Reviewed, UniProtKB/Swiss-Prot O76329 (ACTNB_DICDI)

Names and origin

Protein names

Recommended name:
    Interaptin
Alternative name(s):
    Alpha-actinin B
    Actin-binding protein D

Gene names

Name:	abpD
Synonyms:	actnB
ORF Names:	DDB_G0287291

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	1738 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May function as linker between cellular membranes and the actin cytoskeleton. Required for normal development of fruiting bodies. Ref.3
Subcellular location	Nucleus membrane; Single-pass type IV membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane. Golgi apparatus › Golgi stack membrane. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton. Note: The largest part of the protein is cytoplasmic, while its C-terminal part is associated either with the nuclear envelope, the Golgi membrane or the endoplasmic reticulum membrane. Ref.1
Developmental stage	Present at very low levels during early stages of development. Levels increase during late aggregation stage, reach a maximum and remain high during culmination and maturation of the fruiting body. Detected in upper and lower cup structures in late culminants and mature fruiting bodies (at protein level). First detected after 12 hours of development. Highly expressed at 12 to 16 hours of development. Levels return to basal levels during maturation of the fruiting body. Ref.1
Induction	Up-regulated by cAMP. Ref.1
Disruption phenotype	Cells have reduced efficiency in fruiting body formation and reduced spore viability. Ref.3
Sequence similarities	Belongs to the alpha-actinin family. Contains 1 actin-binding domain. Contains 2 CH (calponin-homology) domains.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Endoplasmic reticulum Golgi apparatus Membrane Nucleus
Domain	Coiled coil Repeat Transmembrane
Ligand	Actin-binding
Molecular function	Developmental protein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell-cell adhesion Ref.1 Inferred from mutant phenotype. Source: dictyBase multicellular organismal development Ref.3 Inferred from mutant phenotype. Source: dictyBase spore germination Ref.3 Inferred from mutant phenotype. Source: dictyBase
Cellular component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell centrosome Ref.4 Inferred from direct assay. Source: dictyBase endoplasmic reticulum membrane Ref.1 Inferred from direct assay. Source: dictyBase integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nuclear envelope Ref.5 Inferred from direct assay. Source: dictyBase
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1738	1738	Interaptin		PRO_0000327607
Regions
	Topological domain	1 – 1705	1705	Cytoplasmic Potential
	Transmembrane	1706 – 1726	21	Anchor for type IV membrane protein
	Domain	1 – 248	248	Actin-binding
	Domain	22 – 128	107	CH 1
	Domain	146 – 248	103	CH 2
	Coiled coil	373 – 1598	1226	Potential
	Compositional bias	256 – 260	5	Poly-Asn
	Compositional bias	262 – 271	10	Poly-Ser
	Compositional bias	292 – 300	9	Poly-Gln
	Compositional bias	434 – 439	6	Poly-Gln
	Compositional bias	1389 – 1392	4	Poly-Gln
	Compositional bias	1407 – 1413	7	Poly-Gln
	Compositional bias	1590 – 1598	9	Poly-Gln

