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Protein

Afadin

Gene

Afdn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • cadherin binding Source: MGI
  • cell adhesion molecule binding Source: BHF-UCL
  • Ras GTPase binding Source: MGI

GO - Biological processi

  • adherens junction maintenance Source: MGI
  • brain morphogenesis Source: MGI
  • cell adhesion Source: UniProtKB-KW
  • cerebral cortex development Source: MGI
  • establishment of endothelial intestinal barrier Source: MGI
  • homeostasis of number of cells Source: MGI
  • neuroepithelial cell differentiation Source: MGI
  • positive regulation of GTPase activity Source: MGI
  • protein localization to cell junction Source: MGI
  • radial glial cell differentiation Source: MGI
  • regulation of oligodendrocyte progenitor proliferation Source: MGI
  • regulation of protein localization Source: GO_Central
  • signal transduction Source: InterPro
  • telencephalon development Source: MGI

Keywordsi

Biological processCell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-418990 Adherens junctions interactions

Names & Taxonomyi

Protein namesi
Recommended name:
Afadin
Alternative name(s):
Afadin adherens junction formation factorImported
Protein Af-6
Gene namesi
Name:AfdnImported
Synonyms:Af6, Mllt4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1314653 Afdn

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002159191 – 1820AfadinAdd BLAST1820

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei216PhosphoserineCombined sources1
Modified residuei246PhosphoserineBy similarity1
Modified residuei256PhosphoserineBy similarity1
Modified residuei391PhosphoserineBy similarity1
Modified residuei424PhosphoserineBy similarity1
Modified residuei512PhosphoserineBy similarity1
Modified residuei557PhosphoserineCombined sources1
Modified residuei562PhosphoserineBy similarity1
Modified residuei655PhosphoserineBy similarity1
Modified residuei1083PhosphoserineCombined sources1
Modified residuei1107PhosphoserineCombined sources1
Modified residuei1126PhosphoserineCombined sources1
Modified residuei1140PhosphoserineBy similarity1
Modified residuei1143PhosphoserineCombined sources1
Modified residuei1172PhosphoserineCombined sources1
Modified residuei1173PhosphoserineBy similarity1
Modified residuei1182PhosphoserineCombined sources1
Modified residuei1199PhosphoserineBy similarity1
Modified residuei1232PhosphothreonineBy similarity1
Modified residuei1238PhosphoserineBy similarity1
Modified residuei1275PhosphoserineBy similarity1
Modified residuei1328PhosphoserineBy similarity1
Modified residuei1330PhosphothreonineBy similarity1
Modified residuei1499PhosphoserineBy similarity1
Modified residuei1510PhosphoserineCombined sources1
Modified residuei1694PhosphoserineBy similarity1
Modified residuei1719PhosphoserineCombined sources1
Modified residuei1770PhosphoserineCombined sources1
Modified residuei1795PhosphoserineCombined sources1
Modified residuei1803N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9QZQ1
PeptideAtlasiQ9QZQ1
PRIDEiQ9QZQ1

PTM databases

iPTMnetiQ9QZQ1
PhosphoSitePlusiQ9QZQ1

Expressioni

Tissue specificityi

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

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiENSMUSG00000068036
ExpressionAtlasiQ9QZQ1 baseline and differential
GenevisibleiQ9QZQ1 MM

Interactioni

Subunit structurei

Homodimer. Interacts with F-actin, nectin and NECTIN3. Essential for the association of nectin and E-cadherin. Isoform 2/s-afadin does 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).By similarity

GO - Molecular functioni

  • cadherin binding Source: MGI
  • cell adhesion molecule binding Source: BHF-UCL
  • Ras GTPase binding Source: MGI

Protein-protein interaction databases

BioGridi201438, 6 interactors
DIPiDIP-60737N
IntActiQ9QZQ1, 5 interactors
STRINGi10090.ENSMUSP00000118318

Structurei

Secondary structure

11820
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 46Combined sources7
Beta strandi57 – 63Combined sources7
Helixi68 – 79Combined sources12
Beta strandi91 – 97Combined sources7
Beta strandi100 – 103Combined sources4
Helixi110 – 114Combined sources5
Beta strandi125 – 130Combined sources6
Beta strandi249 – 252Combined sources4
Turni255 – 257Combined sources3
Beta strandi259 – 261Combined sources3
Beta strandi264 – 267Combined sources4
Helixi274 – 285Combined sources12
Beta strandi288 – 290Combined sources3
Turni292 – 294Combined sources3
Beta strandi295 – 301Combined sources7
Beta strandi308 – 311Combined sources4
Beta strandi315 – 317Combined sources3
Helixi325 – 330Combined sources6
Helixi334 – 336Combined sources3
Beta strandi339 – 345Combined sources7
Helixi381 – 383Combined sources3
Beta strandi386 – 390Combined sources5
Beta strandi418 – 420Combined sources3
Beta strandi423 – 427Combined sources5
Beta strandi429 – 431Combined sources3
Beta strandi450 – 457Combined sources8
Beta strandi459 – 464Combined sources6
Beta strandi466 – 468Combined sources3
Beta strandi470 – 474Combined sources5
Beta strandi481 – 483Combined sources3
Beta strandi488 – 491Combined sources4
Turni492 – 494Combined sources3
Beta strandi495 – 500Combined sources6
Beta strandi1007 – 1013Combined sources7
Beta strandi1015 – 1017Combined sources3
Beta strandi1019 – 1026Combined sources8
Beta strandi1031 – 1041Combined sources11
Helixi1045 – 1049Combined sources5
Beta strandi1057 – 1061Combined sources5
Helixi1071 – 1079Combined sources9
Beta strandi1083 – 1090Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WLNNMR-A381-502[»]
1WXANMR-A246-348[»]
3AXAX-ray2.78A/B1003-1095[»]
6AMBX-ray2.50B38-136[»]
ProteinModelPortaliQ9QZQ1
SMRiQ9QZQ1
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QZQ1

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 133Ras-associating 1PROSITE-ProRule annotationAdd BLAST95
Domaini246 – 348Ras-associating 2PROSITE-ProRule annotationAdd BLAST103
Domaini426 – 492FHAAdd BLAST67
Domaini653 – 908DilutePROSITE-ProRule annotationAdd BLAST256
Domaini1007 – 1093PDZPROSITE-ProRule annotationAdd BLAST87

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili146 – 186Sequence analysisAdd BLAST41
Coiled coili1410 – 1446Sequence analysisAdd BLAST37
Coiled coili1523 – 1561Sequence analysisAdd BLAST39
Coiled coili1593 – 1665Sequence analysisAdd BLAST73

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi163 – 175Glu/Lys-richAdd BLAST13
Compositional biasi1346 – 1392Pro-richAdd BLAST47
Compositional biasi1676 – 1706Pro-richAdd BLAST31
Compositional biasi1733 – 1736Poly-Glu4

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG1892 Eukaryota
ENOG410XR0S LUCA
GeneTreeiENSGT00390000010033
HOGENOMiHOG000008041
HOVERGENiHBG050463
InParanoidiQ9QZQ1
KOiK05702
PhylomeDBiQ9QZQ1
TreeFamiTF350731

Family and domain databases

CDDicd00060 FHA, 1 hit
cd15471 Myo5p-like_CBD_afadin, 1 hit
InterProiView protein in InterPro
IPR028842 Afadin
IPR037977 CBD_Afadin
IPR002710 Dilute_dom
IPR000253 FHA_dom
IPR001478 PDZ
IPR036034 PDZ_sf
IPR000159 RA_dom
IPR008984 SMAD_FHA_dom_sf
IPR029071 Ubiquitin-like_domsf
PANTHERiPTHR10398 PTHR10398, 1 hit
PfamiView protein in Pfam
PF01843 DIL, 1 hit
PF00498 FHA, 1 hit
PF00595 PDZ, 1 hit
PF00788 RA, 2 hits
SMARTiView protein in SMART
SM01132 DIL, 1 hit
SM00240 FHA, 1 hit
SM00228 PDZ, 1 hit
SM00314 RA, 2 hits
SUPFAMiSSF49879 SSF49879, 1 hit
SSF50156 SSF50156, 1 hit
SSF54236 SSF54236, 2 hits
PROSITEiView protein in PROSITE
PS51126 DILUTE, 1 hit
PS50106 PDZ, 1 hit
PS50200 RA, 2 hits

