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Q8WYA0 (IFT81_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Intraflagellar transport protein 81 homolog
Alternative name(s):
Carnitine deficiency-associated protein expressed in ventricle 1
Short name=CDV-1
Gene names
Name:IFT81
Synonyms:CDV1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length676 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the intraflagellar transport (IFT) complex B: together with IFT74, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds tubulin via its CH (calponin-homology)-like region. Required for ciliogenesis. Ref.11

Subunit structure

Component of the IFT complex B, at least composed of IFT20, IFT25/HSPB11, IFT27, IFT52, IFT57, IFT74, IFT81, IFT88 and TRAF3IP1. Interacts with IFT74; the interaction is direct: within the IFT complex B, IFT74 and IFT81 mediate the transport of tubulin within the cilium. Interacts with tubulin; interaction is direct. Interacts with RABL2/RABL2A; binding is equal in the presence of GTP or GDP. Ref.7 Ref.11

Subcellular location

Cell projectioncilium Probable Ref.11.

Tissue specificity

Highly expressed in testis, moderately in ovary, heart, liver, skeletal muscle, kidney and pancreas, low in prostate, brain, placenta and lung and not detected in spleen, thymus, small intestine and colon. Isoform CDV-1R is abundantly expressed in testis. Ref.2

Domain

The CH (calponin-homology)-like region shows high similarity to a CH (calponin-homology) domain and mediated binding to the globular domain of tubulin (Ref.11).

Sequence similarities

Belongs to the IFT81 family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform CDV-1R Ref.1 Ref.2 (identifier: Q8WYA0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8WYA0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     397-431: FKRYVNKLRSKSTVFKKKHQIIAELKAEFGLLQRT → RQDLTLSPRLECGGVIMAYCSLKLLGSSDPPTSAS
     432-676: Missing.
Note: No experimental confirmation available.
Isoform CDV-1 (identifier: Q8WYA0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-569: Missing.
Note: Produced by alternative initiation at Met-570 of isoform CDV-1R.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 676675Intraflagellar transport protein 81 homolog
PRO_0000020916

Regions

Region2 – 121120CH (calponin-homology)-like region
Coiled coil132 – 258127 Potential
Coiled coil306 – 38984 Potential
Coiled coil416 – 45641 Potential
Coiled coil490 – 622133 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.10
Modified residue611Phosphothreonine Ref.8

Natural variations

Alternative sequence1 – 569569Missing in isoform CDV-1.
VSP_018784
Alternative sequence397 – 43135FKRYV…LLQRT → RQDLTLSPRLECGGVIMAYC SLKLLGSSDPPTSAS in isoform 2.
VSP_050695
Alternative sequence432 – 676245Missing in isoform 2.
VSP_050696

Experimental info

Mutagenesis73 – 753KYK → EYE: Abolishes tubulin-binding and impaired ciliogenesis; when associated with 113-E-E-114. Ref.11
Mutagenesis113 – 1142KK → EE: Abolishes tubulin-binding and impaired ciliogenesis; when associated with 73-E--E-75.
Sequence conflict591E → K in BAC03690. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform CDV-1R [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: E5EBD887A6BF953E

FASTA67679,746
        10         20         30         40         50         60 
MSDQIKFIMD SLNKEPFRKN YNLITFDSLE PMQLLQVLSD VLAEIDPKQL VDIREEMPEQ 

        70         80         90        100        110        120 
TAKRMLSLLG ILKYKPSGNA TDMSTFRQGL VIGSKPVIYP VLHWLLQRTN ELKKRAYLAR 

       130        140        150        160        170        180 
FLIKLEVPSE FLQDETVADT NKQYEELMEA FKTLHKEYEQ LKISGFSTAE IRKDISAMEE 

       190        200        210        220        230        240 
EKDQLIKRVE HLKKRVETAQ NHQWMLKIAR QLRVEKEREE YLAQQKQEQK NQLFHAVQRL 

       250        260        270        280        290        300 
QRVQNQLKSM RQAAADAKPE SLMKRLEEEI KFNLYMVTEK FPKELENKKK ELHFLQKVVS 

       310        320        330        340        350        360 
EPAMGHSDLL ELESKINEIN TEINQLIEKK MMRNEPIEGK LSLYRQQASI ISRKKEAKAE 

       370        380        390        400        410        420 
ELQEAKEKLA SLEREASVKR NQTREFDGTE VLKGDEFKRY VNKLRSKSTV FKKKHQIIAE 

       430        440        450        460        470        480 
LKAEFGLLQR TEELLKQRHE NIQQQLQTME EKKGISGYSY TQEELERVSA LKSEVDEMKG 

       490        500        510        520        530        540 
RTLDDMSEMV KKLYSLVSEK KSALASVIKE LRQLRQKYQE LTQECDEKKS QYDSCAAGLE 

       550        560        570        580        590        600 
SNRSKLEQEV RRLREECLQE ESRYHYTNCM IKNLEVQLRR ATDEMKAYIS SDQQEKRKAI 

       610        620        630        640        650        660 
REQYTKNTAE QENLGKKLRE KQKVIRESHG PNMKQAKMWR DLEQLMECKK QCFLKQQSQT 

       670 
SIGQVIQEGG EDRLIL 

« Hide

Isoform 2 [UniParc].

