MARH8_HUMAN
ID MARH8_HUMAN Reviewed; 291 AA.
AC Q5T0T0; B2R8E7; H0Y7C6; Q5T0S8; Q8TC72;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF8;
DE EC=2.3.2.27;
DE AltName: Full=Cellular modulator of immune recognition;
DE Short=c-MIR;
DE AltName: Full=Membrane-associated RING finger protein 8;
DE AltName: Full=Membrane-associated RING-CH protein VIII;
DE Short=MARCH-VIII;
DE AltName: Full=RING finger protein 178;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF8 {ECO:0000305};
GN Name=MARCHF8 {ECO:0000312|HGNC:HGNC:23356}; Synonyms=MARCH8, MIR, RNF178;
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], FUNCTION, INTERACTION WITH CD86, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12582153; DOI=10.1074/jbc.m211285200;
RA Goto E., Ishido S., Sato Y., Ohgimoto S., Ohgimoto K., Nagano-Fujii M.,
RA Hotta H.;
RT "c-MIR, a human E3 ubiquitin ligase, is a functional homolog of herpesvirus
RT proteins MIR1 and MIR2 and has similar activity.";
RL J. Biol. Chem. 278:14657-14668(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-266.
RC TISSUE=Testis;
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=14722266; DOI=10.1128/jvi.78.3.1109-1120.2004;
RA Bartee E., Mansouri M., Hovey Nerenberg B.T., Gouveia K., Frueh K.;
RT "Downregulation of major histocompatibility complex class I by human
RT ubiquitin ligases related to viral immune evasion proteins.";
RL J. Virol. 78:1109-1120(2004).
RN [7]
RP FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR BETA.
RX PubMed=18389477; DOI=10.1002/eji.200737902;
RA Thibodeau J., Bourgeois-Daigneault M.C., Huppe G., Tremblay J., Aumont A.,
RA Houde M., Bartee E., Brunet A., Gauvreau M.E., de Gassart A., Gatti E.,
RA Baril M., Cloutier M., Bontron S., Fruh K., Lamarre D., Steimle V.;
RT "Interleukin-10-induced MARCH1 mediates intracellular sequestration of MHC
RT class II in monocytes.";
RL Eur. J. Immunol. 38:1225-1230(2008).
RN [8]
RP FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR ALPHA AND BETA, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19117940; DOI=10.1074/jbc.m805736200;
RA Lapaque N., Jahnke M., Trowsdale J., Kelly A.P.;
RT "The HLA-DRalpha chain is modified by polyubiquitination.";
RL J. Biol. Chem. 284:7007-7016(2009).
RN [9]
RP FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR.
RX PubMed=19566897; DOI=10.1111/j.1600-0854.2009.00948.x;
RA Gauvreau M.E., Cote M.H., Bourgeois-Daigneault M.C., Rivard L.D., Xiu F.,
RA Brunet A., Shaw A., Steimle V., Thibodeau J.;
RT "Sorting of MHC class II molecules into exosomes through a ubiquitin-
RT independent pathway.";
RL Traffic 10:1518-1527(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP STRUCTURE BY NMR OF 65-136.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RING domain of the human cellular modulator of
RT immune recognition protein.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC CD86 and MHC class II proteins, such as HLA-DR alpha and beta, and
CC promotes their subsequent endocytosis and sorting to lysosomes via
CC multivesicular bodies. May also promote ubiquitination and endocytosis
CC of TFRC and FAS. {ECO:0000269|PubMed:12582153,
CC ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:18389477,
CC ECO:0000269|PubMed:19117940, ECO:0000269|PubMed:19566897}.
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 with CD86. {ECO:0000269|PubMed:12582153}.