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 3 (identifier: Q9QZQ1-3) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSAGGRDEER RKLADIIHHW NANRLDLFEI SQPTEDLEFH GVMRFYFQDK
60 70 80 90 100
AAGNFATKCI RVSSTATTQD VIETLAEKFR PDMRMLSSPK YSLYEVHVSG
110 120 130 140 150
ERRLDIDEKP LVVQLNWNKD DREGRFVLKN ENDAIPAKKA QSNGPEKQEK
160 170 180 190 200
EGVIQNFKRT LSKKEKKEKK KKEKEALRQA SDKEERPSQG DDSENSRLAA
210 220 230 240 250
EVYKDMPETS FTRTISNPEV VMKRRRQQKL EKRMQEFRSS DGRPDSGGTL
260 270 280 290 300
RIYADSLKPN IPYKTILLST TDTADFAVAE SLEKYGLEKE NPKDYCIARV
310 320 330 340 350
MLPPGAQHSD ERGAKEIILD DDECPLQIFR EWPSDKGILV FQLKRRPPDY
360 370 380 390 400
IPKKMKKHVE GKSLKGKDRA DGSGYGSALP PEKLPYLVEL SPGRRNHFAY
410 420 430 440 450
YSYHTYEDGS DSRDKPKLYR LQLSVTEVGT EKFDDNSIQL FGPGIQPHHC
460 470 480 490 500
DLTNMDGVVT VTPRSMDAET YVDGQRISET TMLQSGMRLQ FGTSHVFKFV
510 520 530 540 550
DPIQDHVLSK RSVDGGLMVK GPRHKPGAVQ ETTFELGGDV HSGTALPASR
560 570 580 590 600
STTRLDSDRV SSASSTAERG MVKPMIRLDQ EQEYRRRENR TQDATGPELI
610 620 630 640 650
LPASIEFRES SEDSFLSAII NYTNSSTVHF KLSPTYVLYM ACRYVLSSQH
660 670 680 690 700
RPDISPTERT HKAIAVVNKM VSMMEGVIQK QKNIAGALAF WMANASELLN
710 720 730 740 750
FIKQDRDLSR ITLDAQDVLA HLVQMAFKYL VHCLQSELNN YMPAFLDDPE
760 770 780 790 800
ENSLQRPKID DVLHTLTGAM SLLRRCRVNA ALTIQLFSQL FHFINMWLFN
810 820 830 840 850
RLVTDPDSGL CSHYWGAIIR QQLGHIEAWA EKQGLELAAD CHLSRIVQAT
860 870 880 890 900
TLLTMDKYVP DDIPNINSTC FKLNSLQLQA LLQNYHCAPD EPFIPTDLIE
910 920 930 940 950
NVVAVAENTA DELARSDGRD VQLEEDPDLQ LPFLLPEDGY SCDVVRNIPN
960 970 980 990 1000
GLQEFLDPLC QRGFCRLVPH TRSPGTWTIY FEGADYESHL MRENAELAQP
1010 1020 1030 1040 1050
LRKEPEIITV TLKKQNGMGL SIVAAKGAGQ DKLGIYVKSV VKGGAADVDG
1060 1070 1080 1090 1100
RLAAGDQLLS VDGRSLVGLS QERAAELMTR TSSVVTLEVA KQGAIYHGLA
1110 1120 1130 1140 1150
TLLNQPSPMM QRISDRRGSG KPRPKSEGFE LYNNSAQNGS PESPQMPWTE
1160 1170 1180 1190 1200
YSEPKKLPGD DRLMKNRADH RSSPNVANQP PSPGGKGPYT SGTAAKITSV
1210 1220 1230 1240 1250
STGNLCTEEQ SPPPRPEAYP IPTQTYTREY FTFPASKSQD RMAPPQSQWP
1260 1270 1280 1290 1300
NYEEKPHVHT ESNHSSIAIQ RVTRSQEELR EEKVYQLERH RVEAGMDRKC
1310 1320 1330 1340 1350
DSDMWINQSS SVESSTSSQE HLNHSSKSVT PASTLTKSGP GRWKTPAAVL
1360 1370 1380 1390 1400
PTPVAVSQPI RTDLPPPPPP PPVHYTSEFD GIPMDLPLPP PPANQAGPQS
1410 1420 1430 1440 1450
AQVAAAEWKK REEHQRWYEK EKARLEEERE RKRREQERKL GQMRSQTLNP
1460 1470 1480 1490 1500
ASFSPLATQA KPEKPSTLQR PQETVIRELQ PQQQPRTIER KDLQYITISK
1510 1520 1530 1540 1550
EELSSGDSLS PDPWKRDARE KLEKQQQMHI VDMLSKEIHE LQNKVDRTAE
1560 1570 1580 1590 1600
ESDRLRKLML EWQFQKRLQE SKQKDEDDDE EEDDDVDTML IMQRLEAERR
1610 1620 1630 1640 1650
ARMQDEERRR QQQLEEMRKR EAEDRVRQEE DGRHQEEERV KRDAEEKRRQ
1660 1670 1680 1690 1700
EEGYYSRLEA ERRRQHEEAA RRLLEPEEPG LSRPPLPRDY EPPSLSSAPC
1710 1720 1730 1740 1750
APPPPPQRNA SYLKTQVLSP DSLFTAKFVA YDEEEEDYGP AGPNSYSGSA
1760 1770 1780 1790 1800
GTAVGAYDAP REAREKLTRS QDADLPGSSG APENLTFKER QRLFSQGQDV
1810 1820
SDKVKASRKL TELENELNTK
Length:1,820
Mass (Da):206,499
Last modified:July 10, 2007 - v3
Checksum:i9FA4F378D840D8B1
GO
Isoform 1 (identifier: Q9QZQ1-2) [UniParc]FASTAAdd to basket
Also known as: l-afadin

The sequence of this isoform differs from the canonical sequence as follows:
     393-407: Missing.

Show »
Length:1,805
Mass (Da):204,553
Checksum:i5987A16BA9F28C2E
GO
Isoform 2 (identifier: Q9QZQ1-1)
Also known as: s-afadin
Sequence is not available
Length:
Mass (Da):

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23N → Y in AAD54283 (PubMed:10477764).Curated1
Sequence conflicti101E → EE in AK016557 (PubMed:16141072).Curated1
Sequence conflicti694N → D in AK016557 (PubMed:16141072).Curated1
Sequence conflicti897 – 900DLIE → PEMR in AK016557 (PubMed:16141072).Curated4

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_026731393 – 407Missing in isoform 1. 1 PublicationAdd BLAST15

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS49955.1 [Q9QZQ1-3]
RefSeqiNP_034936.1, NM_010806.1 [Q9QZQ1-3]
UniGeneiMm.59167

Genome annotation databases

EnsembliENSMUST00000139666; ENSMUSP00000118318; ENSMUSG00000068036 [Q9QZQ1-3]
ENSMUST00000150848; ENSMUSP00000122447; ENSMUSG00000068036 [Q9QZQ1-2]
GeneIDi17356
KEGGimmu:17356
UCSCiuc008amr.1 mouse [Q9QZQ1-3]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiAFAD_MOUSE
AccessioniPrimary (citable) accession number: Q9QZQ1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 10, 2007
Last modified: March 28, 2018
This is version 145 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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