ZMY10_HUMAN
ID ZMY10_HUMAN Reviewed; 440 AA.
AC O75800; A6NK41; B3KU54; O14570; O75801; Q53FE6; Q8N4R6; Q8NDN6;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Zinc finger MYND domain-containing protein 10 {ECO:0000305};
DE AltName: Full=Protein BLu {ECO:0000303|Ref.1};
GN Name=ZMYND10 {ECO:0000312|HGNC:HGNC:19412};
GN Synonyms=BLU {ECO:0000303|Ref.1}; ORFNames=LUCA12.4;
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] (ISOFORMS 1 AND 2), AND VARIANT TRP-369.
RC TISSUE=Lung, and Testis;
RA Duh F.-M., Latif F., Bader S., Sekido Y., Kuzmin I., Minna J.D., Koonin E.,
RA Lerman M.I.;
RT "A novel gene (BLu) that resides in the lung cancer region on chromosome
RT 3p21.3 has the MYND Zn finger-like module.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
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 [7]
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 [8]
RP DISCUSSION OF SEQUENCE, AND VARIANT GLN-407.
RX PubMed=11085536;
RG The international lung cancer chromosome 3p21.3 tumor suppressor gene consortium;
RA Lerman M.I., Minna J.D.;
RT "The 630-kb lung cancer homozygous deletion region on human chromosome
RT 3p21.3: identification and evaluation of the resident candidate tumor
RT suppressor genes.";
RL Cancer Res. 60:6116-6133(2000).
RN [9]
RP STRUCTURE BY NMR OF 384-440.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the MYND domain of the human zinc finger MYND
RT domain-containing protein 10.";
RL Submitted (JUN-2006) to the PDB data bank.
RN [10]
RP VARIANTS CILD22 GLY-16; PRO-29; 323-GLN--LYS-440 DEL; 366-GLN--LYS-440 DEL
RP AND CYS-379, CHARACTERIZATION OF VARIANTS CILD22 GLY-16; PRO-29;
RP 323-GLN--LYS-440 DEL; 366-GLN--LYS-440 DEL AND CYS-379, FUNCTION,
RP INTERACTION WITH DNAAF11, AND INVOLVEMENT IN CILD22.
RX PubMed=23891469; DOI=10.1016/j.ajhg.2013.06.007;
RA Zariwala M.A., Gee H.Y., Kurkowiak M., Al-Mutairi D.A., Leigh M.W.,
RA Hurd T.W., Hjeij R., Dell S.D., Chaki M., Dougherty G.W., Adan M.,
RA Spear P.C., Esteve-Rudd J., Loges N.T., Rosenfeld M., Diaz K.A.,
RA Olbrich H., Wolf W.E., Sheridan E., Batten T.F., Halbritter J.,
RA Porath J.D., Kohl S., Lovric S., Hwang D.Y., Pittman J.E., Burns K.A.,
RA Ferkol T.W., Sagel S.D., Olivier K.N., Morgan L.C., Werner C., Raidt J.,
RA Pennekamp P., Sun Z., Zhou W., Airik R., Natarajan S., Allen S.J.,
RA Amirav I., Wieczorek D., Landwehr K., Nielsen K., Schwerk N., Sertic J.,
RA Kohler G., Washburn J., Levy S., Fan S., Koerner-Rettberg C., Amselem S.,
RA Williams D.S., Mitchell B.J., Drummond I.A., Otto E.A., Omran H.,
RA Knowles M.R., Hildebrandt F.;
RT "ZMYND10 is mutated in primary ciliary dyskinesia and interacts with
RT LRRC6.";
RL Am. J. Hum. Genet. 93:336-345(2013).
RN [11]
RP VARIANTS CILD22 GLY-16; PRO-39 AND PRO-266, FUNCTION, AND INTERACTION WITH
RP DNAAF11.
RX PubMed=23891471; DOI=10.1016/j.ajhg.2013.07.009;
RA Moore D.J., Onoufriadis A., Shoemark A., Simpson M.A., Zur Lage P.I.,
RA de Castro S.C., Bartoloni L., Gallone G., Petridi S., Woollard W.J.,
RA Antony D., Schmidts M., Didonna T., Makrythanasis P., Bevillard J.,
RA Mongan N.P., Djakow J., Pals G., Lucas J.S., Marthin J.K., Nielsen K.G.,
RA Santoni F., Guipponi M., Hogg C., Antonarakis S.E., Emes R.D., Chung E.M.,
RA Greene N.D., Blouin J.L., Jarman A.P., Mitchison H.M.;
RT "Mutations in ZMYND10, a gene essential for proper axonemal assembly of
RT inner and outer dynein arms in humans and flies, cause primary ciliary
RT dyskinesia.";
RL Am. J. Hum. Genet. 93:346-356(2013).
RN [12]
RP INVOLVEMENT IN CILD22.
RX PubMed=25186273; DOI=10.1183/09031936.00052014;
RA Raidt J., Wallmeier J., Hjeij R., Onnebrink J.G., Pennekamp P., Loges N.T.,
RA Olbrich H., Haeffner K., Dougherty G.W., Omran H., Werner C.;
RT "Ciliary beat pattern and frequency in genetic variants of primary ciliary
RT dyskinesia.";
RL Eur. Respir. J. 44:1579-1588(2014).
RN [13]
RP VARIANT CILD22 366-GLN--LYS-440 DEL, CHARACTERIZATION OF VARIANT CILD22
RP 366-GLN--LYS-440 DEL, AND INTERACTION WITH DNAAF4; DNAL1; HSPA8; IQUB;
RP DNAAF11; RUVBL2 AND DYNTL5.
RX PubMed=29601588; DOI=10.1371/journal.pgen.1007316;
RA Cho K.J., Noh S.H., Han S.M., Choi W.I., Kim H.Y., Yu S., Lee J.S.,
RA Rim J.H., Lee M.G., Hildebrandt F., Gee H.Y.;
RT "ZMYND10 stabilizes intermediate chain proteins in the cytoplasmic pre-
RT assembly of dynein arms.";
RL PLoS Genet. 14:E1007316-E1007316(2018).
CC -!- FUNCTION: Plays a role in axonemal structure organization and motility
CC (PubMed:23891469, PubMed:23891471). Involved in axonemal pre-assembly
CC of inner and outer dynein arms (IDA and ODA, respectively) for proper
CC axoneme building for cilia motility (By similarity). May act by
CC indirectly regulating transcription of dynein proteins (By similarity).
CC {ECO:0000250|UniProtKB:Q99ML0, ECO:0000269|PubMed:23891469,
CC ECO:0000269|PubMed:23891471}.
CC -!- SUBUNIT: Interacts (via C-terminus) with DNAAF11 (via CS domain); this
CC interaction stabilizes DNAAF11 at the protein level (PubMed:23891469,
CC PubMed:23891471, PubMed:29601588). Interacts (via C-terminus) with
CC DNAL1; this interaction stabilizes DNAL1 at the protein level
CC (PubMed:29601588). Interacts with DNAAF4, HSPA8, IQUB, RUVBL2 and
CC DYNTL5 (PubMed:29601588). {ECO:0000269|PubMed:23891469,
CC ECO:0000269|PubMed:23891471, ECO:0000269|PubMed:29601588}.
CC -!- INTERACTION:
CC O75800; P51861: CDR1; NbExp=6; IntAct=EBI-747061, EBI-2836538;
CC O75800; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-747061, EBI-3867333;
CC O75800; Q7L2H7: EIF3M; NbExp=3; IntAct=EBI-747061, EBI-353901;
CC O75800; B7ZLH0: FAM22F; NbExp=3; IntAct=EBI-747061, EBI-10220102;
CC O75800; Q96FT9: IFT43; NbExp=3; IntAct=EBI-747061, EBI-10189681;
CC O75800; Q96FT9-2: IFT43; NbExp=3; IntAct=EBI-747061, EBI-11944538;
CC O75800; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-747061, EBI-11522433;
CC O75800; Q86Y26: NUTM1; NbExp=3; IntAct=EBI-747061, EBI-10178410;
CC O75800; P57052: RBM11; NbExp=3; IntAct=EBI-747061, EBI-741332;
CC O75800; Q9Y5W9: SNX11; NbExp=3; IntAct=EBI-747061, EBI-10329449;
CC O75800; Q99593: TBX5; NbExp=3; IntAct=EBI-747061, EBI-297043;
CC O75800; P15884-3: TCF4; NbExp=3; IntAct=EBI-747061, EBI-13636688;
CC O75800; Q9Y3Q8: TSC22D4; NbExp=5; IntAct=EBI-747061, EBI-739485;
CC O75800; Q96G27: WBP1; NbExp=3; IntAct=EBI-747061, EBI-3867685;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6AXZ5}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriolar satellite {ECO:0000250|UniProtKB:Q6AXZ5}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q99ML0}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:Q5FWU8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Lung;
CC IsoId=O75800-1; Sequence=Displayed;
CC Name=2; Synonyms=Testis;
CC IsoId=O75800-2; Sequence=VSP_003328;
CC -!- DISEASE: Ciliary dyskinesia, primary, 22 (CILD22) [MIM:615444]: A
CC disorder characterized by abnormalities of motile cilia. Respiratory
CC infections leading to chronic inflammation and bronchiectasis are
CC recurrent, due to defects in the respiratory cilia. Patients may
CC exhibit randomization of left-right body asymmetry and situs inversus,
CC due to dysfunction of monocilia at the embryonic node. Primary ciliary
CC dyskinesia associated with situs inversus is referred to as Kartagener
CC syndrome. {ECO:0000269|PubMed:23891469, ECO:0000269|PubMed:23891471,
CC ECO:0000269|PubMed:25186273, ECO:0000269|PubMed:29601588}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the ZMYND10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB67311.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U70824; AAC24726.1; -; mRNA.
DR EMBL; U70880; AAC24728.1; -; mRNA.
DR EMBL; AL833828; CAD38688.1; -; mRNA.
DR EMBL; AK096525; BAG53316.1; -; mRNA.
DR EMBL; AK223343; BAD97063.1; -; mRNA.
DR EMBL; AC002481; AAB67311.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471055; EAW65104.1; -; Genomic_DNA.
DR EMBL; BC033732; AAH33732.1; -; mRNA.
DR CCDS; CCDS2825.1; -. [O75800-1]
DR CCDS; CCDS77747.1; -. [O75800-2]
DR RefSeq; NP_001295308.1; NM_001308379.1. [O75800-2]
DR RefSeq; NP_056980.2; NM_015896.3. [O75800-1]
DR PDB; 2D8Q; NMR; -; A=384-440.
DR PDB; 2DAN; NMR; -; A=384-430.
DR PDBsum; 2D8Q; -.
DR PDBsum; 2DAN; -.
DR AlphaFoldDB; O75800; -.
DR BMRB; O75800; -.
DR SMR; O75800; -.
DR BioGRID; 119499; 21.
DR IntAct; O75800; 18.
DR MINT; O75800; -.
DR STRING; 9606.ENSP00000231749; -.
DR iPTMnet; O75800; -.
DR PhosphoSitePlus; O75800; -.
DR BioMuta; ZMYND10; -.
DR MassIVE; O75800; -.
DR PaxDb; O75800; -.
DR PeptideAtlas; O75800; -.
DR PRIDE; O75800; -.
DR ProteomicsDB; 50200; -. [O75800-1]
DR ProteomicsDB; 50201; -. [O75800-2]
DR Antibodypedia; 30915; 186 antibodies from 27 providers.
DR DNASU; 51364; -.
DR Ensembl; ENST00000231749.8; ENSP00000231749.3; ENSG00000004838.14. [O75800-1]
DR Ensembl; ENST00000360165.7; ENSP00000353289.3; ENSG00000004838.14. [O75800-2]
DR GeneID; 51364; -.
DR KEGG; hsa:51364; -.
DR MANE-Select; ENST00000231749.8; ENSP00000231749.3; NM_015896.4; NP_056980.2.
DR UCSC; uc003dag.2; human. [O75800-1]
DR CTD; 51364; -.
DR DisGeNET; 51364; -.
DR GeneCards; ZMYND10; -.
DR GeneReviews; ZMYND10; -.
DR HGNC; HGNC:19412; ZMYND10.
DR HPA; ENSG00000004838; Group enriched (fallopian tube, testis).
DR MalaCards; ZMYND10; -.
DR MIM; 607070; gene.
DR MIM; 615444; phenotype.
DR neXtProt; NX_O75800; -.
DR OpenTargets; ENSG00000004838; -.
DR Orphanet; 244; Primary ciliary dyskinesia.
DR PharmGKB; PA134981649; -.
DR VEuPathDB; HostDB:ENSG00000004838; -.
DR eggNOG; ENOG502QS3F; Eukaryota.
DR GeneTree; ENSGT00940000153820; -.
DR HOGENOM; CLU_034036_1_0_1; -.
DR InParanoid; O75800; -.
DR OMA; LIHEAYC; -.
DR OrthoDB; 685805at2759; -.
DR PhylomeDB; O75800; -.
DR TreeFam; TF324215; -.
DR PathwayCommons; O75800; -.
DR SignaLink; O75800; -.
DR BioGRID-ORCS; 51364; 21 hits in 1065 CRISPR screens.
DR EvolutionaryTrace; O75800; -.
DR GeneWiki; ZMYND10; -.
DR GenomeRNAi; 51364; -.
DR Pharos; O75800; Tbio.
DR PRO; PR:O75800; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O75800; protein.
DR Bgee; ENSG00000004838; Expressed in right uterine tube and 104 other tissues.
DR ExpressionAtlas; O75800; baseline and differential.
DR Genevisible; O75800; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:Ensembl.
DR GO; GO:0044183; F:protein folding chaperone; IEA:Ensembl.
DR GO; GO:0003341; P:cilium movement; IEA:Ensembl.
DR GO; GO:0036159; P:inner dynein arm assembly; IMP:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; IMP:UniProtKB.
DR GO; GO:0036158; P:outer dynein arm assembly; IMP:UniProtKB.
DR GO; GO:1905505; P:positive regulation of motile cilium assembly; ISS:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; IEA:Ensembl.
DR InterPro; IPR017333; UCP037948_Znf-MYND.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF01753; zf-MYND; 1.
DR PIRSF; PIRSF037948; UCP037948_Znf_MYND10; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Ciliopathy; Cytoplasm;
KW Cytoskeleton; Disease variant; Kartagener syndrome; Membrane;
KW Metal-binding; Primary ciliary dyskinesia; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..440
FT /note="Zinc finger MYND domain-containing protein 10"
FT /id="PRO_0000218314"
FT ZN_FING 394..430
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 366..440
FT /note="Interaction with DNAAF11"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT VAR_SEQ 200..234
FT /note="SLSLSTLSRMLSTHNLPCLLVELLEHSPWSRREGG -> RQWSVSQPPQLAH
FT LKRIQRLHPVCWFLSPG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_003328"
FT VARIANT 16
FT /note="V -> G (in CILD22; no loss of interaction with
FT DNAAF11; dbSNP:rs138815960)"
FT /evidence="ECO:0000269|PubMed:23891469,
FT ECO:0000269|PubMed:23891471"
FT /id="VAR_070184"
FT VARIANT 29
FT /note="S -> P (in CILD22; no loss of interaction with
FT DNAAF11; dbSNP:rs587621539)"
FT /evidence="ECO:0000269|PubMed:23891469"
FT /id="VAR_070185"
FT VARIANT 39
FT /note="L -> P (in CILD22)"
FT /evidence="ECO:0000269|PubMed:23891471"
FT /id="VAR_070186"
FT VARIANT 266
FT /note="L -> P (in CILD22; dbSNP:rs200913791)"
FT /evidence="ECO:0000269|PubMed:23891471"
FT /id="VAR_070187"
FT VARIANT 323..440
FT /note="Missing (in CILD22; loss of interaction with
FT DNAAF11)"
FT /evidence="ECO:0000269|PubMed:23891469"
FT /id="VAR_080482"
FT VARIANT 366..440
FT /note="Missing (in CILD22; loss of interaction with DNAL1)"
FT /evidence="ECO:0000269|PubMed:23891469,
FT ECO:0000269|PubMed:29601588"
FT /id="VAR_080483"
FT VARIANT 369
FT /note="R -> W (in dbSNP:rs142613783)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_070188"
FT VARIANT 379
FT /note="Y -> C (in CILD22; no loss of interaction with
FT DNAAF11; dbSNP:rs753061612)"
FT /evidence="ECO:0000269|PubMed:23891469"
FT /id="VAR_070189"
FT VARIANT 407
FT /note="R -> Q (in non-small cell lung cancer cell lines;
FT dbSNP:rs182064110)"
FT /evidence="ECO:0000269|PubMed:11085536"
FT /id="VAR_014227"
FT CONFLICT 35
FT /note="Q -> R (in Ref. 2; CAD38688)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="K -> E (in Ref. 3; BAG53316)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="V -> A (in Ref. 4; BAD97063)"
FT /evidence="ECO:0000305"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:2D8Q"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:2D8Q"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:2DAN"
FT HELIX 416..421
FT /evidence="ECO:0007829|PDB:2D8Q"
FT HELIX 423..429
FT /evidence="ECO:0007829|PDB:2D8Q"
SQ SEQUENCE 440 AA; 50344 MW; 510D41074C956CA3 CRC64;
MGDLELLLPG EAEVLVRGLR SFPLREMGSE GWNQQHENLE KLNMQAILDA TVSQGEPIQE
LLVTHGKVPT LVEELIAVEM WKQKVFPVFC RVEDFKPQNT FPIYMVVHHE ASIINLLETV
FFHKEVCESA EDTVLDLVDY CHRKLTLLVA QSGCGGPPEG EGSQDSNPMQ ELQKQAELME
FEIALKALSV LRYITDCVDS LSLSTLSRML STHNLPCLLV ELLEHSPWSR REGGKLQQFE
GSRWHTVAPS EQQKLSKLDG QVWIALYNLL LSPEAQARYC LTSFAKGRLL KLRAFLTDTL
LDQLPNLAHL QSFLAHLTLT ETQPPKKDLV LEQIPEIWER LERENRGKWQ AIAKHQLQHV
FSPSEQDLRL QARRWAETYR LDVLEAVAPE RPRCAYCSAE ASKRCSRCQN EWYCCRECQV
KHWEKHGKTC VLAAQGDRAK
