IFT81_MOUSE
ID IFT81_MOUSE Reviewed; 676 AA.
AC O35594; Q8R4W2; Q9CSA1; Q9EQM1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 4.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Intraflagellar transport protein 81 homolog;
DE AltName: Full=Carnitine deficiency-associated protein expressed in ventricle 1;
DE Short=CDV-1;
GN Name=Ift81; Synonyms=Cdv-1, Cdv1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CDV-1R AND CDV-1), AND TISSUE
RP SPECIFICITY (ISOFORMS CDV-1R AND CDV-1).
RC STRAIN=C3H/HeJ; TISSUE=Brain, and Heart;
RX PubMed=9187371; DOI=10.1016/s0014-5793(97)00429-8;
RA Masuda M., Kobayashi K., Horiuchi M., Terazono H., Yoshimura N., Saheki T.;
RT "A novel gene suppressed in the ventricle of carnitine-deficient juvenile
RT visceral steatosis mice.";
RL FEBS Lett. 408:221-224(1997).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Horiuchi M.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE INITIATION (ISOFORMS
RP CDV-1R AND CDV-1).
RX PubMed=11130971; DOI=10.1007/s003350010207;
RA Higashi M., Kobayashi K., Iijima M., Wakana S., Horiuchi M., Yasuda T.,
RA Yoshida G., Kanmura Y., Saheki T.;
RT "Genomic organization and mapping of mouse CDV (carnitine deficiency-
RT associated gene expressed in ventricle)-1 and its related CDV-1R gene.";
RL Mamm. Genome 11:1053-1057(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CDV-1R), FUNCTION (ISOFORM CDV-1R),
RP DEVELOPMENTAL STAGE (ISOFORM CDV-1R), AND TISSUE SPECIFICITY (ISOFORM
RP CDV-1R).
RX PubMed=12549821; DOI=10.1023/a:1021232518628;
RA Peng J., Yu L., Horiuchi M., Zhang P., Huang X., Zhang Y., Li D.,
RA Jalil M.A., Zhao S.;
RT "Identification of human CDV-1R and mouse Cdv-1R, two novel proteins with
RT putative signal peptides, especially highly expressed in testis and
RT increased with the male sex maturation.";
RL Mol. Biol. Rep. 29:353-362(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CDV-1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CDV-1R).
RC STRAIN=C57BL/6J; 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 [7]
RP FUNCTION (ISOFORM CDV-1).
RX PubMed=10210276; DOI=10.1016/s0024-3205(99)00042-9;
RA Jalil A., Horiuchi M., Nomoto M., Kobayashi K., Saheki T.;
RT "Catecholamine metabolism inhibitors and receptor blockades only partially
RT suppress cardiac hypertrophy of juvenile visceral steatosis mice with
RT systemic carnitine deficiency.";
RL Life Sci. 64:1137-1144(1999).
RN [8]
RP IDENTIFICATION IN THE IFT COMPLEX B, INTERACTION WITH IFT88, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19253336; DOI=10.1002/cm.20346;
RA Follit J.A., Xu F., Keady B.T., Pazour G.J.;
RT "Characterization of mouse IFT complex B.";
RL Cell Motil. Cytoskeleton 66:457-468(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH RABL2, AND TISSUE SPECIFICITY.
RX PubMed=23055941; DOI=10.1371/journal.pgen.1002969;
RA Lo J.C., Jamsai D., O'Connor A.E., Borg C., Clark B.J., Whisstock J.C.,
RA Field M.C., Adams V., Ishikawa T., Aitken R.J., Whittle B., Goodnow C.C.,
RA Ormandy C.J., O'Bryan M.K.;
RT "RAB-like 2 has an essential role in male fertility, sperm intra-flagellar
RT transport, and tail assembly.";
RL PLoS Genet. 8:E1002969-E1002969(2012).
RN [11]
RP IDENTIFICATION IN THE IFT COMPLEX B, AND INTERACTION WITH IFT57 AND TTC30B.
