ID   LTN1_HUMAN              Reviewed;        1766 AA.
AC   O94822; A6NL41; A7E2D0; B2RTS0; C9J7U3; J3KPL4; Q05C47; Q9H8M4; Q9NUY5;
AC   Q9P0E9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 6.
DT   28-JAN-2026, entry version 214.
DE   RecName: Full=E3 ubiquitin-protein ligase listerin;
DE            EC=2.3.2.27 {ECO:0000305|PubMed:25578875};
DE   AltName: Full=RING finger protein 160;
DE   AltName: Full=RING-type E3 ubiquitin transferase listerin {ECO:0000305};
DE   AltName: Full=Zinc finger protein 294;
GN   Name=LTN1; Synonyms=C21orf10, C21orf98, KIAA0714, RNF160, ZNF294;
GN   ORFNames=HSPC087;
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] (ISOFORM 1), AND VARIANT SER-403.
RC   TISSUE=Brain;
RX   PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XI. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:277-286(1998).
RN   [2]
RP   SEQUENCE REVISION.
RA   Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-403.
RC   TISSUE=Bone marrow;
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 [LARGE SCALE MRNA] OF 1-696 (ISOFORM 1), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 73-1766 (ISOFORM 2), AND VARIANT SER-403.
RC   TISSUE=Placenta;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-473 (ISOFORM 1), AND VARIANT
RP   SER-403.
RC   TISSUE=Umbilical cord blood;
RA   Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA   Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT   "Human partial CDS from CD34+ stem cells.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-108 (ISOFORM 3).
RC   TISSUE=Testis;
RA   Arakawa T., Carninci P., Fukuda S., Hasegawa A., Hayashida K., Hori F.,
RA   Kai C., Kawai J., Kojima M., Murata M., Nakamura M., Nishiyori H.,
RA   Nomura K., Ohno M., Sasaki D., Shibazaki E., Tagami M., Tagami Y.,
RA   Hayashizaki Y.;
RT   "RIKEN full-length enriched human cDNA library.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [8]
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   [9]
RP   FUNCTION.
RX   PubMed=23685075; DOI=10.1016/j.molcel.2013.04.015;
RA   Shao S., von der Malsburg K., Hegde R.S.;
RT   "Listerin-dependent nascent protein ubiquitination relies on ribosome
RT   subunit dissociation.";
RL   Mol. Cell 50:637-648(2013).
RN   [10]
RP   FUNCTION.
RX   PubMed=25132172; DOI=10.1016/j.molcel.2014.07.006;
RA   Shao S., Hegde R.S.;
RT   "Reconstitution of a minimal ribosome-associated ubiquitination pathway
RT   with purified factors.";
RL   Mol. Cell 55:880-890(2014).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=28757607; DOI=10.1038/s41467-017-00188-1;
RA   Matsuo Y., Ikeuchi K., Saeki Y., Iwasaki S., Schmidt C., Udagawa T.,
RA   Sato F., Tsuchiya H., Becker T., Tanaka K., Ingolia N.T., Beckmann R.,
RA   Inada T.;
RT   "Ubiquitination of stalled ribosome triggers ribosome-associated quality
RT   control.";
RL   Nat. Commun. 8:159-159(2017).
RN   [12] {ECO:0007744|PDB:3J92}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) AS PART OF THE RIBOSOME
RP   QUALITY CONTROL COMPLEX, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   SUBUNIT.
RX   PubMed=25578875; DOI=10.1016/j.molcel.2014.12.015;
RA   Shao S., Brown A., Santhanam B., Hegde R.S.;
RT   "Structure and assembly pathway of the ribosome quality control complex.";
RL   Mol. Cell 57:433-444(2015).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase component of the ribosome quality
CC       control complex (RQC), a ribosome-associated complex that mediates
CC       ubiquitination and extraction of incompletely synthesized nascent
CC       chains for proteasomal degradation (PubMed:23685075, PubMed:25132172,
CC       PubMed:25578875, PubMed:28757607). Within the RQC complex, LTN1 is
CC       recruited to stalled 60S ribosomal subunits by NEMF and mediates
CC       ubiquitination of stalled nascent chains (PubMed:25578875).
CC       Ubiquitination leads to VCP/p97 recruitment for extraction and
CC       degradation of the incomplete translation product (By similarity).
CC       {ECO:0000250|UniProtKB:Q04781, ECO:0000269|PubMed:23685075,
CC       ECO:0000269|PubMed:25132172, ECO:0000269|PubMed:25578875,
CC       ECO:0000269|PubMed:28757607}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000305|PubMed:25578875};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000269|PubMed:25578875}.
