ID   TRI17_HUMAN             Reviewed;         477 AA.
AC   Q9Y577; B4DVJ2; Q5VST8;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 191.
DE   RecName: Full=E3 ubiquitin-protein ligase TRIM17;
DE            EC=2.3.2.27;
DE   AltName: Full=RING finger protein 16;
DE   AltName: Full=RING-type E3 ubiquitin transferase TRIM17 {ECO:0000305};
DE   AltName: Full=Testis RING finger protein;
DE   AltName: Full=Tripartite motif-containing protein 17;
GN   Name=TRIM17; Synonyms=RBCC, RNF16, TERF;
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] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=9792805; DOI=10.1006/bbrc.1998.9502;
RA   Ogawa S., Goto W., Orimo A., Hosoi T., Ouchi Y., Muramatsu M., Inoue S.;
RT   "Molecular cloning of a novel RING finger-B box-coiled coil (RBCC) protein,
RT   terf, expressed in the testis.";
RL   Biochem. Biophys. Res. Commun. 251:515-519(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Spleen;
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=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   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   FUNCTION, TISSUE SPECIFICITY, AUTOUBIQUITINATION, AND INTERACTION WITH
RP   TRIM44.
RX   PubMed=19358823; DOI=10.1016/j.bbrc.2009.04.010;
RA   Urano T., Usui T., Takeda S., Ikeda K., Okada A., Ishida Y., Iwayanagi T.,
RA   Otomo J., Ouchi Y., Inoue S.;
RT   "TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3 ligase.";
RL   Biochem. Biophys. Res. Commun. 383:263-268(2009).
RN   [6]
RP   FUNCTION.
RX   PubMed=22023800; DOI=10.1093/jb/mvr128;
RA   Endo H., Ikeda K., Urano T., Horie-Inoue K., Inoue S.;
RT   "Terf/TRIM17 stimulates degradation of kinetochore protein ZWINT and
RT   regulates cell proliferation.";
RL   J. Biochem. 151:139-144(2012).
RN   [7]
RP   FUNCTION IN AUTOPHAGY, SUBCELLULAR LOCATION, AND INTERACTION WITH BECN1.
RX   PubMed=27562068; DOI=10.1242/jcs.190017;
RA   Mandell M.A., Jain A., Kumar S., Castleman M.J., Anwar T., Eskelinen E.L.,
RA   Johansen T., Prekeris R., Deretic V.;
RT   "TRIM17 contributes to autophagy of midbodies while actively sparing other
RT   targets from degradation.";
RL   J. Cell Sci. 129:3562-3573(2016).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH TRIM28.
RX   PubMed=30042493; DOI=10.1038/s41418-018-0169-5;
RA   Lionnard L., Duc P., Brennan M.S., Kueh A.J., Pal M., Guardia F., Mojsa B.,
RA   Damiano M.A., Mora S., Lassot I., Ravichandran R., Cochet C.,
RA   Aouacheria A., Potts P.R., Herold M.J., Desagher S., Kucharczak J.;
RT   "TRIM17 and TRIM28 antagonistically regulate the ubiquitination and anti-
RT   apoptotic activity of BCL2A1.";
RL   Cell Death Differ. 26:902-917(2019).
CC   -!- FUNCTION: E3 ubiquitin ligase that plays important roles in the
CC       regulation of neuronal apoptosis, selective autophagy or cell
CC       proliferation (PubMed:22023800, PubMed:19358823, PubMed:27562068).
CC       Stimulates the degradation of kinetochore ZW10 interacting protein
CC       ZWINT in a proteasome-dependent manner, leading to negative regulation
CC       of cell proliferation (PubMed:22023800). Inhibits autophagic
CC       degradation of diverse known targets while contributing to autophagy of
CC       midbodies. Autophagy-inhibitory activity involves MCL1, which TRIM17
CC       assembles into complexes with the key autophagy regulator BECN1
CC       (PubMed:27562068). Controls neuronal apoptosis by mediating
CC       ubiquitination and degradation of MCL1 to initiate neuronal death. In
CC       addition, regulates NFAT transcription factors NFATC3 and NFATC4
CC       activities by preventing their nuclear localization, thus inhibiting
CC       their transcriptional activities. Decreases TRIM41-mediated degradation
CC       of ZSCAN2 thereby stimulating alpha-synuclein/SNCA transcription in
CC       neuronal cells (By similarity). Prevents the E3 ubiquitin-ligase
CC       activity of TRIM28 and its interaction with anti-apoptotic BCL2A1,
CC       blocking TRIM28 from ubiquitinating BCL2A1 (PubMed:19358823).
