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CDIP1_HUMAN
ID   CDIP1_HUMAN             Reviewed;         208 AA.
AC   Q9H305; A8K7M1; B4DFU1; B4DY75; D3DUD6; Q96ID8; Q9H0Q4; Q9P112;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Cell death-inducing p53-target protein 1;
DE   AltName: Full=Cell death involved p53-target;
DE   AltName: Full=Cell death-inducing protein;
DE   AltName: Full=LITAF-like protein;
DE   AltName: Full=Lipopolysaccharide-induced tumor necrosis factor-alpha-like protein;
DE   AltName: Full=Transmembrane protein I1;
GN   Name=CDIP1; Synonyms=C16orf5, CDIP, LITAFL;
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 TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10570909; DOI=10.1007/s100380050183;
RA   Bhalla K., Eyre H.J., Whitmore S.A., Sutherland G.R., Callen D.F.;
RT   "C16orf5, a novel proline-rich gene at 16p13.3, is highly expressed in the
RT   brain.";
RL   J. Hum. Genet. 44:383-387(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Zhou Y., Du G., Wang J., Yuan J., Qiang B.;
RT   "Cloning a novel human cDNA encoding a novel transmembrane protein.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND FUNCTION.
RX   PubMed=17599062; DOI=10.1038/sj.emboj.7601779;
RA   Brown L., Ongusaha P.P., Kim H.G., Nuti S., Mandinova A., Lee J.W.,
RA   Khosravi-Far R., Aaronson S.A., Lee S.W.;
RT   "CDIP, a novel pro-apoptotic gene, regulates TNFalpha-mediated apoptosis in
RT   a p53-dependent manner.";
RL   EMBO J. 26:3410-3422(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Amygdala, Spleen, 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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Amygdala;
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   [9]
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   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye, and Lung;
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   [11]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=27582497; DOI=10.1042/bcj20160657;
RA   Qin W., Wunderley L., Barrett A.L., High S., Woodman P.G.;
RT   "The Charcot Marie Tooth disease protein LITAF is a zinc-binding monotopic
RT   membrane protein.";
RL   Biochem. J. 473:3965-3978(2016).
CC   -!- FUNCTION: Acts as an important p53/TP53-apoptotic effector. Regulates
CC       TNF-alpha-mediated apoptosis in a p53/TP53-dependent manner.
CC       {ECO:0000269|PubMed:17599062}.
CC   -!- INTERACTION:
CC       Q9H305; Q96GG9: DCUN1D1; NbExp=3; IntAct=EBI-2876678, EBI-740086;
CC       Q9H305; Q6ICB0: DESI1; NbExp=4; IntAct=EBI-2876678, EBI-2806959;
CC       Q9H305; O95208-2: EPN2; NbExp=3; IntAct=EBI-2876678, EBI-12135243;
CC       Q9H305; O43561-2: LAT; NbExp=3; IntAct=EBI-2876678, EBI-8070286;
CC       Q9H305; P46934: NEDD4; NbExp=2; IntAct=EBI-2876678, EBI-726944;
CC       Q9H305; Q96DC9: OTUB2; NbExp=3; IntAct=EBI-2876678, EBI-746259;
CC       Q9H305; Q6GQQ9: OTUD7B; NbExp=3; IntAct=EBI-2876678, EBI-527784;
CC       Q9H305; Q15025: TNIP1; NbExp=4; IntAct=EBI-2876678, EBI-357849;
CC       Q9H305; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-2876678, EBI-74615;
CC       Q9H305; P0CG47: UBB; NbExp=3; IntAct=EBI-2876678, EBI-413034;
CC       Q9H305; P0CG48: UBC; NbExp=3; IntAct=EBI-2876678, EBI-3390054;
CC       Q9H305; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-2876678, EBI-741480;
CC       Q9H305; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2876678, EBI-947187;
CC       Q9H305; P46937: YAP1; NbExp=2; IntAct=EBI-2876678, EBI-1044059;
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000269|PubMed:27582497}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:27582497}; Cytoplasmic side
CC       {ECO:0000269|PubMed:27582497}. Lysosome membrane
CC       {ECO:0000269|PubMed:27582497}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:27582497}; Cytoplasmic side
CC       {ECO:0000269|PubMed:27582497}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9H305-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H305-2; Sequence=VSP_046929;
CC       Name=3;
CC         IsoId=Q9H305-3; Sequence=VSP_046928;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain. Expressed at lower level
CC       in heart, skeletal muscle, kidney, pancreas and liver. Weakly or not
CC       expressed in placenta and lung. {ECO:0000269|PubMed:10570909}.
CC   -!- INDUCTION: Up-regulated by p53/TP53. {ECO:0000269|PubMed:17599062}.
CC   -!- DOMAIN: The LITAF domain is stabilized by a bound zinc ion. The LITAF
CC       domain contains an amphipathic helix that mediates interaction with
CC       lipid membranes. {ECO:0000250|UniProtKB:Q99732}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to competing acceptor splice
CC       site. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CDIP1/LITAF family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF26619.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF131218; AAF26619.1; ALT_FRAME; mRNA.
DR   EMBL; AF195661; AAG35583.1; -; mRNA.
DR   EMBL; DQ167023; AAZ94626.1; -; mRNA.
DR   EMBL; AL136698; CAB66633.1; -; mRNA.
DR   EMBL; CR533446; CAG38477.1; -; mRNA.
DR   EMBL; AK292036; BAF84725.1; -; mRNA.
DR   EMBL; AK294257; BAG57552.1; -; mRNA.
DR   EMBL; AK302297; BAG63637.1; -; mRNA.
DR   EMBL; AL833853; CAD38712.1; -; mRNA.
DR   EMBL; AC007606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC023830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471112; EAW85291.1; -; Genomic_DNA.
DR   EMBL; CH471112; EAW85292.1; -; Genomic_DNA.
DR   EMBL; CH471112; EAW85293.1; -; Genomic_DNA.
DR   EMBL; CH471112; EAW85294.1; -; Genomic_DNA.
DR   EMBL; CH471112; EAW85296.1; -; Genomic_DNA.
DR   EMBL; BC002882; AAH02882.1; -; mRNA.
DR   EMBL; BC007604; AAH07604.1; -; mRNA.
DR   CCDS; CCDS42114.1; -. [Q9H305-1]
DR   CCDS; CCDS58419.1; -. [Q9H305-2]
DR   CCDS; CCDS58420.1; -. [Q9H305-3]
DR   RefSeq; NP_001185983.1; NM_001199054.1. [Q9H305-1]
DR   RefSeq; NP_001185984.1; NM_001199055.1. [Q9H305-2]
DR   RefSeq; NP_001185985.1; NM_001199056.1. [Q9H305-3]
DR   RefSeq; NP_037531.2; NM_013399.2. [Q9H305-1]
DR   AlphaFoldDB; Q9H305; -.
DR   BioGRID; 118998; 16.
DR   IntAct; Q9H305; 19.
DR   MINT; Q9H305; -.
DR   STRING; 9606.ENSP00000382508; -.
DR   iPTMnet; Q9H305; -.
DR   PhosphoSitePlus; Q9H305; -.
DR   SwissPalm; Q9H305; -.
DR   BioMuta; CDIP1; -.
DR   DMDM; 74733567; -.
DR   jPOST; Q9H305; -.
DR   MassIVE; Q9H305; -.
DR   MaxQB; Q9H305; -.
DR   PaxDb; Q9H305; -.
DR   PeptideAtlas; Q9H305; -.
DR   PRIDE; Q9H305; -.
DR   ProteomicsDB; 4079; -.
DR   ProteomicsDB; 5503; -.
DR   ProteomicsDB; 80639; -. [Q9H305-1]
DR   Antibodypedia; 24347; 78 antibodies from 21 providers.
DR   DNASU; 29965; -.
DR   Ensembl; ENST00000399599.7; ENSP00000382508.2; ENSG00000089486.17. [Q9H305-1]
DR   Ensembl; ENST00000562334.5; ENSP00000455050.1; ENSG00000089486.17. [Q9H305-3]
DR   Ensembl; ENST00000563332.6; ENSP00000454994.1; ENSG00000089486.17. [Q9H305-1]
DR   Ensembl; ENST00000563507.5; ENSP00000455462.1; ENSG00000089486.17. [Q9H305-2]
DR   Ensembl; ENST00000567695.6; ENSP00000457877.1; ENSG00000089486.17. [Q9H305-1]
DR   Ensembl; ENST00000611166.2; ENSP00000480842.1; ENSG00000274336.2. [Q9H305-1]
DR   Ensembl; ENST00000631859.1; ENSP00000488843.1; ENSG00000274336.2. [Q9H305-3]
DR   Ensembl; ENST00000632680.1; ENSP00000488474.1; ENSG00000274336.2. [Q9H305-1]
DR   Ensembl; ENST00000632937.1; ENSP00000488066.1; ENSG00000274336.2. [Q9H305-1]
DR   Ensembl; ENST00000633324.1; ENSP00000487657.1; ENSG00000274336.2. [Q9H305-2]
DR   GeneID; 29965; -.
DR   KEGG; hsa:29965; -.
DR   MANE-Select; ENST00000567695.6; ENSP00000457877.1; NM_013399.3; NP_037531.2.
DR   UCSC; uc002cwu.4; human. [Q9H305-1]
DR   CTD; 29965; -.
DR   DisGeNET; 29965; -.
DR   GeneCards; CDIP1; -.
DR   HGNC; HGNC:13234; CDIP1.
DR   HPA; ENSG00000089486; Low tissue specificity.
DR   MIM; 610503; gene.
DR   neXtProt; NX_Q9H305; -.
DR   OpenTargets; ENSG00000089486; -.
DR   PharmGKB; PA134879441; -.
DR   VEuPathDB; HostDB:ENSG00000089486; -.
DR   eggNOG; ENOG502S2GM; Eukaryota.
DR   GeneTree; ENSGT00940000157696; -.
DR   HOGENOM; CLU_095549_0_0_1; -.
DR   InParanoid; Q9H305; -.
DR   OMA; THEIGLM; -.
DR   OrthoDB; 1564782at2759; -.
DR   PhylomeDB; Q9H305; -.
DR   TreeFam; TF313294; -.
DR   PathwayCommons; Q9H305; -.
DR   SignaLink; Q9H305; -.
DR   BioGRID-ORCS; 29965; 11 hits in 1089 CRISPR screens.
DR   ChiTaRS; CDIP1; human.
DR   GenomeRNAi; 29965; -.
DR   Pharos; Q9H305; Tbio.
DR   PRO; PR:Q9H305; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q9H305; protein.
DR   Bgee; ENSG00000089486; Expressed in prefrontal cortex and 97 other tissues.
DR   ExpressionAtlas; Q9H305; baseline and differential.
DR   Genevisible; Q9H305; HS.
DR   GO; GO:0098560; C:cytoplasmic side of late endosome membrane; IDA:UniProtKB.
DR   GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IGI:MGI.
DR   GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:MGI.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IGI:MGI.
DR   InterPro; IPR006629; LITAF.
DR   InterPro; IPR037519; LITAF_fam.
DR   PANTHER; PTHR23292; PTHR23292; 1.
DR   Pfam; PF10601; zf-LITAF-like; 1.
DR   SMART; SM00714; LITAF; 1.
DR   PROSITE; PS51837; LITAF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Endosome; Lysosome; Membrane;
KW   Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..208
FT                   /note="Cell death-inducing p53-target protein 1"
FT                   /id="PRO_0000280336"
FT   DOMAIN          122..206
FT                   /note="LITAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01181"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..184
FT                   /note="Membrane-binding amphipathic helix"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        31..67
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
FT   VAR_SEQ         42..120
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046928"
FT   VAR_SEQ         82..120
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046929"
FT   CONFLICT        150
FT                   /note="T -> A (in Ref. 4; CAB66633 and 5; CAG38477)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   208 AA;  21892 MW;  6C7334668A3C15A7 CRC64;
     MSSEPPPPYP GGPTAPLLEE KSGAPPTPGR SSPAVMQPPP GMPLPPADIG PPPYEPPGHP
     MPQPGFIPPH MSADGTYMPP GFYPPPGPHP PMGYYPPGPY TPGPYPGPGG HTATVLVPSG
     AATTVTVLQG EIFEGAPVQT VCPHCQQAIT TKISYEIGLM NFVLGFFCCF MGCDLGCCLI
     PCLINDFKDV THTCPSCKAY IYTYKRLC
 
 
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