RX PubMed=23810713; DOI=10.1016/j.yexcr.2013.06.010;
RA Howard P.W., Jue S.F., Maurer R.A.;
RT "Interaction of mouse TTC30/DYF-1 with multiple intraflagellar transport
RT complex B proteins and KIF17.";
RL Exp. Cell Res. 319:2275-2281(2013).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=32233951; DOI=10.1152/ajpcell.00450.2019;
RA Qu W., Yuan S., Quan C., Huang Q., Zhou Q., Yap Y., Shi L., Zhang D.,
RA Guest T., Li W., Yee S.P., Zhang L., Cazin C., Hess R.A., Ray P.F.,
RA Kherraf Z.E., Zhang Z.;
RT "The essential role of intraflagellar transport protein IFT81 in male mice
RT spermiogenesis and fertility.";
RL Am. J. Physiol. 318:C1092-C1106(2020).
CC -!- FUNCTION: Component of the intraflagellar transport (IFT) complex B:
CC together with IFT74, forms a tubulin-binding module that specifically
CC mediates transport of tubulin within the cilium. Binds tubulin via its
CC CH (calponin-homology)-like region. Required for ciliogenesis. Required
CC for proper regulation of SHH signaling (By similarity). Plays an
CC important role during spermatogenesis by modulating the assembly and
CC elongation of the sperm flagella (PubMed:32233951).
CC {ECO:0000250|UniProtKB:Q8WYA0, ECO:0000269|PubMed:32233951}.
CC -!- FUNCTION: [Isoform CDV-1]: May be involved in cardiac hypertrophy
CC caused by carnitine deficiency. {ECO:0000269|PubMed:10210276}.
CC -!- FUNCTION: [Isoform CDV-1R]: May play a role in development of the
CC testis and spermatogenesis. {ECO:0000269|PubMed:12549821}.
CC -!- SUBUNIT: Component of the IFT complex B, at least composed of IFT20,
CC IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74,
CC IFT81, and IFT88 (PubMed:19253336, PubMed:23810713). Interacts with
CC IFT74; the interaction is direct: within the IFT complex B, IFT74 and
CC IFT81 mediate the transport of tubulin within the cilium. Interacts
CC with tubulin; the interaction is direct (By similarity). Interacts with
CC IFT57 and TTC30B (PubMed:23810713). Interacts with RABL2/RABL2A;
CC binding is equal in the presence of GTP or GDP (PubMed:23055941).
CC Interacts with IFT88 (PubMed:19253336). Interacts (via the IFT74/IFT81
CC heterodimer) with RABL2B (By similarity).
CC {ECO:0000250|UniProtKB:Q8WYA0, ECO:0000269|PubMed:19253336,
CC ECO:0000269|PubMed:23055941, ECO:0000269|PubMed:23810713}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:19253336}. Cytoplasm {ECO:0000269|PubMed:32233951}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=CDV-1R;
CC IsoId=O35594-1; Sequence=Displayed;
CC Name=CDV-1;
CC IsoId=O35594-2; Sequence=VSP_018785;
CC -!- TISSUE SPECIFICITY: Highly expressed in the testis (at protein level)
CC (PubMed:32233951). Co-localizes with RABL2/RABL2A in the midpiece of
CC elongated spermatids within the testis (at protein level)
CC (PubMed:23055941). {ECO:0000269|PubMed:23055941,
CC ECO:0000269|PubMed:32233951}.
CC -!- TISSUE SPECIFICITY: [Isoform CDV-1R]: Expressed predominantly in the
CC testis. {ECO:0000269|PubMed:12549821}.
CC -!- TISSUE SPECIFICITY: [Isoform CDV-1]: Expressed specifically in heart
CC and suppressed specifically in ventricles, but not in auricles, of
CC carnitine-deficient juvenile visceral steatosis (JVS) mice.
CC {ECO:0000269|PubMed:12549821, ECO:0000269|PubMed:9187371}.
