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DYLT4_HUMAN
ID   DYLT4_HUMAN             Reviewed;         221 AA.
AC   Q5JR98;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Dynein light chain Tctex-type 4;
DE   AltName: Full=Protein N22.1;
DE   AltName: Full=Tctex-2-beta;
DE   AltName: Full=Tctex1 domain-containing protein 4;
GN   Name=DYNLT4 {ECO:0000312|HGNC:HGNC:32315}; Synonyms=TCTEX1D4;
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], INTERACTION WITH ENG; TGFBR2 AND TGFBR3, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=16982625; DOI=10.1074/jbc.m608614200;
RA   Meng Q.-J., Lux A., Holloschi A., Li J., Hughes J.M.X., Foerg T.,
RA   McCarthy J.E.G., Heagerty A.M., Kioschis P., Hafner M., Garland J.M.;
RT   "Identification of Tctex2beta, a novel dynein light chain family member
RT   that interacts with different transforming growth factor-beta receptors.";
RL   J. Biol. Chem. 281:37069-37080(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   SUBCELLULAR LOCATION, INTERACTION WITH PPP1CC, TISSUE SPECIFICITY, AND
RP   MUTAGENESIS OF 90-ARG--PHE-93 AND PHE-93.
RX   PubMed=23789093; DOI=10.1242/bio.20131065;
RA   Korrodi-Gregorio L., Vieira S.I., Esteves S.L., Silva J.V., Freitas M.J.,
RA   Brauns A.K., Luers G., Abrantes J., Esteves P.J., da Cruz e Silva O.A.,
RA   Fardilha M., da Cruz e Silva E.F.;
RT   "TCTEX1D4, a novel protein phosphatase 1 interactor: connecting the
RT   phosphatase to the microtubule network.";
RL   Biol. Open 2:453-465(2013).
CC   -!- SUBUNIT: Interacts with ENG/endoglin, TGFBR2 and TGFBR3
CC       (PubMed:16982625). Interacts with PPP1CC (PubMed:23789093).
CC       {ECO:0000269|PubMed:16982625, ECO:0000269|PubMed:23789093}.
CC   -!- INTERACTION:
CC       Q5JR98; Q99750: MDFI; NbExp=3; IntAct=EBI-4311709, EBI-724076;
CC       Q5JR98; P36873-1: PPP1CC; NbExp=2; IntAct=EBI-4311709, EBI-356289;
CC       Q5JR98; P36873-2: PPP1CC; NbExp=3; IntAct=EBI-4311709, EBI-3964623;
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC       {ECO:0000269|PubMed:23789093}. Cytoplasmic vesicle, secretory vesicle,
CC       acrosome {ECO:0000269|PubMed:23789093}. Cytoplasm, cytoskeleton, cilium
CC       axoneme {ECO:0000269|PubMed:23789093}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8CDY7}. Nucleus {ECO:0000250|UniProtKB:Q8CDY7}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center
CC       {ECO:0000269|PubMed:23789093}. Note=Present along the entire length of
CC       the flagellum, including principal and endpiece, and more predominantly
CC       in the midpiece region. {ECO:0000269|PubMed:23789093}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:16982625). Expressed
CC       in testis (at protein level) (PubMed:23789093).
CC       {ECO:0000269|PubMed:16982625, ECO:0000269|PubMed:23789093}.
CC   -!- SIMILARITY: Belongs to the dynein light chain Tctex-type family.
CC       {ECO:0000305}.
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DR   EMBL; DQ132441; ABA06522.1; -; mRNA.
DR   EMBL; AL592166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC092499; AAH92499.1; -; mRNA.
DR   CCDS; CCDS30699.1; -.
DR   RefSeq; NP_001013654.1; NM_001013632.3.
DR   RefSeq; XP_011539677.1; XM_011541375.2.
DR   RefSeq; XP_011539678.1; XM_011541376.2.
DR   AlphaFoldDB; Q5JR98; -.
DR   SMR; Q5JR98; -.
DR   BioGRID; 131262; 20.
DR   IntAct; Q5JR98; 3.
DR   STRING; 9606.ENSP00000341803; -.
DR   iPTMnet; Q5JR98; -.
DR   PhosphoSitePlus; Q5JR98; -.
DR   BioMuta; TCTEX1D4; -.
DR   DMDM; 74741821; -.
DR   MassIVE; Q5JR98; -.
DR   PaxDb; Q5JR98; -.
DR   PeptideAtlas; Q5JR98; -.
DR   PRIDE; Q5JR98; -.
DR   ProteomicsDB; 63077; -.
DR   Antibodypedia; 32555; 65 antibodies from 21 providers.
DR   DNASU; 343521; -.
DR   Ensembl; ENST00000339355.3; ENSP00000341803.2; ENSG00000188396.4.
DR   Ensembl; ENST00000675259.1; ENSP00000501642.1; ENSG00000188396.4.
DR   GeneID; 343521; -.
DR   KEGG; hsa:343521; -.
DR   MANE-Select; ENST00000339355.3; ENSP00000341803.2; NM_001377534.1; NP_001364463.1.
DR   UCSC; uc057fwn.1; human.
DR   CTD; 343521; -.
DR   GeneCards; DYNLT4; -.
DR   HGNC; HGNC:32315; DYNLT4.
DR   HPA; ENSG00000188396; Tissue enhanced (choroid plexus, fallopian tube).
DR   MIM; 611713; gene.
DR   neXtProt; NX_Q5JR98; -.
DR   OpenTargets; ENSG00000188396; -.
DR   VEuPathDB; HostDB:ENSG00000188396; -.
DR   eggNOG; KOG4108; Eukaryota.
DR   GeneTree; ENSGT00940000162474; -.
DR   HOGENOM; CLU_097204_1_1_1; -.
DR   InParanoid; Q5JR98; -.
DR   OMA; CPPRYKL; -.
DR   OrthoDB; 1435776at2759; -.
DR   PhylomeDB; Q5JR98; -.
DR   TreeFam; TF313904; -.
DR   PathwayCommons; Q5JR98; -.
DR   SignaLink; Q5JR98; -.
DR   BioGRID-ORCS; 343521; 24 hits in 1015 CRISPR screens.
DR   GenomeRNAi; 343521; -.
DR   Pharos; Q5JR98; Tbio.
DR   PRO; PR:Q5JR98; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q5JR98; protein.
DR   Bgee; ENSG00000188396; Expressed in right uterine tube and 90 other tissues.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR   GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR   GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; IDA:MGI.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IDA:MGI.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   Gene3D; 3.30.1140.40; -; 1.
DR   InterPro; IPR005334; Tctex-1-like.
DR   InterPro; IPR038586; Tctex-1-like_sf.
DR   PANTHER; PTHR21255; PTHR21255; 1.
DR   Pfam; PF03645; Tctex-1; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW   Flagellum; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..221
FT                   /note="Dynein light chain Tctex-type 4"
FT                   /id="PRO_0000316872"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CDY7"
FT   MUTAGEN         90..93
FT                   /note="RVSF->AAAA: Partially reduces the binding to PP1CC."
FT                   /evidence="ECO:0000269|PubMed:23789093"
FT   MUTAGEN         93
FT                   /note="F->A: Decreased colocalization with PPP1CC by 27%."
FT                   /evidence="ECO:0000269|PubMed:23789093"
SQ   SEQUENCE   221 AA;  23353 MW;  77A6BB803CC83373 CRC64;
     MASRPLPPGR QEEENAKDSG RKPSPVRPRG CLPSIDEARP AGPGPAPASR RGSMLGLAAS
     FSRRNSLVGP GAGPGGQRPS LGPVPPLGSR VSFSGLPLAP ARWVAPSYRT EPVPGERWEA
     ARAQRALEAA LAAGLHDACY SSDEAARLVR ELCEQVHVRL RELSPPRYKL VCSVVLGPRA
     GQGVHVVSRA LWDVARDGLA SVSYTNTSLF AVATVHGLYC E
 
 
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