TXND3_CIOIN
ID TXND3_CIOIN Reviewed; 653 AA.
AC Q95YJ5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Thioredoxin domain-containing protein 3 homolog;
DE AltName: Full=Dynein intermediate chain 3;
GN Name=CiIC3;
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=11574167; DOI=10.1016/s0378-1119(01)00661-8;
RA Padma P., Hozumi A., Ogawa K., Inaba K.;
RT "Molecular cloning and characterization of a thioredoxin/nucleoside
RT diphosphate kinase related dynein intermediate chain from the ascidian,
RT Ciona intestinalis.";
RL Gene 275:177-183(2001).
CC -!- FUNCTION: May be required during the final stages of sperm tail
CC maturation. May act by reducing disulfide bonds within the sperm
CC components (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis-specific.
CC -!- DOMAIN: Contains 3 inactive NDK domains that each lack the active His
CC residue, suggesting that they have no NDP kinase activity.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NDK family.
CC {ECO:0000305}.
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DR EMBL; AB057786; BAB68388.1; -; mRNA.
DR RefSeq; NP_001027618.1; NM_001032446.1.
DR AlphaFoldDB; Q95YJ5; -.
DR SMR; Q95YJ5; -.
DR STRING; 7719.XP_009859668.1; -.
DR Ensembl; ENSCINT00000013583; ENSCINP00000013583; ENSCING00000006612.
DR GeneID; 445617; -.
DR KEGG; cin:445617; -.
DR CTD; 445617; -.
DR eggNOG; KOG0888; Eukaryota.
DR eggNOG; KOG0907; Eukaryota.
DR GeneTree; ENSGT00940000164537; -.
DR HOGENOM; CLU_016708_1_0_1; -.
DR InParanoid; Q95YJ5; -.
DR OMA; REIQYFF; -.
DR TreeFam; TF106374; -.
DR Proteomes; UP000008144; Unassembled WGS sequence.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.70.141; -; 3.
DR InterPro; IPR034907; NDK-like_dom.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR InterPro; IPR001564; Nucleoside_diP_kinase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00334; NDK; 3.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR SMART; SM00562; NDK; 3.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54919; SSF54919; 3.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Disulfide bond;
KW Redox-active center; Reference proteome; Spermatogenesis.
FT CHAIN 1..653
FT /note="Thioredoxin domain-containing protein 3 homolog"
FT /id="PRO_0000120160"
FT DOMAIN 9..114
FT /note="Thioredoxin"
FT REGION 155..299
FT /note="NDK 1"
FT REGION 300..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..459
FT /note="NDK 2"
FT REGION 459..597
FT /note="NDK 3"
FT REGION 603..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 38..41
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 653 AA; 73038 MW; 4D2313C9DB485F93 CRC64;
MAKRKEVILQ ETLNTQEAWE VAMNSGKLYV VDAHQKWCGP CTAIVGMLKR IKNELGDDLL
RFATAQVDVI DTLEQYRGKC EPNFLFYGGG ELVAAVRGCN APLVQETIQE TLKNEHKILS
GEMERKVFRD VYSDTPDQEE EEEDEEEEEG GVVSKQITVA LIKPDVVQNG QVDEILQKIS
EAGIEVLADE ERMLTVEEAR DFYKNKEEEE YFDQLIDYVT SGPCRVLVLT KGESGEGVVT
LWRDIIGPFD AAVAKEENPD SLRAIYGTDA TSNALHGSSS TEEAVRELGF FFPDFKPPTY
RSAKSAASRA SGRRSKTPSQ KPRLQRTLAI IRPDALQAHK DSILQKIDEA GFKIAMQKEM
VLTREQAESF YSEHKDTDYF EPLVKQMTCG PVLALCLAHD DAVDHWRSML GPKVVADAVE
EQPDSLRAQF RVEEAEVNML HGSDSAEAAE EELSKIFHVE QTLAVIKPDA IDEKEQIMGK
LKEAGFMISC QKDMNLSKEI ASEIYKSKEG SEYYDHLIDH MTSGPTLMMV LSAENAVEKL
RDIMGPTDPE VAKESHPESL RAMFAKSILE NAIHSPSTNE SAQEKIRIVF GDAQFDWDVN
DMQAEEGEVN ETSGEQPTDE QSGETEKTEE DGEHEGAQSD QQQAVSEAME KEE