CC   -!- SUBUNIT: Component of the ribosome quality control complex (RQC),
CC       composed of the E3 ubiquitin ligase LTN1, TCF25 and NEMF associated
CC       with the 60S ribosomal subunit (PubMed:25578875). The complex probably
CC       also contains VCP/p97 and its ubiquitin-binding cofactors (By
CC       similarity). {ECO:0000250|UniProtKB:Q04781,
CC       ECO:0000269|PubMed:25578875}.
CC   -!- INTERACTION:
CC       O94822; Q92985: IRF7; NbExp=2; IntAct=EBI-1044684, EBI-968267;
CC       O94822; Q86WV6: STING1; NbExp=2; IntAct=EBI-1044684, EBI-2800345;
CC       O94822; P58753: TIRAP; NbExp=2; IntAct=EBI-1044684, EBI-528644;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28757607}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O94822-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O94822-2; Sequence=VSP_040138;
CC       Name=3;
CC         IsoId=O94822-3; Sequence=VSP_044911;
CC   -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q6A009}.
CC   -!- SIMILARITY: Belongs to the LTN1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF28910.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAH29371.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=BAA34434.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA91976.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB90430.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB018257; BAA34434.2; ALT_INIT; mRNA.
DR   EMBL; AF129075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF260011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL163248; CAB90429.3; -; Genomic_DNA.
DR   EMBL; AL163249; CAB90430.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC029371; AAH29371.1; ALT_SEQ; mRNA.
DR   EMBL; BC140790; AAI40791.1; -; mRNA.
DR   EMBL; BC150284; AAI50285.1; -; mRNA.
DR   EMBL; AK001915; BAA91976.1; ALT_INIT; mRNA.
DR   EMBL; AK023499; BAB14589.1; -; mRNA.
DR   EMBL; AF161350; AAF28910.1; ALT_FRAME; mRNA.
DR   EMBL; DB452437; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS33527.3; -. [O94822-1]
DR   RefSeq; NP_056380.3; NM_015565.3. [O94822-1]
DR   PDB; 3J92; EM; 3.60 A; 0/w/z=1-1766.
DR   PDB; 9GY4; EM; 3.00 A; F=1-1766.
DR   PDBsum; 3J92; -.
DR   PDBsum; 9GY4; -.
DR   AlphaFoldDB; O94822; -.
DR   EMDB; EMD-2832; -.
DR   EMDB; EMD-51681; -.
DR   SMR; O94822; -.
DR   BioGRID; 117509; 240.
DR   ComplexPortal; CPX-2656; Ribosome quality control complex.
DR   FunCoup; O94822; 3222.
DR   IntAct; O94822; 133.
DR   MINT; O94822; -.
DR   STRING; 9606.ENSP00000478783; -.
DR   GlyCosmos; O94822; 3 sites, 2 glycans.
DR   GlyGen; O94822; 3 sites, 2 O-linked glycans (3 sites).
DR   iPTMnet; O94822; -.
DR   PhosphoSitePlus; O94822; -.
DR   SwissPalm; O94822; -.
DR   BioMuta; LTN1; -.
DR   jPOST; O94822; -.
DR   MassIVE; O94822; -.
DR   PaxDb; 9606-ENSP00000478783; -.
DR   PeptideAtlas; O94822; -.
DR   ProteomicsDB; 50463; -. [O94822-1]
DR   ProteomicsDB; 50464; -. [O94822-2]
DR   Pumba; O94822; -.
DR   Antibodypedia; 41917; 125 antibodies from 20 providers.
DR   DNASU; 26046; -.
DR   Ensembl; ENST00000361371.10; ENSP00000354977.4; ENSG00000198862.15. [O94822-1]
DR   Ensembl; ENST00000389194.7; ENSP00000373846.3; ENSG00000198862.15. [O94822-1]
DR   Ensembl; ENST00000614971.4; ENSP00000478783.1; ENSG00000198862.15. [O94822-3]
DR   Ensembl; ENST00000707893.1; ENSP00000517021.1; ENSG00000291534.1. [O94822-1]
DR   Ensembl; ENST00000707894.1; ENSP00000517022.1; ENSG00000291534.1. [O94822-1]
DR   Ensembl; ENST00000707899.1; ENSP00000517025.1; ENSG00000291534.1. [O94822-3]
DR   GeneID; 26046; -.
DR   KEGG; hsa:26046; -.
DR   MANE-Select; ENST00000361371.10; ENSP00000354977.4; NM_015565.3; NP_056380.3.
DR   UCSC; uc002ymr.2; human. [O94822-1]
DR   AGR; HGNC:13082; -.
DR   ClinPGx; PA37658; -.
DR   CTD; 26046; -.
DR   DisGeNET; 26046; -.
DR   GeneCards; LTN1; -.
DR   HGNC; HGNC:13082; LTN1.
DR   HPA; ENSG00000198862; Low tissue specificity.
