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Q9QZQ1 (AFAD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. 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:
Afadin
Alternative name(s):
Protein Af-6
Gene names
Name:Mllt4
Synonyms:Af6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1820 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. May play a key role in the organization of epithelial structures of the embryonic ectoderm. Ref.2

Subunit structure

Homodimer. Interacts with F-actin, nectin and PVRL3/nectin-3. Essential for the association of nectin and E-cadherin. Isoform 2/s-afadindoes not interact with F-actin. Interacts with ZO-1 and occludin, but probably in an indirect manner. Interacts with RIT1, RIT2, NRXN1 and BCR By similarity. Ref.4

Subcellular location

Cell junctionadherens junction. Note: Not found at cell-matrix AJs.

Tissue specificity

Isoform 1 is expressed only in a restricted set of epithelial structures during early embryogenesis. Ref.2

Developmental stage

Highly expressed at restricted set of epithelial structures and highly concentrated at their junctional complex regions. At E6.5, localized at the most apical regions of cell-cell adhesion sites of the entire embryonic ectoderm; not detected in the extraembryonic regions. At E7.0, expressed in the primitive streak and the migrating paraxial mesoderm. At E7.5, highly expressed at the junctional complex regions in the primitive streak region (neuroepithelium) and the neural fold/grove region, but hardly detected in other areas of the ectoderm. By E8.5, highly expressed in the tail bud, somites and the paraxial mesoderm, concentrated at the junctional complex regions in neural tube, somites and pericardioperitoneal canal. Ref.2

Disruption phenotype

Mice show developmental defects at stages during and after gastrulation, including disorganization of the ectoderm, impaired migration of the mesoderm and loss of somites and other structures derived from both the ectoderm and mesoderm. Cell-cell adherens juntions and tight junctions are improperly organized in the ectoderm-derived cells. No redundancy exists in the function of afadin during gastrulation. Ref.2

Sequence similarities

Contains 1 dilute domain.

Contains 1 FHA domain.

Contains 1 PDZ (DHR) domain.

Contains 2 Ras-associating domains.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: Q9QZQ1-3)

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 1 (identifier: Q9QZQ1-2)

Also known as: l-afadin;

The sequence of this isoform differs from the canonical sequence as follows:
     393-407: Missing.
Isoform 2 (identifier: Q9QZQ1-1)

Also known as: s-afadin;

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18201820Afadin
PRO_0000215919

Regions

Domain39 – 13395Ras-associating 1
Domain246 – 348103Ras-associating 2
Domain426 – 49267FHA
Domain653 – 908256Dilute
Domain1007 – 109387PDZ
Coiled coil146 – 18641 Potential
Coiled coil1410 – 144637 Potential
Coiled coil1523 – 156139 Potential
Coiled coil1593 – 166573 Potential
Compositional bias163 – 17513Glu/Lys-rich
Compositional bias1346 – 139247Pro-rich
Compositional bias1676 – 170631Pro-rich
Compositional bias1733 – 17364Poly-Glu

Amino acid modifications

Modified residue2161Phosphoserine Ref.6
Modified residue5571Phosphoserine Ref.7
Modified residue11071Phosphoserine Ref.8
Modified residue11821Phosphoserine Ref.8
Modified residue12321Phosphothreonine By similarity
Modified residue17191Phosphoserine By similarity
Modified residue17951Phosphoserine By similarity
Modified residue18031N6-acetyllysine Ref.9

Natural variations

Alternative sequence393 – 40715Missing in isoform 1.
VSP_026731

Experimental info

Sequence conflict231N → Y in AAD54283. Ref.2
Sequence conflict1011E → EE in AK016557. Ref.3
Sequence conflict6941N → D in AK016557. Ref.3
Sequence conflict897 – 9004DLIE → PEMR in AK016557. Ref.3

Secondary structure

.................................................................. 1820
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified July 10, 2007. Version 3.
Checksum: 9FA4F378D840D8B1

FASTA1,820206,499
        10         20         30         40         50         60 
MSAGGRDEER RKLADIIHHW NANRLDLFEI SQPTEDLEFH GVMRFYFQDK AAGNFATKCI 

        70         80         90        100        110        120 
RVSSTATTQD VIETLAEKFR PDMRMLSSPK YSLYEVHVSG ERRLDIDEKP LVVQLNWNKD 

       130        140        150        160        170        180 
DREGRFVLKN ENDAIPAKKA QSNGPEKQEK EGVIQNFKRT LSKKEKKEKK KKEKEALRQA 

       190        200        210        220        230        240 
SDKEERPSQG DDSENSRLAA EVYKDMPETS FTRTISNPEV VMKRRRQQKL EKRMQEFRSS 

