ID   DNAI7_MACFA             Reviewed;         722 AA.
AC   Q4R796;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Dynein axonemal intermediate chain 7 {ECO:0000305};
GN   Name=DNAI7 {ECO:0000250|UniProtKB:Q6TDU7}; ORFNames=QtsA-15847;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Via its association with the multisubunit axonemal dynein
CC       complex, is potentially involved in the regulation of cilia function.
CC       May act as a cell cycle regulator. {ECO:0000250|UniProtKB:Q6TDU8}.
CC   -!- SUBUNIT: Part of the multisubunit axonemal dynein complex formed at
CC       least of two heavy chains and a number of intermediate and light
CC       chains. Associates with tubulin. Interacts with microtubule.
CC       {ECO:0000250|UniProtKB:Q6TDU8}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000250|UniProtKB:Q6TDU8}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q6TDU8}. Note=Colocalizes with microtubules in
CC       interphase. {ECO:0000250|UniProtKB:Q6TDU8}.
CC   -!- PTM: Ubiquitinated. Ubiquitination leads to its degradation through the
CC       26S proteasome. Ubiquitin-proteasome-mediated DNAI7 degradation occurs
CC       in mitosis. {ECO:0000250|UniProtKB:Q6TDU8}.
CC   -!- SIMILARITY: Belongs to the DNAI7 family. {ECO:0000305}.
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DR   EMBL; AB168925; BAE01026.1; -; mRNA.
DR   AlphaFoldDB; Q4R796; -.
DR   SMR; Q4R796; -.
DR   STRING; 9541.XP_005570444.1; -.
DR   eggNOG; ENOG502QQM9; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005858; C:axonemal dynein complex; ISS:UniProtKB.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   InterPro; IPR022110; CASC1_C.
DR   InterPro; IPR031826; IC97/Casc1_N.
DR   InterPro; IPR023247; IC97/Dnai7-like.
DR   PANTHER; PTHR20929; PTHR20929; 1.
DR   Pfam; PF12366; Casc1_C; 1.
DR   Pfam; PF15927; Casc1_N; 1.
DR   PRINTS; PR02043; CANCERSCCP1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cytoplasm; Reference proteome; Ubl conjugation.
FT   CHAIN           1..722
FT                   /note="Dynein axonemal intermediate chain 7"
FT                   /id="PRO_0000332732"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   722 AA;  84086 MW;  C3FC7D89C1CE6B3D CRC64;
     MGPKAKKSGS KKKKVTKAER LKLLQEEEDR RLKEEEEARL KYEKEEMERL EIQRIEKEKW
     NRLEAKDLER RNEELEELYL LERCFPEAEK LKQETRMLSQ WKHYIQCDGS PDPSIAQEMN
     TFISLWKEKT NETFEEVIEK SKVVLNLIEK LKFILLETPL CDLQDKNIIQ YQESILQLQE
     LLHLKFNVAT EILLRQASTL ADLDSGNMEK VIKDENVTLY VWANLKKNPR HRSVRFSETQ
     IGFEIPRILA TSDIAVRLLH THYDHVSALH PVSTPSKEHT SSATELVKDD VENVEKAISK
     EVEEESKQQE KQSHLIQEEK LKVEEEQDDI EVKMGSAEEE SEAIKCELEM KVLSETVSAA
     QLLLVENSSE KPDFFENDMV DLFQFTTLGG VYHLDILELP PQCKPVKGWM IVEILKEGLQ
     KYTYPPETTE DFETENAFPP IEVTLEVHEN VIFFENPMVV RWDAEGKHWR TDGISNVSYK
     PNERLITFSL DTFGPVTLIQ DAHINMPYQS WELRPLDVNK VLLTVTTVFT EIQIQIKENL
     CMLSSVKLKD KKHISILEGT WMTPIPFIIA LKEAGLNIFP TRYSHFYVVI NNKVPLVEVK
     AYRQMALLSS TFAFGWSKWN LLCNSTKVVF KVREHLPEEC TENPNWALLM FSGDRAQRLK
     IKEESEAFSE ALKEETEFHS TLYHMVRDFA SKEAMEKVRS SNCQFVNSVC HMLLSTRLLS
     YS