DR   MIM; 613083; gene.
DR   OpenTargets; ENSG00000198862; -.
DR   VEuPathDB; HostDB:ENSG00000198862; -.
DR   eggNOG; KOG0803; Eukaryota.
DR   GeneTree; ENSGT00390000016055; -.
DR   HOGENOM; CLU_002412_0_0_1; -.
DR   InParanoid; O94822; -.
DR   OMA; IYGSHWE; -.
DR   OrthoDB; 6108at2759; -.
DR   PAN-GO; O94822; 6 GO annotations based on evolutionary models.
DR   PhylomeDB; O94822; -.
DR   PathwayCommons; O94822; -.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; O94822; -.
DR   SIGNOR; O94822; -.
DR   UniPathway; UPA00143; -.
DR   Agora; ENSG00000198862; -.
DR   BioGRID-ORCS; 26046; 16 hits in 1191 CRISPR screens.
DR   ChiTaRS; LTN1; human.
DR   GenomeRNAi; 26046; -.
DR   Pharos; O94822; Tbio.
DR   PRO; PR:O94822; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; O94822; protein.
DR   Bgee; ENSG00000198862; Expressed in secondary oocyte and 213 other cell types or tissues.
DR   ExpressionAtlas; O94822; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0022626; C:cytosolic ribosome; IDA:UniProt.
DR   GO; GO:1990112; C:RQC complex; IDA:UniProtKB.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProt.
DR   GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   CDD; cd16491; RING-CH-C4HC3_LTN1; 1.
DR   FunFam; 3.30.40.10:FF:000038; E3 ubiquitin-protein ligase listerin; 1.
DR   FunFam; 1.25.10.10:FF:001251; Predicted protein; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039795; LTN1/Rkr1.
DR   InterPro; IPR054477; LTN1_E3_ligase_6th.
DR   InterPro; IPR056241; LTN1_HEAT_5th.
DR   InterPro; IPR054476; Ltn1_N.
DR   InterPro; IPR054478; LTN1_UBC.
DR   InterPro; IPR039804; RING-CH-C4HC3_LTN1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12389:SF0; E3 UBIQUITIN-PROTEIN LIGASE LISTERIN; 1.
DR   PANTHER; PTHR12389; ZINC FINGER PROTEIN 294; 1.
DR   Pfam; PF22958; Ltn1_1st; 1.
DR   Pfam; PF24618; LTN1_E3_ligase_5th; 1.
DR   Pfam; PF22999; LTN1_E3_ligase_6th; 1.
DR   Pfam; PF23009; UBC_like; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Metal-binding;
KW   Proteomics identification; Reference proteome; Repeat; Transferase;
KW   Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..1766
FT                   /note="E3 ubiquitin-protein ligase listerin"
FT                   /id="PRO_0000056304"
FT   REPEAT          59..96
FT                   /note="HEAT 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          100..138
FT                   /note="HEAT 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          273..314
FT                   /note="HEAT 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          335..372
FT                   /note="HEAT 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          380..418
FT                   /note="HEAT 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          433..473
FT                   /note="HEAT 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          513..551
FT                   /note="HEAT 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          611..658
FT                   /note="HEAT 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          676..714
FT                   /note="HEAT 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          768..810
FT                   /note="HEAT 10"
FT                   /evidence="ECO:0000255"
FT   REPEAT          911..949
FT                   /note="HEAT 11"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1068..1105
FT                   /note="HEAT 12"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1184..1227
FT                   /note="HEAT 13"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1314..1352
FT                   /note="HEAT 14"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1377..1414
FT                   /note="HEAT 15"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1475..1512
FT                   /note="HEAT 16"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         1715..1762