       250        260        270        280        290        300 
DGRPDSGGTL RIYADSLKPN IPYKTILLST TDTADFAVAE SLEKYGLEKE NPKDYCIARV 

       310        320        330        340        350        360 
MLPPGAQHSD ERGAKEIILD DDECPLQIFR EWPSDKGILV FQLKRRPPDY IPKKMKKHVE 

       370        380        390        400        410        420 
GKSLKGKDRA DGSGYGSALP PEKLPYLVEL SPGRRNHFAY YSYHTYEDGS DSRDKPKLYR 

       430        440        450        460        470        480 
LQLSVTEVGT EKFDDNSIQL FGPGIQPHHC DLTNMDGVVT VTPRSMDAET YVDGQRISET 

       490        500        510        520        530        540 
TMLQSGMRLQ FGTSHVFKFV DPIQDHVLSK RSVDGGLMVK GPRHKPGAVQ ETTFELGGDV 

       550        560        570        580        590        600 
HSGTALPASR STTRLDSDRV SSASSTAERG MVKPMIRLDQ EQEYRRRENR TQDATGPELI 

       610        620        630        640        650        660 
LPASIEFRES SEDSFLSAII NYTNSSTVHF KLSPTYVLYM ACRYVLSSQH RPDISPTERT 

       670        680        690        700        710        720 
HKAIAVVNKM VSMMEGVIQK QKNIAGALAF WMANASELLN FIKQDRDLSR ITLDAQDVLA 

       730        740        750        760        770        780 
HLVQMAFKYL VHCLQSELNN YMPAFLDDPE ENSLQRPKID DVLHTLTGAM SLLRRCRVNA 

       790        800        810        820        830        840 
ALTIQLFSQL FHFINMWLFN RLVTDPDSGL CSHYWGAIIR QQLGHIEAWA EKQGLELAAD 

       850        860        870        880        890        900 
CHLSRIVQAT TLLTMDKYVP DDIPNINSTC FKLNSLQLQA LLQNYHCAPD EPFIPTDLIE 

       910        920        930        940        950        960 
NVVAVAENTA DELARSDGRD VQLEEDPDLQ LPFLLPEDGY SCDVVRNIPN GLQEFLDPLC 

       970        980        990       1000       1010       1020 
QRGFCRLVPH TRSPGTWTIY FEGADYESHL MRENAELAQP LRKEPEIITV TLKKQNGMGL 

      1030       1040       1050       1060       1070       1080 
SIVAAKGAGQ DKLGIYVKSV VKGGAADVDG RLAAGDQLLS VDGRSLVGLS QERAAELMTR 

      1090       1100       1110       1120       1130       1140 
TSSVVTLEVA KQGAIYHGLA TLLNQPSPMM QRISDRRGSG KPRPKSEGFE LYNNSAQNGS 

      1150       1160       1170       1180       1190       1200 
PESPQMPWTE YSEPKKLPGD DRLMKNRADH RSSPNVANQP PSPGGKGPYT SGTAAKITSV 

      1210       1220       1230       1240       1250       1260 
STGNLCTEEQ SPPPRPEAYP IPTQTYTREY FTFPASKSQD RMAPPQSQWP NYEEKPHVHT 

      1270       1280       1290       1300       1310       1320 
ESNHSSIAIQ RVTRSQEELR EEKVYQLERH RVEAGMDRKC DSDMWINQSS SVESSTSSQE 

      1330       1340       1350       1360       1370       1380 
HLNHSSKSVT PASTLTKSGP GRWKTPAAVL PTPVAVSQPI RTDLPPPPPP PPVHYTSEFD 

      1390       1400       1410       1420       1430       1440 
GIPMDLPLPP PPANQAGPQS AQVAAAEWKK REEHQRWYEK EKARLEEERE RKRREQERKL 

      1450       1460       1470       1480       1490       1500 
GQMRSQTLNP ASFSPLATQA KPEKPSTLQR PQETVIRELQ PQQQPRTIER KDLQYITISK 

      1510       1520       1530       1540       1550       1560 
EELSSGDSLS PDPWKRDARE KLEKQQQMHI VDMLSKEIHE LQNKVDRTAE ESDRLRKLML 

      1570       1580       1590       1600       1610       1620 
EWQFQKRLQE SKQKDEDDDE EEDDDVDTML IMQRLEAERR ARMQDEERRR QQQLEEMRKR 

      1630       1640       1650       1660       1670       1680 
EAEDRVRQEE DGRHQEEERV KRDAEEKRRQ EEGYYSRLEA ERRRQHEEAA RRLLEPEEPG 

      1690       1700       1710       1720       1730       1740 
LSRPPLPRDY EPPSLSSAPC APPPPPQRNA SYLKTQVLSP DSLFTAKFVA YDEEEEDYGP 

      1750       1760       1770       1780       1790       1800 
AGPNSYSGSA GTAVGAYDAP REAREKLTRS QDADLPGSSG APENLTFKER QRLFSQGQDV 

      1810       1820 
SDKVKASRKL TELENELNTK 

« Hide

Isoform 1 (l-afadin) [UniParc].

Checksum: 5987A16BA9F28C2E
Show »

FASTA1,805204,553
Isoform 2 (s-afadin) (Sequence not available).

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"Afadin: a key molecule essential for structural organization of cell-cell junctions of polarized epithelia during embryogenesis."
Ikeda W., Nakanishi H., Miyoshi J., Mandai K., Ishizaki H., Tanaka M., Togawa A., Takahashi K., Nishioka H., Yoshida H., Mizoguchi A., Nishikawa S., Takai Y.
J. Cell Biol. 146:1117-1132(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-320 (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
Strain: C57BL/6.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-900 (ISOFORM 3).
Tissue: Leukemia.
[4]"Nectin-3: a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities."
Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M., Nishimura M., Tachibana K., Mizoguchi A., Takai Y.
J. Biol. Chem. 275:10291-10299(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PVRL3.
[5]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107 AND SER-1182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[9]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1803, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[10]"Solution structure of the FHA domain and RAS-binding domain in mouse AF-6 protein."
RIKEN structural genomics initiative (RSGI)
Submitted (JUL-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 246-487.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC155253 Genomic DNA. No translation available.
CAAA01106165 Genomic DNA. No translation available.
CAAA01134612 Genomic DNA. No translation available.
CAAA01201738 Genomic DNA. No translation available.
CAAA01218165 Genomic DNA. No translation available.
AF172447 mRNA. Translation: AAD54283.1.
AK016557 mRNA. No translation available.
CCDSCCDS49955.1. [Q9QZQ1-3]
RefSeqNP_034936.1. NM_010806.1. [Q9QZQ1-3]
UniGeneMm.59167.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLNNMR-A381-502[»]
1WXANMR-A246-348[»]
3AXAX-ray2.78A/B1003-1095[»]
ProteinModelPortalQ9QZQ1.
SMRQ9QZQ1. Positions 42-135, 249-348, 381-502, 604-936, 1001-1096, 1507-1685.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201438. 5 interactions.
DIPDIP-60737N.
IntActQ9QZQ1. 2 interactions.

PTM databases

PhosphoSiteQ9QZQ1.

Proteomic databases

MaxQBQ9QZQ1.
PaxDbQ9QZQ1.
PRIDEQ9QZQ1.

Protocols and materials databases

DNASU17356.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000139666; ENSMUSP00000118318; ENSMUSG00000068036. [Q9QZQ1-3]
ENSMUST00000150848; ENSMUSP00000122447; ENSMUSG00000068036. [Q9QZQ1-2]
GeneID17356.
KEGGmmu:17356.
UCSCuc008amr.1. mouse. [Q9QZQ1-3]

Organism-specific databases

CTD4301.
MGIMGI:1314653. Mllt4.

Phylogenomic databases

eggNOGNOG291597.
GeneTreeENSGT00390000010033.
HOGENOMHOG000008041.
HOVERGENHBG050463.
InParanoidQ9QZQ1.
KOK05702.
OrthoDBEOG7G4QDD.
PhylomeDBQ9QZQ1.
TreeFamTF350731.

Gene expression databases

ArrayExpressQ9QZQ1.
BgeeQ9QZQ1.
GenevestigatorQ9QZQ1.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
2.60.200.20. 1 hit.
InterProIPR018444. Dil_domain.
IPR002710. Dilute.
IPR000253. FHA_dom.
IPR001478. PDZ.
IPR000159. Ras-assoc.
IPR008984. SMAD_FHA_domain.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF01843. DIL. 1 hit.
PF00498. FHA. 1 hit.
PF00595. PDZ. 1 hit.
PF00788. RA. 2 hits.
[Graphical view]
SMARTSM00240. FHA. 1 hit.
SM00228. PDZ. 1 hit.
SM00314. RA. 2 hits.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 2 hits.
PROSITEPS51126. DILUTE. 1 hit.
PS50106. PDZ. 1 hit.
PS50200. RA. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMLLT4. mouse.
EvolutionaryTraceQ9QZQ1.
NextBio291962.
PROQ9QZQ1.
SOURCESearch...

Entry information

Entry nameAFAD_MOUSE
AccessionPrimary (citable) accession number: Q9QZQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 10, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot