R144B_HUMAN
ID R144B_HUMAN Reviewed; 303 AA.
AC Q7Z419; B3KUA8; B4DZI2; Q5TB85; Q6P4Q0; Q8N3R7; Q9BX38;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=E3 ubiquitin-protein ligase RNF144B;
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:O60260};
DE AltName: Full=IBR domain-containing protein 2;
DE AltName: Full=RING finger protein 144B;
DE AltName: Full=p53-inducible RING finger protein;
GN Name=RNF144B; Synonyms=IBRDC2, P53RFP;
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), FUNCTION, AND INTERACTION WITH
RP LCMT2.
RX PubMed=12853982; DOI=10.1038/sj.onc.1206586;
RA Ng C.-C., Arakawa H., Fukuda S., Kondoh H., Nakamura Y.;
RT "p53RFP, a p53-inducible RING-finger protein, regulates the stability of
RT p21WAF1.";
RL Oncogene 22:4449-4458(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Prostate, and Testis;
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 MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
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 [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 TISSUE SPECIFICITY, AND INTERACTION WITH UBE2L3 AND UBE2L6.
RX PubMed=16427630; DOI=10.1016/j.febslet.2005.09.105;
RA Huang J., Xu L.-G., Liu T., Zhai Z., Shu H.-B.;
RT "The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent
RT apoptosis.";
RL FEBS Lett. 580:940-947(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP BAX.
RX PubMed=20300062; DOI=10.1038/emboj.2010.39;
RA Benard G., Neutzner A., Peng G., Wang C., Livak F., Youle R.J.,
RA Karbowski M.;
RT "IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax
RT and apoptosis activation.";
RL EMBO J. 29:1458-1471(2010).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2
CC ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a
CC thioester and then directly transfers the ubiquitin to targeted
CC substrates such as LCMT2, thereby promoting their degradation. Induces
CC apoptosis via a p53/TP53-dependent but caspase-independent mechanism.
CC However, its overexpression also produces a decrease of the ubiquitin-
CC dependent stability of BAX, a pro-apoptotic protein, ultimately leading
CC to protection of cell death; But, it is not an anti-apoptotic protein
CC per se. {ECO:0000269|PubMed:12853982, ECO:0000269|PubMed:20300062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:O60260};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with UBE2L3, UBE2L6 and LCMT2, as well as with BAX.
CC {ECO:0000269|PubMed:12853982, ECO:0000269|PubMed:16427630,
CC ECO:0000269|PubMed:20300062}.
CC -!- INTERACTION:
CC Q7Z419; Q07812: BAX; NbExp=5; IntAct=EBI-2129982, EBI-516580;
CC Q7Z419; O15350: TP73; NbExp=2; IntAct=EBI-2129982, EBI-389606;
CC Q7Z419; O15350-8: TP73; NbExp=2; IntAct=EBI-2129982, EBI-5651259;
CC Q7Z419; O14933: UBE2L6; NbExp=4; IntAct=EBI-2129982, EBI-2129974;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:20300062}; Single-pass membrane protein
CC {ECO:0000269|PubMed:20300062}. Cytoplasm {ECO:0000269|PubMed:20300062}.
CC Note=Mostly cytosololic, accumulates in submitochondrial domains
CC specifically upon apoptosis induction, in synchrony with BAX
CC activation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z419-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z419-2; Sequence=VSP_055853, VSP_055854;
CC -!- TISSUE SPECIFICITY: Broadly expressed, with lowest levels in brain and
CC thymus, and highest levels detectable in heart, ovary and testis.
CC {ECO:0000269|PubMed:16427630, ECO:0000269|PubMed:20300062}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme (By similarity). The transmembrane domain
CC is essential for translocation to the mitochondria upon induction of
CC apoptosis. {ECO:0000250}.
CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC interact with the E2 conjugating enzyme UBE2L3 and function like HECT-
CC type E3 enzymes: they bind E2s via the first RING domain, but require
CC an obligate trans-thiolation step during the ubiquitin transfer,
CC requiring a conserved cysteine residue in the second RING domain.
CC {ECO:0000250|UniProtKB:O60260}.
CC -!- PTM: Auto-ubiquitinated.
CC -!- SIMILARITY: Belongs to the RBR family. RNF144 subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks the His residue in the RING-type domain 2 that is one of
CC the conserved features of the family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD38622.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB076367; BAC02434.1; -; mRNA.
DR EMBL; AK096832; BAG53370.1; -; mRNA.
DR EMBL; AK302935; BAG64094.1; -; mRNA.
DR EMBL; AL832329; CAD38622.1; ALT_INIT; mRNA.
DR EMBL; AL138725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55407.1; -; Genomic_DNA.
DR EMBL; BC063311; AAH63311.1; -; mRNA.
DR CCDS; CCDS34345.1; -. [Q7Z419-1]
DR RefSeq; NP_877434.2; NM_182757.3. [Q7Z419-1]
DR AlphaFoldDB; Q7Z419; -.
DR SMR; Q7Z419; -.
DR BioGRID; 129106; 37.
DR DIP; DIP-43771N; -.
DR IntAct; Q7Z419; 11.
DR MINT; Q7Z419; -.
DR STRING; 9606.ENSP00000259939; -.
DR iPTMnet; Q7Z419; -.
DR PhosphoSitePlus; Q7Z419; -.
DR BioMuta; RNF144B; -.
DR DMDM; 57012811; -.
DR MassIVE; Q7Z419; -.
DR PaxDb; Q7Z419; -.
DR PeptideAtlas; Q7Z419; -.
DR PRIDE; Q7Z419; -.
DR ProteomicsDB; 69130; -. [Q7Z419-1]
DR Antibodypedia; 2130; 420 antibodies from 27 providers.
DR DNASU; 255488; -.
DR Ensembl; ENST00000259939.4; ENSP00000259939.4; ENSG00000137393.10. [Q7Z419-1]
DR GeneID; 255488; -.
DR KEGG; hsa:255488; -.
DR MANE-Select; ENST00000259939.4; ENSP00000259939.4; NM_182757.4; NP_877434.2.
DR UCSC; uc003ncs.3; human. [Q7Z419-1]
DR CTD; 255488; -.
DR DisGeNET; 255488; -.
DR GeneCards; RNF144B; -.
DR HGNC; HGNC:21578; RNF144B.
DR HPA; ENSG00000137393; Tissue enhanced (skeletal).
DR MIM; 618869; gene.
DR neXtProt; NX_Q7Z419; -.
DR OpenTargets; ENSG00000137393; -.
DR PharmGKB; PA162401565; -.
DR VEuPathDB; HostDB:ENSG00000137393; -.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00940000158819; -.
DR HOGENOM; CLU_053598_1_0_1; -.
DR InParanoid; Q7Z419; -.
DR OMA; PQRTWCP; -.
DR OrthoDB; 1188714at2759; -.
DR PhylomeDB; Q7Z419; -.
DR TreeFam; TF324777; -.
DR PathwayCommons; Q7Z419; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q7Z419; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 255488; 38 hits in 1116 CRISPR screens.
DR ChiTaRS; RNF144B; human.
DR GenomeRNAi; 255488; -.
DR Pharos; Q7Z419; Tbio.
DR PRO; PR:Q7Z419; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q7Z419; protein.
DR Bgee; ENSG00000137393; Expressed in deltoid and 181 other tissues.
DR Genevisible; Q7Z419; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; PTHR11685; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cytoplasm; Membrane; Metal-binding;
KW Mitochondrion; Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..303
FT /note="E3 ubiquitin-protein ligase RNF144B"
FT /id="PRO_0000055911"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 30..80
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 101..166
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 193..222
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 26..244
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ACT_SITE 206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT VAR_SEQ 1..21
FT /note="MGSAGRLHYLAMTAENPTPGD -> MLWITMPHPAHLGLFIAVTLS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055853"
FT VAR_SEQ 22..110
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055854"
FT CONFLICT 262
FT /note="L -> P (in Ref. 3; CAD38622)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="Missing (in Ref. 6; AAH63311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 33697 MW; 9FD505CDFB70B6A5 CRC64;
MGSAGRLHYL AMTAENPTPG DLAPAPLITC KLCLCEQSLD KMTTLQECQC IFCTACLKQY
MQLAIREGCG SPITCPDMVC LNHGTLQEAE IACLVPVDQF QLYQRLKFER EVHLDPYRTW
CPVADCQTVC PVASSDPGQP VLVECPSCHL KFCSCCKDAW HAEVSCRDSQ PIVLPTEHRA
LFGTDAEAPI KQCPVCRVYI ERNEGCAQMM CKNCKHTFCW YCLQNLDNDI FLRHYDKGPC
RNKLGHSRAS VMWNRTQVVG ILVGLGIIAL VTSPLLLLAS PCIICCVCKS CRGKKKKHDP
STT