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   VAR_SEQ         1
FT                   /note="M -> MDRVGGGKGPGGSYYRVSSSAARSRKLCPGRVNRGLSAQSTAATATM
FT                   (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.7"
FT                   /id="VSP_044911"
FT   VAR_SEQ         438..1766
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040138"
FT   VARIANT         403
FT                   /note="L -> S (in dbSNP:rs2254796)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9872452,
FT                   ECO:0000269|Ref.6"
FT                   /id="VAR_020957"
FT   VARIANT         500
FT                   /note="A -> V (in dbSNP:rs16983580)"
FT                   /id="VAR_057218"
FT   VARIANT         565
FT                   /note="G -> C (in dbSNP:rs34191159)"
FT                   /id="VAR_057219"
FT   VARIANT         761
FT                   /note="V -> I (in dbSNP:rs34635840)"
FT                   /id="VAR_057220"
FT   CONFLICT        1
FT                   /note="M -> K (in Ref. 5; BAA91976)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="R -> T (in Ref. 7; DB452437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133
FT                   /note="I -> T (in Ref. 5; BAA91976)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="A -> G (in Ref. 6; AAF28910)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150
FT                   /note="Y -> D (in Ref. 5; BAB14589)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        372
FT                   /note="Q -> H (in Ref. 5; BAB14589/BAA91976)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        413
FT                   /note="F -> Y (in Ref. 5; BAA91976)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1766 AA;  200552 MW;  9312CB2283C50AEE CRC64;
     MGGKNKQRTK GNLRPSNSGR AAELLAKEQG TVPGFIGFGT SQSDLGYVPA IQGAEEIDSL
     VDSDFRMVLR KLSKKDVTTK LKAMQEFGTM CTERDTETVK GVLPYWPRIF CKISLDHDRR
     VREATQQAFE KLILKVKKQL APYLKSLMGY WLMAQCDTYT PAAFAAKDAF EAAFPPSKQP
     EAIAFCKDEI TSVLQDHLIK ETPDTLSDPQ TVPEEEREAK FYRVVTCSLL ALKRLLCLLP
     DNELDSLEEK FKSLLSQNKF WKYGKHSVPQ IRSAYFELVS ALCQRIPQLM KEEASKVSPS
     VLLSIDDSDP IVCPALWEAV LYTLTTIEDC WLHVNAKKSV FPKLSTVIRE GGRGLATVIY
     PYLLPFISKL PQSITNPKLD FFKNFLTSLV AGLSTERTKT SSLESSAVIS AFFECLRFIM
     QQNLGEEEIE QMLVNDQLIP FIDAVLKDPG LQHGQLFNHL AETLSSWEAK ADTEKDEKTA
     HNLENVLIHF WERLSEICVA KISEPEADVE SVLGVSNLLQ VLQKPKSSLK SSKKKNGKVR
     FADEILESNK ENEKCVSSEG EKIEGWELTT EPSLTHNSSG LLSPLRKKPL EDLVCKLADI
     SINYVNERKS EQHLRFLSTL LDSFSSSRVF KMLLGDEKQS IVQAKPLEIA KLVQKNPAVQ
     FLYQKLIGWL NEDQRKDFGF LVDILYSALR CCDNDMERKK VLDDLTKVDL KWNSLLKIIE
     KACPSSDKHA LVTPWLKGDI LGEKLVNLAD CLCNEDLESR VSSESHFSER WTLLSLVLSQ
     HVKNDYLIGD VYVERIIVRL HETLFKTKKL SEAESSDSSV SFICDVAYNY FSSAKGCLLM
     PSSEDLLLTL FQLCAQSKEK THLPDFLICK LKNTWLSGVN LLVHQTDSSY KESTFLHLSA
     LWLKNQVQAS SLDINSLQVL LSAVDDLLNT LLESEDSYLM GVYIGSVMPN DSEWEKMRQS
     LPMQWLHRPL LEGRLSLNYE CFKTDFKEQD IKTLPSHLCT SALLSKMVLI ALRKETVLEN
     NELEKIIAEL LYSLQWCEEL DNPPIFLIGF CEILQKMNIT YDNLRVLGNT SGLLQLLFNR
     SREHGTLWSL IIAKLILSRS ISSDEVKPHY KRKESFFPLT EGNLHTIQSL CPFLSKEEKK
     EFSAQCIPAL LGWTKKDLCS TNGGFGHLAI FNSCLQTKSI DDGELLHGIL KIIISWKKEH
     EDIFLFSCNL SEASPEVLGV NIEIIRFLSL FLKYCSSPLA ESEWDFIMCS MLAWLETTSE
     NQALYSIPLV QLFACVSCDL ACDLSAFFDS TTLDTIGNLP VNLISEWKEF FSQGIHSLLL
     PILVTVTGEN KDVSETSFQN AMLKPMCETL TYISKEQLLS HKLPARLVAD QKTNLPEYLQ
     TLLNTLAPLL LFRARPVQIA VYHMLYKLMP ELPQYDQDNL KSYGDEEEEP ALSPPAALMS
     LLSIQEDLLE NVLGCIPVGQ IVTIKPLSED FCYVLGYLLT WKLILTFFKA ASSQLRALYS
     MYLRKTKSLN KLLYHLFRLM PENPTYAETA VEVPNKDPKT FFTEELQLSI RETTMLPYHI
     PHLACSVYHM TLKDLPAMVR LWWNSSEKRV FNIVDRFTSK YVSSVLSFQE ISSVQTSTQL
     FNGMTVKARA TTREVMATYT IEDIVIELII QLPSNYPLGS IIVESGKRVG VAVQQWRNWM
     LQLSTYLTHQ NGSIMEGLAL WKNNVDKRFE GVEDCMICFS VIHGFNYSLP KKACRTCKKK
     FHSACLYKWF TSSNKSTCPL CRETFF
//