CC -!- DEVELOPMENTAL STAGE: First detected at postnatal day (PND) 8, its level
CC increased dramatically from PND 16 to 42 (at protein level).
CC {ECO:0000269|PubMed:32233951}.
CC -!- DEVELOPMENTAL STAGE: [Isoform CDV-1R]: Poorly expressed in the testis
CC 15 days after birth. Levels increase sharply between days 15 and 30
CC reaching a maximum by day 45 and the onset of spermatogenesis.
CC {ECO:0000269|PubMed:12549821}.
CC -!- DOMAIN: The CH (calponin-homology)-like region shows high similarity to
CC a CH (calponin-homology) domain and mediated binding to the globular
CC domain of tubulin. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice show impaired spermiogenesis, abnormal sperm
CC morphology and significantly reduced sperm number and motility
CC (PubMed:32233951). In addition to oligozoospermia, spermatozoa show
CC dysmorphic and non-functional flagella (PubMed:32233951).
CC {ECO:0000269|PubMed:32233951}.
CC -!- SIMILARITY: Belongs to the IFT81 family. {ECO:0000305}.
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DR EMBL; Y10495; CAA71519.2; -; mRNA.
DR EMBL; Y10496; CAA71520.1; -; mRNA.
DR EMBL; AF203441; AAG35650.1; -; Genomic_DNA.
DR EMBL; AF203431; AAG35650.1; JOINED; Genomic_DNA.
DR EMBL; AF203432; AAG35650.1; JOINED; Genomic_DNA.
DR EMBL; AF203433; AAG35650.1; JOINED; Genomic_DNA.
DR EMBL; AF203434; AAG35650.1; JOINED; Genomic_DNA.
DR EMBL; AF203435; AAG35650.1; JOINED; Genomic_DNA.
DR EMBL; AF203436; AAG35650.1; JOINED; Genomic_DNA.
DR EMBL; AF203437; AAG35650.1; JOINED; Genomic_DNA.
DR EMBL; AF203438; AAG35650.1; JOINED; Genomic_DNA.
DR EMBL; AF203439; AAG35650.1; JOINED; Genomic_DNA.
DR EMBL; AF203440; AAG35650.1; JOINED; Genomic_DNA.
DR EMBL; AF203441; AAG35651.1; -; Genomic_DNA.
DR EMBL; AF203438; AAG35651.1; JOINED; Genomic_DNA.
DR EMBL; AF203439; AAG35651.1; JOINED; Genomic_DNA.
DR EMBL; AF203440; AAG35651.1; JOINED; Genomic_DNA.
DR EMBL; AF354757; AAL83977.1; -; mRNA.
DR EMBL; AK013424; BAB28849.3; -; mRNA.
DR EMBL; AK042372; BAC31242.1; -; mRNA.
DR EMBL; BC055721; AAH55721.1; -; mRNA.
DR CCDS; CCDS19650.1; -. [O35594-1]
DR RefSeq; NP_034009.2; NM_009879.3. [O35594-1]
DR RefSeq; XP_006530190.1; XM_006530127.3.
DR AlphaFoldDB; O35594; -.
DR SMR; O35594; -.
DR BioGRID; 198662; 5.
DR ComplexPortal; CPX-5028; IFT-B complex.
DR STRING; 10090.ENSMUSP00000031426; -.
DR iPTMnet; O35594; -.
DR PhosphoSitePlus; O35594; -.
DR EPD; O35594; -.
DR MaxQB; O35594; -.
DR PaxDb; O35594; -.
DR PRIDE; O35594; -.
DR ProteomicsDB; 267287; -. [O35594-1]
DR ProteomicsDB; 267288; -. [O35594-2]
DR Antibodypedia; 18491; 160 antibodies from 26 providers.
DR Ensembl; ENSMUST00000031426; ENSMUSP00000031426; ENSMUSG00000029469. [O35594-1]
DR GeneID; 12589; -.
DR KEGG; mmu:12589; -.
DR UCSC; uc008zlm.2; mouse. [O35594-1]
DR CTD; 28981; -.