Checksum: D6C78C86420CE32C
Show »

FASTA43150,241
Isoform CDV-1 [UniParc].

Checksum: 2721396F751403AC
Show »

FASTA10712,667

References

« Hide 'large scale' references
[1]"Genomic organization and mapping of mouse CDV (carnitine deficiency-associated gene expressed in ventricle)-1 and its related CDV-1R gene."
Higashi M., Kobayashi K., Iijima M., Wakana S., Horiuchi M., Yasuda T., Yoshida G., Kanmura Y., Saheki T.
Mamm. Genome 11:1053-1057(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CDV-1R).
Tissue: Lymphocyte.
[2]"Identification of human CDV-1R and mouse Cdv-1R, two novel proteins with putative signal peptides, especially highly expressed in testis and increased with the male sex maturation."
Peng J., Yu L., Horiuchi M., Zhang P., Huang X., Zhang Y., Li D., Jalil M.A., Zhao S.
Mol. Biol. Rep. 29:353-362(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CDV-1R), TISSUE SPECIFICITY.
Tissue: Testis.
[3]Hu G.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CDV-1).
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND CDV-1).
Tissue: Skeletal muscle and Uterus.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-676 (ISOFORM CDV-1R).
Tissue: Fetal brain.
[7]"Characterization of the intraflagellar transport complex B core: direct interaction of the IFT81 and IFT74/72 subunits."
Lucker B.F., Behal R.H., Qin H., Siron L.C., Taggart W.D., Rosenbaum J.L., Cole D.G.
J. Biol. Chem. 280:27688-27696(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IFT74.
[8]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Molecular basis of tubulin transport within the cilium by IFT74 and IFT81."
Bhogaraju S., Cajanek L., Fort C., Blisnick T., Weber K., Taschner M., Mizuno N., Lamla S., Bastin P., Nigg E.A., Lorentzen E.
Science 341:1009-1012(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE IFT COMPLEX B, INTERACTION WITH TUBULIN AND IFT74, MUTAGENESIS OF 73-LYS--LYS-75 AND 113-LYS-LYS-114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF250326 mRNA. Translation: AAL50343.1.
AF332010 mRNA. Translation: AAO32947.1.
AF139540 mRNA. Translation: AAP97269.1.
AF078932 mRNA. Translation: AAD48091.1.
CH471054 Genomic DNA. Translation: EAW97898.1.
BC004536 mRNA. Translation: AAH04536.2.
BC029349 mRNA. Translation: AAH29349.1.
BC108257 mRNA. Translation: AAI08258.1.
AK091549 mRNA. Translation: BAC03690.1. Sequence problems.
RefSeqNP_001137251.1. NM_001143779.1.
NP_054774.2. NM_014055.3.
NP_113661.2. NM_031473.3.
UniGeneHs.528382.

3D structure databases

ProteinModelPortalQ8WYA0.
SMRQ8WYA0. Positions 5-122.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118802. 3 interactions.
STRING9606.ENSP00000242591.

PTM databases

PhosphoSiteQ8WYA0.

Polymorphism databases

DMDM48474907.

Proteomic databases

PaxDbQ8WYA0.
PRIDEQ8WYA0.

Protocols and materials databases

DNASU28981.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242591; ENSP00000242591; ENSG00000122970. [Q8WYA0-1]
ENST00000361948; ENSP00000355372; ENSG00000122970. [Q8WYA0-3]
ENST00000552912; ENSP00000449718; ENSG00000122970. [Q8WYA0-1]
GeneID28981.
KEGGhsa:28981.
UCSCuc001tqg.3. human. [Q8WYA0-3]
uc001tqh.3. human. [Q8WYA0-1]

Organism-specific databases

CTD28981.
GeneCardsGC12P110562.
HGNCHGNC:14313. IFT81.
HPAHPA019087.
HPA020051.
MIM605489. gene.
neXtProtNX_Q8WYA0.
PharmGKBPA26349.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG77882.
HOGENOMHOG000237323.
HOVERGENHBG048817.
InParanoidQ8WYA0.
OMAYPVLHWL.
OrthoDBEOG7JHM54.
PhylomeDBQ8WYA0.
TreeFamTF314635.

Gene expression databases

ArrayExpressQ8WYA0.
BgeeQ8WYA0.
CleanExHS_IFT81.
GenevestigatorQ8WYA0.

Family and domain databases

ProtoNetSearch...

Other

ChiTaRSIFT81. human.
GeneWikiIFT81.
GenomeRNAi28981.
NextBio51867.
PROQ8WYA0.
SOURCESearch...

Entry information

Entry nameIFT81_HUMAN
AccessionPrimary (citable) accession number: Q8WYA0
Secondary accession number(s): Q2YDY1 expand/collapse secondary AC list , Q8NB51, Q9BSV2, Q9UNY8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM