679..713
FT                   /note="TPR 12"
FT   REPEAT          790..824
FT                   /note="TPR 13"
FT   REPEAT          826..860
FT                   /note="TPR 14"
FT   REPEAT          861..894
FT                   /note="TPR 15"
FT   REPEAT          980..1013
FT                   /note="TPR 16"
FT   REPEAT          1020..1054
FT                   /note="TPR 17"
FT   REPEAT          1056..1084
FT                   /note="TPR 18"
FT   REPEAT          1326..1359
FT                   /note="TPR 19"
FT   REPEAT          1400..1433
FT                   /note="TPR 20"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   VARIANT         251
FT                   /note="G -> R (in THES1; dbSNP:rs763816083)"
FT                   /evidence="ECO:0000269|PubMed:20176027"
FT                   /id="VAR_067957"
FT   VARIANT         437
FT                   /note="L -> V (in dbSNP:rs17084873)"
FT                   /id="VAR_027705"
FT   VARIANT         860..878
FT                   /note="Missing (found in a THES1 patient)"
FT                   /evidence="ECO:0000269|PubMed:21120949"
FT                   /id="VAR_065297"
FT   VARIANT         1077
FT                   /note="A -> D (found in a THES1 patient)"
FT                   /evidence="ECO:0000269|PubMed:21120949"
FT                   /id="VAR_065298"
FT   VARIANT         1270
FT                   /note="P -> A (found in a THES1 patient;
FT                   dbSNP:rs146627706)"
FT                   /evidence="ECO:0000269|PubMed:21120949"
FT                   /id="VAR_065299"
FT   VARIANT         1283
FT                   /note="D -> N (in THES1)"
FT                   /evidence="ECO:0000269|PubMed:20176027"
FT                   /id="VAR_067958"
FT   VARIANT         1296
FT                   /note="R -> S (in dbSNP:rs2303650)"
FT                   /id="VAR_027706"
FT   VARIANT         1485
FT                   /note="L -> R (found in a THES1 patient)"
FT                   /evidence="ECO:0000269|PubMed:21120949"
FT                   /id="VAR_065300"
FT   VARIANT         1505
FT                   /note="L -> S (in THES1; dbSNP:rs376720108)"
FT                   /evidence="ECO:0000269|PubMed:20176027"
FT                   /id="VAR_067959"
FT   HELIX           355..365
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           370..382
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           389..399
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   STRAND          403..405
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           406..415
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           422..435
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           439..451
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           457..469
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   TURN            470..472
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   TURN            476..479
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           480..488
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   STRAND          492..496
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           497..503
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           510..523
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           530..540
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           547..556
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           564..576
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           580..593
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           598..610
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           615..626
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           632..644
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           648..661
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           666..685
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           689..709
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           714..725
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   STRAND          732..734
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   STRAND          737..739
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           742..744
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   STRAND          751..753
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           755..772
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           776..795
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   STRAND          800..803
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           804..820
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           825..835
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   TURN            838..840
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           843..856
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           861..873
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           877..890
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           895..907
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           913..923
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           927..942
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           952..958
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           961..975
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           980..992
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           996..1009
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1017..1032
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1036..1044
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1051..1064
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1067..1079
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1085..1101
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1104..1115
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   STRAND          1117..1119
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1124..1134
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1138..1151
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1160..1171
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1177..1188
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1193..1205
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1211..1223
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1229..1243
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   STRAND          1251..1254
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1255..1265
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1270..1290
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1300..1312
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1318..1339
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1342..1355
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1362..1370
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   STRAND          1372..1374
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1383..1395
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1400..1413
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1416..1433
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1437..1455
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1463..1477
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1481..1493
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1499..1510
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1516..1532
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1536..1547
FT                   /evidence="ECO:0007829|PDB:7QDY"
FT   HELIX           1553..1562
FT                   /evidence="ECO:0007829|PDB:7QDY"
SQ   SEQUENCE   1564 AA;  175486 MW;  12D6B45B4A6F367A CRC64;
     MSSKEVKTAL KSARDAIRNK EYKEALKHCK TVLKQEKNNY NAWVFIGVAA AELEQPDQAQ
     SAYKKAAELE PDQLLAWQGL ANLYEKYNHI NAKDDLPGVY QKLLDLYESV DKQKWCDVCK
     KLVDLYYQEK KHLEVARTWH KLIKTRQEQG AENEELHQLW RKLTQFLAES TEDQNNETQQ
     LLFTAFENAL GLSDKIPSED HQVLYRHFIQ SLSKFPHESA RLKKACEGMI NIYPTVQYPL
     EVLCLHLIES GNLTDEGQQY CCRLVEMDSK SGPGLIGLGI KALQDKKYED AVRNLTEGLK
     ESPVCTSGWY HLAEAQVKMH RPKEAVLSCS QALKIVDNLG ASGNSLYQRN LCLHLKAEAL
     IKLSDYDSSE EAIRTLDQIS DADNIPGLLV LKSLAYRNKG SFDEAAKIME DLLSSYPDLA
     EVHALEALIH FTKKDYLQAE KCFQRALEKD TEVAEYHYQL GLTYWFMGEE TRKDKTKALT
     HFLKAARLDT YMGKVFCYLG HYYRDVVGDK NRARGCYRKA FELDDTDAES GAAAVDLSVE
     LEDMEMALAI LTTVTQKASA GTAKWAWLRR GLYYLKAGQH SQAVADLQAA LRADPKDFNC
     WESLGEAYLS RGGYTTALKS FTKASELNPE SIYSVFKVAA IQQILGKYKE AVAQYQMIIK
     KKEDYVPALK GLGECHLMMA KAALVDYLDG KAVDYIEKAL EYFTCALQHR ADVSCLWKLA
     GDACTCLYAV APSKVNVHVL GVLLGQKEGK QVLKKNELLH LGGRCYGRAL KLMSTSNTWC
     DLGINYYRQA QHLAETGSNM NDLKELLEKS LHCLKKAVRL DSNNHLYWNA LGVVACYSGI
     GNYALAQHCF IKSIQSEQIN AVAWTNLGVL YLTNENIEQA HEAFKMAQSL DPSYLMCWIG
     QALIAEAVGS YDTMDLFRHT TELNMHTEGA LGYAYWVCTT LQDKSNRETE LYQYNILQMN
     AIPAAQVILN KYVERIQNYA PAFTMLGYLN EHLQLKKEAA NAYQRAILLL QTAEDQDTYN
     VAIRNYGRLL CSTGEYDKAI QAFKSTPLEV LEDIIGFALA LFMKGLYKES SKAYERALSI
     VESEQDKAHI LTALAITEYK QGKTDVAKTL LFKCSILKEP TTESLQALCA LGLAMQDATL
     SKAALNELLK HIKHKDSNYQ RCLLTSAIYA LQGRSVAVQK QISKAVHSNP GDPALWSLLS
     RVVAQYAQRN AKGGVVAGNV AHILDSNHGK KALLYTAVNQ LAMGSSSAED EKNTALKTIQ
     KAALLSPGDP AIWAGLMAAC HADDKLALVN NTQPKRIDLY LALLSAVSAS IKDEKFFENY
     NQSLEKWSLS QAVTGLIDTG RISEAETLCT KNLKSNPDQP AVILLLRQVQ CKPLLESQKP
     LPDAVLEELQ KTVMSNSTSV PAWQWLAHVY QSQGMMRAAE MCYRKSLQLA SQRGSWSGKL
     SSLLRLALLA LKVCMANISN DHWPSLVQEA TTEALKLCFC PLAVLLQALL QFKRKMGARE
     TRRLLERVVY QPGYPKSIAS TARWYLLRHL YAKDDYELID VLVNNAKTHG DTRALELNQR
     LSSQ
//