TRIM9_HUMAN
ID TRIM9_HUMAN Reviewed; 710 AA.
AC Q9C026; D3DSB7; D3DSB8; Q92557; Q96D24; Q96NI4; Q9C025; Q9C027;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM9;
DE EC=2.3.2.27 {ECO:0000269|PubMed:20085810};
DE AltName: Full=RING finger protein 91;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM9 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 9;
GN Name=TRIM9; Synonyms=KIAA0282, RNF91;
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), AND VARIANT PHE-653.
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-653.
RC TISSUE=Brain;
RX PubMed=9179496; DOI=10.1093/dnares/4.1.53;
RA Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA Nomura N.;
RT "Construction and characterization of human brain cDNA libraries suitable
RT for analysis of cDNA clones encoding relatively large proteins.";
RL DNA Res. 4:53-59(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Fetal brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND VARIANT
RP PHE-653.
RC TISSUE=Brain, and Uterus;
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCALIZATION, TISSUE
RP SPECIFICITY, AND AUTOUBIQUITINATION.
RX PubMed=20085810; DOI=10.1016/j.nbd.2010.01.007;
RA Tanji K., Kamitani T., Mori F., Kakita A., Takahashi H., Wakabayashi K.;
RT "TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in the
RT brain of Parkinson's disease and dementia with Lewy bodies.";
RL Neurobiol. Dis. 38:210-218(2010).
RN [8]
RP STRUCTURE BY NMR OF 437-534.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the FN3 domain of human tripartite motif protein
RT 9.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which ubiquitinates itself in
CC cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting
CC signal for proteasomal degradation. May play a role in regulation of
CC neuronal functions and may also participate in the formation or
CC breakdown of abnormal inclusions in neurodegenerative disorders. May
CC act as a regulator of synaptic vesicle exocytosis by controlling the
CC availability of SNAP25 for the SNARE complex formation.
CC {ECO:0000269|PubMed:20085810}.
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:0000269|PubMed:20085810};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:20085810}.
CC -!- SUBUNIT: Interacts with SNAP25. {ECO:0000250|UniProtKB:Q91ZY8}.
CC -!- INTERACTION:
CC Q9C026; Q9Y2T2: AP3M1; NbExp=3; IntAct=EBI-720828, EBI-2371151;
CC Q9C026; P05067: APP; NbExp=3; IntAct=EBI-720828, EBI-77613;
CC Q9C026; P54253: ATXN1; NbExp=6; IntAct=EBI-720828, EBI-930964;
CC Q9C026; B7Z3H4: BTRC; NbExp=3; IntAct=EBI-720828, EBI-16429269;
CC Q9C026; Q9Y297: BTRC; NbExp=7; IntAct=EBI-720828, EBI-307461;
CC Q9C026; P48730: CSNK1D; NbExp=3; IntAct=EBI-720828, EBI-751621;
CC Q9C026; Q2TBE0: CWF19L2; NbExp=6; IntAct=EBI-720828, EBI-5453285;
CC Q9C026; Q9UI08: EVL; NbExp=3; IntAct=EBI-720828, EBI-346653;
CC Q9C026; Q9UI08-2: EVL; NbExp=3; IntAct=EBI-720828, EBI-6448852;
CC Q9C026; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-720828, EBI-11986315;
CC Q9C026; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-720828, EBI-6658203;
CC Q9C026; Q969S9: GFM2; NbExp=3; IntAct=EBI-720828, EBI-2371750;
CC Q9C026; O60333-2: KIF1B; NbExp=3; IntAct=EBI-720828, EBI-10975473;
CC Q9C026; Q969V5: MUL1; NbExp=3; IntAct=EBI-720828, EBI-744120;
CC Q9C026; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-720828, EBI-10271199;
CC Q9C026; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-720828, EBI-741158;
CC Q9C026; Q9NZD8: SPG21; NbExp=6; IntAct=EBI-720828, EBI-742688;
CC Q9C026; Q13148: TARDBP; NbExp=6; IntAct=EBI-720828, EBI-372899;
CC Q9C026; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-720828, EBI-3918381;
CC Q9C026; Q68CQ4: UTP25; NbExp=3; IntAct=EBI-720828, EBI-747711;
CC Q9C026; P50552: VASP; NbExp=4; IntAct=EBI-720828, EBI-748201;
CC Q9C026-5; A0A0S2Z507: BTRC; NbExp=3; IntAct=EBI-16437499, EBI-16429247;
CC Q9C026-5; B7Z3H4: BTRC; NbExp=3; IntAct=EBI-16437499, EBI-16429269;
CC Q9C026-5; Q9Y297: BTRC; NbExp=4; IntAct=EBI-16437499, EBI-307461;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20085810}. Cell
CC projection, dendrite {ECO:0000269|PubMed:20085810}. Cytoplasmic
CC vesicle, secretory vesicle, synaptic vesicle
CC {ECO:0000250|UniProtKB:Q91ZY8}. Synapse {ECO:0000250|UniProtKB:Q91ZY8}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q91ZY8}. Note=Enriched
CC at synaptic terminals where it exists in a soluble form and a synaptic
CC vesicle-associated form. Associated with the cytoskeleton (By
CC similarity). Found in proximal dendrites of pyramidal neurons in the
CC cerebral cortex and hippocampus, and Purkinje cells in the cerebellum
CC (PubMed:20085810). {ECO:0000250|UniProtKB:Q91ZY8,
CC ECO:0000269|PubMed:20085810}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Beta;
CC IsoId=Q9C026-1; Sequence=Displayed;
CC Name=4;
CC IsoId=Q9C026-4; Sequence=VSP_007922, VSP_007923, VSP_007924;
CC Name=5;
CC IsoId=Q9C026-5; Sequence=VSP_007925, VSP_007926;
CC -!- TISSUE SPECIFICITY: Brain. Highly expressed in the cerebral cortex (at
CC protein level). Severely decreased in the affected brain areas in
CC Parkinson disease and dementia with Lewy bodies.