CC       {ECO:0000250|UniProtKB:Q7TPM3, ECO:0000269|PubMed:19358823,
CC       ECO:0000269|PubMed:22023800, ECO:0000269|PubMed:27562068}.
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;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts (via coiled coil) with TRIM44 (via coiled coil)
CC       (PubMed:19358823). Interacts with TRIM28; this interaction prevents
CC       TRIM28 activity on BCL2A1 (PubMed:30042493). Interacts with TRIM41;
CC       this interaction prevents TRIM41 activity on ZSCAN2 (By similarity).
CC       Interacts with BECN1 (PubMed:27562068). Interacts with NFATC3 and
CC       NFATC4; these interactions prevent NFATC3 and NFATC4 nuclear
CC       localization (By similarity). {ECO:0000250|UniProtKB:Q7TPM3,
CC       ECO:0000269|PubMed:19358823, ECO:0000269|PubMed:27562068,
CC       ECO:0000269|PubMed:30042493}.
CC   -!- INTERACTION:
CC       Q9Y577; O14964: HGS; NbExp=6; IntAct=EBI-743894, EBI-740220;
CC       Q9Y577; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-743894, EBI-16439278;
CC       Q9Y577; Q9HCM9: TRIM39; NbExp=8; IntAct=EBI-743894, EBI-739510;
CC       Q9Y577; Q8WV44: TRIM41; NbExp=4; IntAct=EBI-743894, EBI-725997;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27562068}. Lysosome
CC       {ECO:0000269|PubMed:27562068}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y577-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y577-2; Sequence=VSP_040994, VSP_040995;
CC   -!- TISSUE SPECIFICITY: Almost exclusively in the testis.
CC       {ECO:0000269|PubMed:19358823}.
CC   -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:19358823}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR   EMBL; AF156271; AAD40286.1; -; mRNA.
DR   EMBL; AK301105; BAG62704.1; -; mRNA.
DR   EMBL; AL670729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL139288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC033788; AAH33788.1; -; mRNA.
DR   CCDS; CCDS1571.1; -. [Q9Y577-1]
DR   CCDS; CCDS44327.1; -. [Q9Y577-2]
DR   RefSeq; NP_001020111.1; NM_001024940.2. [Q9Y577-1]
DR   RefSeq; NP_001128327.1; NM_001134855.1. [Q9Y577-2]
DR   RefSeq; NP_057186.1; NM_016102.3. [Q9Y577-1]
DR   RefSeq; XP_006711842.1; XM_006711779.2. [Q9Y577-1]
DR   RefSeq; XP_011542511.1; XM_011544209.2. [Q9Y577-1]
DR   RefSeq; XP_011542512.1; XM_011544210.2. [Q9Y577-1]
DR   AlphaFoldDB; Q9Y577; -.
DR   SMR; Q9Y577; -.
DR   BioGRID; 119314; 35.
DR   IntAct; Q9Y577; 25.
DR   STRING; 9606.ENSP00000355658; -.
DR   GlyGen; Q9Y577; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y577; -.
DR   PhosphoSitePlus; Q9Y577; -.
DR   BioMuta; TRIM17; -.
DR   DMDM; 38605530; -.
DR   MassIVE; Q9Y577; -.
DR   MaxQB; Q9Y577; -.
DR   PaxDb; 9606-ENSP00000355658; -.
DR   PeptideAtlas; Q9Y577; -.
DR   ProteomicsDB; 86309; -. [Q9Y577-1]
DR   ProteomicsDB; 86310; -. [Q9Y577-2]
DR   Antibodypedia; 20781; 192 antibodies from 25 providers.
DR   DNASU; 51127; -.
DR   Ensembl; ENST00000295033.7; ENSP00000295033.3; ENSG00000162931.12. [Q9Y577-1]
DR   Ensembl; ENST00000366697.6; ENSP00000355658.2; ENSG00000162931.12. [Q9Y577-1]
DR   Ensembl; ENST00000366698.7; ENSP00000355659.2; ENSG00000162931.12. [Q9Y577-1]
DR   Ensembl; ENST00000456946.6; ENSP00000403312.2; ENSG00000162931.12. [Q9Y577-2]
DR   GeneID; 51127; -.
