ZMY10_RAT
ID ZMY10_RAT Reviewed; 440 AA.
AC Q6AXZ5;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Zinc finger MYND domain-containing protein 10;
GN Name=Zmynd10;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Plays a role in axonemal structure organization and motility.
CC Involved in axonemal pre-assembly of inner and outer dynein arms (IDA
CC and ODA, respectively) for proper axoneme building for cilia motility
CC (By similarity). May act by indirectly regulating transcription of
CC dynein proteins (By similarity). {ECO:0000250|UniProtKB:Q99ML0}.
CC -!- SUBUNIT: Interacts (via C-terminus) with DNAAF11 (via CS domain); this
CC interaction stabilizes DNAAF11 at the protein level. Interacts (via C-
CC terminus) with DNAL1; this interaction stabilizes DNAL1 at the protein
CC level. Interacts with DNAAF4, HSPA8, IQUB, RUVBL2 and DYNTL5.
CC {ECO:0000250|UniProtKB:O75800}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23891469}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriolar satellite {ECO:0000269|PubMed:23891469}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q99ML0}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:Q5FWU8}.
CC -!- SIMILARITY: Belongs to the ZMYND10 family. {ECO:0000305}.
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DR EMBL; AABR06057029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473954; EDL77250.1; -; Genomic_DNA.
DR EMBL; BC079255; AAH79255.1; -; mRNA.
DR RefSeq; NP_001004284.1; NM_001004284.1.
DR AlphaFoldDB; Q6AXZ5; -.
DR SMR; Q6AXZ5; -.
DR CORUM; Q6AXZ5; -.
DR STRING; 10116.ENSRNOP00000031055; -.
DR iPTMnet; Q6AXZ5; -.
DR PhosphoSitePlus; Q6AXZ5; -.
DR PaxDb; Q6AXZ5; -.
DR Ensembl; ENSRNOT00000039258; ENSRNOP00000031055; ENSRNOG00000021602.
DR GeneID; 363139; -.
DR KEGG; rno:363139; -.
DR UCSC; RGD:1303250; rat.
DR CTD; 51364; -.
DR RGD; 1303250; Zmynd10.
DR eggNOG; ENOG502QS3F; Eukaryota.
DR GeneTree; ENSGT00940000153820; -.
DR HOGENOM; CLU_034036_1_0_1; -.
DR InParanoid; Q6AXZ5; -.
DR OMA; LIHEAYC; -.
DR OrthoDB; 685805at2759; -.
DR PhylomeDB; Q6AXZ5; -.
DR TreeFam; TF324215; -.
DR PRO; PR:Q6AXZ5; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000021602; Expressed in testis and 19 other tissues.
DR Genevisible; Q6AXZ5; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0044183; F:protein folding chaperone; ISO:RGD.
DR GO; GO:0003341; P:cilium movement; ISO:RGD.
DR GO; GO:0036159; P:inner dynein arm assembly; ISS:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; ISS:UniProtKB.
DR GO; GO:0036158; P:outer dynein arm assembly; ISS:UniProtKB.
DR GO; GO:1905505; P:positive regulation of motile cilium assembly; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; ISO:RGD.
DR GO; GO:0061512; P:protein localization to cilium; ISO:RGD.
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 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..440
FT /note="Zinc finger MYND domain-containing protein 10"
FT /id="PRO_0000424815"
FT ZN_FING 394..430
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
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"
SQ SEQUENCE 440 AA; 50675 MW; 824114B160977B47 CRC64;
MGDLELLLPG EAEVLVQGLH SFQLREMGSE GWSKQHENLE KLNMQAILDA TVSQAEPIQE
LLVTHGKIPT LVEELIAVEM WKQKVFPVLC RLEDFKPQNT FPIYMVVHHE ASIINLLETV
FFHKEVCESA DDTVLDLVDY CHRKLILLVA RKGGGDLSEE ERFQDSTPMQ ELQKQAEMME
FEISLKALSV LRYITDCMDS LSLSTLNRML TTHNLPCLLV ELLEHSPWSR REGGKLQHFE
SGRWQTVAPS EHQKLNKLDG QVWIALYNLL LSPEARTRYC LTNFAKGQLL KLQAFLTDTL
LDQLPNLADL KSFLAHLALV ETQPPKKDLV LEQIPEIWDR LERENKGKWQ AIAKHQLQHV
FSLSEKDLRQ QAQRWAETYR LDVLEAVAPE RPRCAYCSAE ASKRCSRCQK VWYCCRECQV
KHWEKHGKTC VLAAQGDRAK