CC {ECO:0000269|PubMed:20085810}.
CC -!- DOMAIN: The coiled coil domain mediates the interaction with the N-
CC terminal t-SNARE domain of SNAP25. {ECO:0000250|UniProtKB:Q91ZY8}.
CC -!- PTM: Auto-ubiquitinated. Poly-ubiquitinated in cultured cells, whereas
CC it is monoubiquitinated in vitro. {ECO:0000269|PubMed:20085810}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to a competing donor splice
CC site, to exon inclusion and to intron retention. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG53490.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG53492.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA13398.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA13398.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF220036; AAG53490.1; ALT_FRAME; mRNA.
DR EMBL; AF220037; AAG53491.1; -; mRNA.
DR EMBL; AF220038; AAG53492.1; ALT_FRAME; mRNA.
DR EMBL; D87458; BAA13398.2; ALT_SEQ; mRNA.
DR EMBL; AK055388; BAB70913.1; -; mRNA.
DR EMBL; CH471078; EAW65680.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65681.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65682.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65684.1; -; Genomic_DNA.
DR EMBL; BC013414; AAH13414.1; -; mRNA.
DR EMBL; BC063872; AAH63872.1; -; mRNA.
DR CCDS; CCDS45105.1; -. [Q9C026-5]
DR CCDS; CCDS9703.1; -. [Q9C026-1]
DR RefSeq; NP_055978.4; NM_015163.5. [Q9C026-1]
DR RefSeq; NP_443210.1; NM_052978.4. [Q9C026-5]
DR RefSeq; XP_011534691.1; XM_011536389.2. [Q9C026-4]
DR RefSeq; XP_016876434.1; XM_017020945.1. [Q9C026-1]
DR PDB; 2DB8; NMR; -; A=439-534.
DR PDB; 7B2S; X-ray; 1.50 A; A=535-710.
DR PDBsum; 2DB8; -.
DR PDBsum; 7B2S; -.
DR AlphaFoldDB; Q9C026; -.
DR BMRB; Q9C026; -.
DR SMR; Q9C026; -.
DR BioGRID; 125280; 398.
DR IntAct; Q9C026; 52.
DR MINT; Q9C026; -.
DR STRING; 9606.ENSP00000298355; -.
DR iPTMnet; Q9C026; -.
DR PhosphoSitePlus; Q9C026; -.
DR BioMuta; TRIM9; -.
DR DMDM; 33516964; -.
DR REPRODUCTION-2DPAGE; Q9C026; -.
DR EPD; Q9C026; -.
DR jPOST; Q9C026; -.
DR MassIVE; Q9C026; -.
DR MaxQB; Q9C026; -.
DR PaxDb; Q9C026; -.
DR PeptideAtlas; Q9C026; -.
DR PRIDE; Q9C026; -.
DR ProteomicsDB; 79943; -. [Q9C026-1]
DR ProteomicsDB; 79944; -. [Q9C026-4]
DR ProteomicsDB; 79945; -. [Q9C026-5]
DR Antibodypedia; 10667; 505 antibodies from 25 providers.
DR DNASU; 114088; -.
DR Ensembl; ENST00000298355.7; ENSP00000298355.3; ENSG00000100505.14. [Q9C026-1]
DR Ensembl; ENST00000338969.9; ENSP00000342970.5; ENSG00000100505.14. [Q9C026-4]
DR Ensembl; ENST00000360392.4; ENSP00000353561.4; ENSG00000100505.14. [Q9C026-5]
DR GeneID; 114088; -.
DR KEGG; hsa:114088; -.
DR UCSC; uc001wyx.5; human. [Q9C026-1]
DR CTD; 114088; -.
DR DisGeNET; 114088; -.
DR GeneCards; TRIM9; -.
DR HGNC; HGNC:16288; TRIM9.
DR HPA; ENSG00000100505; Tissue enhanced (brain, retina).
DR MIM; 606555; gene.
DR neXtProt; NX_Q9C026; -.
DR OpenTargets; ENSG00000100505; -.
DR PharmGKB; PA38116; -.
DR VEuPathDB; HostDB:ENSG00000100505; -.
DR eggNOG; KOG4367; Eukaryota.
DR GeneTree; ENSGT00940000154071; -.
DR HOGENOM; CLU_013137_19_2_1; -.
DR InParanoid; Q9C026; -.
DR OMA; PDTICTI; -.
DR OrthoDB; 516512at2759; -.
DR PhylomeDB; Q9C026; -.
DR TreeFam; TF315216; -.
DR PathwayCommons; Q9C026; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9C026; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 114088; 29 hits in 1108 CRISPR screens.
DR ChiTaRS; TRIM9; human.
DR EvolutionaryTrace; Q9C026; -.
DR GeneWiki; TRIM9; -.
DR GenomeRNAi; 114088; -.
DR Pharos; Q9C026; Tbio.
DR PRO; PR:Q9C026; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9C026; protein.
DR Bgee; ENSG00000100505; Expressed in right hemisphere of cerebellum and 143 other tissues.
DR Genevisible; Q9C026; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003877; SPRY_dom.
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 Pfam; PF00041; fn3; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..710
FT /note="E3 ubiquitin-protein ligase TRIM9"
FT /id="PRO_0000056208"
FT DOMAIN 374..432
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT DOMAIN 440..535
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 533..702
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 10..50
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 163..212
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 224..266
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 273..340
FT /evidence="ECO:0000255"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C7M3"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C7M3"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C7M3"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C7M3"
FT VAR_SEQ 436..439
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007922"
FT VAR_SEQ 534
FT /note="E -> EDTDSEEQTLPFPVPSERLPLRRMSPFSSTLNLQPSFPGRSYFDFRS
FT SPHQLSLHSSLQSLNAPGCNFETQSAPYSQLVDIKKLLA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007923"
FT VAR_SEQ 535..550
FT /note="VAWFAFDPGSAHSDII -> GKALQQYPSERELRGI (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007925"
FT VAR_SEQ 551..710
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007926"
FT VAR_SEQ 692..710
FT /note="TLHTGLPVPDFYSSRASIA -> STLPLRLNSCCWLPVQRLPRAVQSNRREG
FT S (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007924"
FT VARIANT 653
FT /note="L -> F (in dbSNP:rs2275462)"
FT /evidence="ECO:0000269|PubMed:11331580,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9179496"
FT /id="VAR_016202"
FT CONFLICT 314
FT /note="A -> V (in Ref. 2; BAB70913)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="Q -> R (in Ref. 2; BAB70913)"
FT /evidence="ECO:0000305"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:2DB8"
FT STRAND 473..479
FT /evidence="ECO:0007829|PDB:2DB8"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:2DB8"
FT STRAND 488..494
FT /evidence="ECO:0007829|PDB:2DB8"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:2DB8"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:2DB8"
FT STRAND 510..516
FT /evidence="ECO:0007829|PDB:2DB8"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:7B2S"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:7B2S"
FT TURN 553..556
FT /evidence="ECO:0007829|PDB:7B2S"
FT STRAND 557..564
FT /evidence="ECO:0007829|PDB:7B2S"
FT STRAND 566..571
FT /evidence="ECO:0007829|PDB:7B2S"
FT STRAND 576..588
FT /evidence="ECO:0007829|PDB:7B2S"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:7B2S"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:7B2S"
FT STRAND 615..620
FT /evidence="ECO:0007829|PDB:7B2S"
FT STRAND 622..629
FT /evidence="ECO:0007829|PDB:7B2S"
FT STRAND 632..638
FT /evidence="ECO:0007829|PDB:7B2S"
FT STRAND 646..652
FT /evidence="ECO:0007829|PDB:7B2S"
FT TURN 653..656
FT /evidence="ECO:0007829|PDB:7B2S"
FT STRAND 657..662
FT /evidence="ECO:0007829|PDB:7B2S"
FT STRAND 679..685
FT /evidence="ECO:0007829|PDB:7B2S"
FT STRAND 689..694
FT /evidence="ECO:0007829|PDB:7B2S"
SQ SEQUENCE 710 AA; 79177 MW; AEAB24807C89D0E2 CRC64;
MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSH RAAGSGVSDY
DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPA THLSPALAPV
PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV
MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY
CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN
MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL
RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS
PLLQSIHQLD FVQVKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV PADGYILELD
DGNGGQFREV YVGKETMCTV DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEVAWFAF
DPGSAHSDII LSNDNLTVTC SSYDDRVVLG KTGFSKGIHY WELTVDRYDN HPDPAFGVAR
MDVMKDVMLG KDDKAWAMYV DNNRSWFMHN NSHTNRTEGG ITKGATIGVL LDLNRKNLTF
FINDEQQGPI AFDNVEGLFF PAVSLNRNVQ VTLHTGLPVP DFYSSRASIA