DR   KEGG; hsa:51127; -.
DR   MANE-Select; ENST00000366698.7; ENSP00000355659.2; NM_016102.4; NP_057186.1.
DR   UCSC; uc001hsu.4; human. [Q9Y577-1]
DR   AGR; HGNC:13430; -.
DR   CTD; 51127; -.
DR   DisGeNET; 51127; -.
DR   GeneCards; TRIM17; -.
DR   HGNC; HGNC:13430; TRIM17.
DR   HPA; ENSG00000162931; Group enriched (brain, testis).
DR   MIM; 606123; gene.
DR   neXtProt; NX_Q9Y577; -.
DR   OpenTargets; ENSG00000162931; -.
DR   PharmGKB; PA37768; -.
DR   VEuPathDB; HostDB:ENSG00000162931; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000162155; -.
DR   HOGENOM; CLU_013137_0_3_1; -.
DR   InParanoid; Q9Y577; -.
DR   OMA; YPCVVGQ; -.
DR   OrthoDB; 3453019at2759; -.
DR   PhylomeDB; Q9Y577; -.
DR   TreeFam; TF338674; -.
DR   PathwayCommons; Q9Y577; -.
DR   Reactome; R-HSA-877300; Interferon gamma signaling.
DR   SignaLink; Q9Y577; -.
DR   SIGNOR; Q9Y577; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 51127; 13 hits in 1181 CRISPR screens.
DR   GenomeRNAi; 51127; -.
DR   Pharos; Q9Y577; Tbio.
DR   PRO; PR:Q9Y577; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9Y577; Protein.
DR   Bgee; ENSG00000162931; Expressed in right hemisphere of cerebellum and 98 other cell types or tissues.
DR   ExpressionAtlas; Q9Y577; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IDA:UniProtKB.
DR   GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR   CDD; cd19762; Bbox2_TRIM7-like; 1.
DR   CDD; cd16595; RING-HC_TRIM17_C-IV; 1.
DR   CDD; cd15812; SPRY_PRY_TRIM17; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR035687; TRIM17_PRY/SPRY.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR   PANTHER; PTHR24103:SF397; E3 UBIQUITIN-PROTEIN LIGASE TRIM17; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; Q9Y577; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Lysosome; Metal-binding;
KW   Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..477
FT                   /note="E3 ubiquitin-protein ligase TRIM17"
FT                   /id="PRO_0000056224"
FT   DOMAIN          277..475
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         16..66
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         94..135
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   COILED          135..223
FT                   /evidence="ECO:0000255"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   VAR_SEQ         295..343
FT                   /note="EDVVPDATSAYPYLLLYESRQRRYLGSSPEGSGFCSKDRFVAYPCAVGQ ->
FT                   GKWAPRARTSDPGSLGDAPLYPLASEATNGGGSTSALPGDGHWLFTVPS (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040994"
FT   VAR_SEQ         344..477
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040995"
SQ   SEQUENCE   477 AA;  54418 MW;  ECA4010661ADD28A CRC64;
     MEAVELARKL QEEATCSICL DYFTDPVMTT CGHNFCRACI QLSWEKARGK KGRRKRKGSF
     PCPECREMSP QRNLLPNRLL TKVAEMAQQH PGLQKQDLCQ EHHEPLKLFC QKDQSPICVV
     CRESREHRLH RVLPAEEAVQ GYKLKLEEDM EYLREQITRT GNLQAREEQS LAEWQGKVKE
     RRERIVLEFE KMNLYLVEEE QRLLQALETE EEETASRLRE SVACLDRQGH SLELLLLQLE
     ERSTQGPLQM LQDMKEPLSR KNNVSVQCPE VAPPTRPRTV CRVPGQIEVL RGFLEDVVPD
     ATSAYPYLLL YESRQRRYLG SSPEGSGFCS KDRFVAYPCA VGQTAFSSGR HYWEVGMNIT
     GDALWALGVC RDNVSRKDRV PKCPENGFWV VQLSKGTKYL STFSALTPVM LMEPPSHMGI
     FLDFEAGEVS FYSVSDGSHL HTYSQATFPG PLQPFFCLGA PKSGQMVIST VTMWVKG
//