DR MGI; MGI:1098597; Ift81.
DR VEuPathDB; HostDB:ENSMUSG00000029469; -.
DR eggNOG; ENOG502QSBR; Eukaryota.
DR GeneTree; ENSGT00390000000999; -.
DR HOGENOM; CLU_017012_1_0_1; -.
DR InParanoid; O35594; -.
DR OMA; WILTHME; -.
DR OrthoDB; 301582at2759; -.
DR PhylomeDB; O35594; -.
DR TreeFam; TF314635; -.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 12589; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Ift81; mouse.
DR PRO; PR:O35594; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O35594; protein.
DR Bgee; ENSMUSG00000029469; Expressed in spermatid and 246 other tissues.
DR ExpressionAtlas; O35594; baseline and differential.
DR Genevisible; O35594; MM.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030992; C:intraciliary transport particle B; IDA:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; IDA:MGI.
DR GO; GO:0097228; C:sperm principal piece; IDA:MGI.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; ISS:UniProtKB.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0120316; P:sperm flagellum assembly; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR Gene3D; 1.10.418.70; -; 1.
DR InterPro; IPR029600; IFT81.
DR InterPro; IPR041146; IFT81_CH.
DR InterPro; IPR043016; IFT81_N_sf.
DR PANTHER; PTHR15614; PTHR15614; 1.
DR Pfam; PF18383; IFT81_CH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Developmental protein; Differentiation; Phosphoprotein; Reference proteome;
KW Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WYA0"
FT CHAIN 2..676
FT /note="Intraflagellar transport protein 81 homolog"
FT /id="PRO_0000020918"
FT REGION 2..121
FT /note="CH (calponin-homology)-like region"
FT /evidence="ECO:0000250"
FT REGION 611..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 133..258
FT /evidence="ECO:0000255"
FT COILED 306..388
FT /evidence="ECO:0000255"
FT COILED 433..453
FT /evidence="ECO:0000255"
FT COILED 497..628
FT /evidence="ECO:0000255"
FT COMPBIAS 612..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYA0"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYA0"
FT VAR_SEQ 1..569
FT /note="Missing (in isoform CDV-1)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9187371"
FT /id="VSP_018785"
SQ SEQUENCE 676 AA; 79285 MW; DB059ACCFFDEBAE8 CRC64;
MSDQIKFIVD SLNKEPFKKN YNLITFDSLG PMQLLQVLND VLAEIDPKQD VDIREEMPEQ
TAKRMLNLLG ILKYKPPGNA TDMSTFRQGL VIGSKPVIYP VLHWLLQRSN ELKKRAYLAR
FLIKLEVPSE FLQDETVADT NKQYEELMEA FKTLHKECEQ LKTSGFSTAE IRRDISAMEE
EKDQLMKRVE RLKKRVETVQ NHQRMLKIAR QLRVEKEREE FLAQQKQEQK NQLFHAVQRL
QRVQNQLKSM RHAAADAKPE SLMKRLEEEI KFNSYMVTEK FPKELESKKK ELHFLQKVVS
EPAMGHSDLL ELETKVNEVN TEINQLIEKK MMRNEPIEGK LSLYRQQASI ISRKKEAKAE
ELQETKEKLA SLEREVLVKT NQTREFDGTE VLKGDEFKRY VSKLRSKSTV FKKKHQIIAE
FKAEFGLLQR TEELLKQRQE TIQHQLRTIE EKKGISGYSY TQEELERVSA LKSEVDEMKG
RTLDDMSEMV KKLNSLVSEK KSALAPVIKE LRQLRQKCQE LTQECDEKKA QYDSCAAGLE
SNRSKLEQEV RGLREECLQE ESKYHYTNCM IKNLEVELRR ATDEMKAYVS SDQQEKRKAI
REQYTKNITE QENLGKKLRE KQKAVRESHG PNMKQAKMWR DLEQLMECKK QCFLKQQSPA
SIGQVIQEGG EDRLVL