CC -!- INTERACTION:
CC Q5T0T0; P36575-2: ARR3; NbExp=3; IntAct=EBI-14061946, EBI-11977533;
CC Q5T0T0; O43169: CYB5B; NbExp=3; IntAct=EBI-14061946, EBI-1058710;
CC Q5T0T0; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-14061946, EBI-11337888;
CC Q5T0T0; O14653: GOSR2; NbExp=3; IntAct=EBI-14061946, EBI-4401517;
CC Q5T0T0; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-14061946, EBI-2339195;
CC Q5T0T0; P63027: VAMP2; NbExp=3; IntAct=EBI-14061946, EBI-520113;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:19117940}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:14722266}; Multi-
CC pass membrane protein {ECO:0000255}. Early endosome membrane
CC {ECO:0000269|PubMed:14722266}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5T0T0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T0T0-2; Sequence=VSP_055697;
CC -!- TISSUE SPECIFICITY: Broadly expressed. Present in immature dendritic
CC cells (at protein level). {ECO:0000269|PubMed:12582153,
CC ECO:0000269|PubMed:14722266}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity.
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DR EMBL; AK313340; BAG36144.1; -; mRNA.
DR EMBL; AL445201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471160; EAW86647.1; -; Genomic_DNA.
DR EMBL; CH471160; EAW86648.1; -; Genomic_DNA.
DR EMBL; BC025394; AAH25394.1; -; mRNA.
DR EMBL; BC066988; AAH66988.1; -; mRNA.
DR CCDS; CCDS60519.1; -. [Q5T0T0-2]
DR CCDS; CCDS7213.1; -. [Q5T0T0-1]
DR RefSeq; NP_001002266.1; NM_001002266.2. [Q5T0T0-1]
DR RefSeq; NP_001269795.1; NM_001282866.1. [Q5T0T0-2]
DR RefSeq; NP_659458.2; NM_145021.5. [Q5T0T0-1]
DR RefSeq; XP_005271861.1; XM_005271804.2. [Q5T0T0-2]
DR RefSeq; XP_006717767.1; XM_006717704.2. [Q5T0T0-2]
DR RefSeq; XP_011537794.1; XM_011539492.2. [Q5T0T0-2]
DR RefSeq; XP_011537795.1; XM_011539493.2.
DR RefSeq; XP_011537796.1; XM_011539494.2.
DR RefSeq; XP_011537797.1; XM_011539495.1. [Q5T0T0-1]
DR RefSeq; XP_016871383.1; XM_017015894.1.
DR PDB; 2D8S; NMR; -; A=70-136.
DR PDBsum; 2D8S; -.
DR AlphaFoldDB; Q5T0T0; -.
DR BMRB; Q5T0T0; -.
DR SMR; Q5T0T0; -.
DR BioGRID; 128666; 47.
DR IntAct; Q5T0T0; 8.
DR iPTMnet; Q5T0T0; -.
DR PhosphoSitePlus; Q5T0T0; -.
DR BioMuta; MARCH8; -.
DR DMDM; 74744352; -.
DR MassIVE; Q5T0T0; -.
DR MaxQB; Q5T0T0; -.
DR PaxDb; Q5T0T0; -.
DR PeptideAtlas; Q5T0T0; -.
DR PRIDE; Q5T0T0; -.
DR ProteomicsDB; 35410; -.
DR ProteomicsDB; 64200; -. [Q5T0T0-1]
DR Antibodypedia; 3041; 167 antibodies from 32 providers.
DR DNASU; 220972; -.
DR Ensembl; ENST00000319836.7; ENSP00000317087.3; ENSG00000165406.16. [Q5T0T0-1]
DR Ensembl; ENST00000395769.6; ENSP00000379116.2; ENSG00000165406.16. [Q5T0T0-1]
DR Ensembl; ENST00000395771.7; ENSP00000379118.4; ENSG00000278545.4.
DR Ensembl; ENST00000453424.7; ENSP00000411848.2; ENSG00000165406.16. [Q5T0T0-2]
DR GeneID; 220972; -.
DR KEGG; hsa:220972; -.
DR MANE-Select; ENST00000453424.7; ENSP00000411848.2; NM_001282866.2; NP_001269795.1. [Q5T0T0-2]
DR UCSC; uc001jcf.5; human. [Q5T0T0-1]
DR CTD; 220972; -.
DR DisGeNET; 220972; -.
DR GeneCards; MARCHF8; -.
DR HGNC; HGNC:23356; MARCHF8.
DR HPA; ENSG00000165406; Low tissue specificity.
DR MIM; 613335; gene.
DR neXtProt; NX_Q5T0T0; -.
DR OpenTargets; ENSG00000165406; -.
DR PharmGKB; PA37370; -.
DR VEuPathDB; HostDB:ENSG00000165406; -.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT00940000158282; -.
DR HOGENOM; CLU_035042_1_0_1; -.
DR InParanoid; Q5T0T0; -.
DR OMA; INRFHQK; -.
DR OrthoDB; 1222747at2759; -.
DR PhylomeDB; Q5T0T0; -.
DR TreeFam; TF319557; -.
DR PathwayCommons; Q5T0T0; -.
DR SignaLink; Q5T0T0; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 220972; 5 hits in 1060 CRISPR screens.
DR ChiTaRS; MARCH8; human.
DR EvolutionaryTrace; Q5T0T0; -.
DR GenomeRNAi; 220972; -.
DR Pharos; Q5T0T0; Tbio.
DR PRO; PR:Q5T0T0; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5T0T0; protein.
DR Bgee; ENSG00000165406; Expressed in bone marrow cell and 107 other tissues.
DR ExpressionAtlas; Q5T0T0; baseline and differential.
DR Genevisible; Q5T0T0; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0042287; F:MHC protein 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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0002495; P:antigen processing and presentation of peptide antigen via MHC class II; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cytoplasmic vesicle;
KW Endosome; Immunity; Lysosome; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..291
FT /note="E3 ubiquitin-protein ligase MARCHF8"
FT /id="PRO_0000274370"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 72..133
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 22..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 79
FT /note="I -> ICSSSAVFSECCHHSSVQSAVVSKAPHCQSSLTQGLTVTVICKDTLQ
FT ASKRNSFGSEWAQALKPAKNTKARRTLKFSRSLNDVGEKAQDTSESFAYVERTCSEGKL
FT ILPQDTCLRTNRFHHKEKRTLNHKPLGNSKHSCVSCLSAGRSTASEVEAGKGGRPGLLL
FT EEKADGEATSRSRQLLQYLFSLSHGLSASSLHRFHELESCAARLHTAKSSSGLAGSMGF
FT CSDEMGDDDVFEDSTSAKLKSRVLRAPLCSTEKDSDLDCPSPFSEKLPPISPVSTSGDV
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055697"
FT VARIANT 92
FT /note="P -> S (in dbSNP:rs3764990)"
FT /id="VAR_030266"
FT VARIANT 266
FT /note="Y -> H (in dbSNP:rs7908745)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030267"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2D8S"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2D8S"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2D8S"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2D8S"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:2D8S"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2D8S"
SQ SEQUENCE 291 AA; 32965 MW; F45D9BFAA3889BB3 CRC64;
MSMPLHQISA IPSQDAISAR VYRSKTKEKE REEQNEKTLG HFMSHSSNIS KAGSPPSASA
PAPVSSFSRT SITPSSQDIC RICHCEGDDE SPLITPCHCT GSLHFVHQAC LQQWIKSSDT
RCCELCKYEF IMETKLKPLR KWEKLQMTSS ERRKIMCSVT FHVIAITCVV WSLYVLIDRT
AEEIKQGQAT GILEWPFWTK LVVVAIGFTG GLLFMYVQCK VYVQLWKRLK AYNRVIYVQN
CPETSKKNIF EKSPLTEPNF ENKHGYGICH SDTNSSCCTE PEDTGAEIIH V