Sequences

	Sequence		Length	Mass (Da)
	O76329-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 577A99D2EC79AF5C	FASTA	1,738	204,427
	10 20 30 40 50 60 MEHSTPLNEE IVHKKNDENW VIAQKKVFTN WCNIFLNQRS QKIEDLETDL YDGILLGSLL 70 80 90 100 110 120 EILSGKNVIL SKCKQLKTRL HYINNLNFSL KFIGDEGLRL VGVASEDITD GNLKLILGLV 130 140 150 160 170 180 WTLILRYQIQ SMQNSKSSQQ NLHSSTKPSE LMLNWVKSQI SDYGHHIKDL TTSFQNGLLF 190 200 210 220 230 240 CALVHKLVPE KLDYKSLSES DSLGNLTLAF EVANKELGIP SILDPHDIIT TPDELSILTY 250 260 270 280 290 300 ISLFPKVYQQ TLEPLNNNNN ISPSLSSSSS SLLNTPNKRN SIQLSKSTSF EQQNQQQQQQ 310 320 330 340 350 360 NLLSPNSYRN SISFSKSPSF EGSQSTGSSR SISPISSPIK NSTTGNSNLS KSTSFEKIEA 370 380 390 400 410 420 SNTTNNNTII IAEESRVIEK IVEKIIEVEK IVEVEKIVEV EKIVEVEKIV EVEKIVKVDD 430 440 450 460 470 480 IEKLTNLQDQ LTEQQQQYQE KSLKLVNLEL ELQEKSNQLV DKSNQLSTMQ ATNSELMEKI 490 500 510 520 530 540 GGLMNDLTDI PTQDIKEKDE IIANLKIESE KNLKCFQDDF NALQSRYSLT IEQTSQLQDR 550 560 570 580 590 600 IKQLINELQE RDDKFIEFTN SSNQSLADNQ RVIDQLTNEK QSITLQLQDQ QDIKEKEFQF 610 620 630 640 650 660 EKQQLLSQID SITTNIQEYQ DKFNNLQQEF NTQQTLNQQE THRLTQQLYQ INTDYNEKQT 670 680 690 700 710 720 QLQSEIKDNQ TINEQLNKQL SEKDKEIEKL SNQQEQQQDE KINNLLLEIK EKDCLIERIN 730 740 750 760 770 780 QQLLENIDLN SKYQQLLLEF ENFKLNSSKE KENQLNELQS KQDERFNQLN DEKLEKEKQL 790 800 810 820 830 840 QSIEDEFNQY KQQQLSSNSN IDQQLQSTII ELSELKEQKE LNDSKLIEKE KQLQQLQQEF 850 860 870 880 890 900 DQLNEKNQKD HQDQLELLEK QLKQLQQEYD QLNETNQSIE NQLNQQNLIN KENLNEKEQE 910 920 930 940 950 960 LLKLQNQLNQ QIEKIQFDQQ EFSKQNSINI ELVNEKNEKL IQLQQDYDQL KQQNRSNDEK 970 980 990 1000 1010 1020 DENDLIEKEN QLKSIQNELN QLIEKNESDH KEQQLKQQSI ENDLIEKENQ IQQLQSQLNE 1030 1040 1050 1060 1070 1080 QRQQQSNQLS EKDQQLNQLI EKNQFDQKEQ QLKQQSIEND LFEKENQIQQ LQSQLNEQRQ 1090 1100 1110 1120 1130 1140 QQSNQLSEKD QQLNQLIEKN ESDQKEQQLK QQSIENDLIE KENQIQQLQL QLNEQRQLQS 1150 1160 1170 1180 1190 1200 EVSIDNDKIL ELEKQLKQCQ SDLLKLNDEK QQQDKQLQDK QIEFDQLQLT FNQFKNDKDS 1210 1220 1230 1240 1250 1260 QFIQLQDDQK QQLQSIQQDL NQLKQENQEK EKQLSEKDEK LQSIQFENQE KEKQLSEKDE 1270 1280 1290 1300 1310 1320 KLQSIQQNLN QLNDENQEKV KQFSEKDEKL QSIQQDLNQL KQENQEKEKQ LSEKDEKLQS 1330 1340 1350 1360 1370 1380 IQQDLNQLND DQIKKNEKLK EKEEQLLKLQ QDFNDQQSQQ LKQLEEKLSE KENQLQQLKQ 1390 1400 1410 1420 1430 1440 ENEINQLNQQ QQSNEIIQQL KDQLLKQQQQ EQQENNNEKE IERLIQEIEQ LKQQQEIDQS 1450 1460 1470 1480 1490 1500 ELSNKEIKIQ TTQQEFDQLS HNRSKDQLHL QQLQQELDQL KQSFDDQDHQ FKKVIDERYN 1510 1520 1530 1540 1550 1560 LQLQLEQSTL SNNQLDQLLK EKLKPLELDS NEKQKTIDDL LSNISNLQIS LQNDKDLISE 1570 1580 1590 1600 1610 1620 RNNSIKTLES RITQQLSLLD EKDNLIKDLQ QQKQQQQQPP TASSSPSSSP SLLSSTPTPK 1630 1640 1650 1660 1670 1680 PQRPNQIEID RLVNEIVNRN QDLIRKNKTK FYKLENGDYI VNSIIYRLSL DDDNDSDLIA 1690 1700 1710 1720 1730 QEYENGNSTT FEKSLRIFPS KNTRPIFDWR ALFFIGAAVL AISTLFSSSR PIKYEKPT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Interaptin, an actin-binding protein of the alpha-actinin superfamily in Dictyostelium discoideum, is developmentally and cAMP-regulated and associates with intracellular membrane compartments." Rivero F., Kuspa A., Brokamp R., Matzner M., Noegel A.A. J. Cell Biol. 142:735-750(1998) [PubMed: 9700162] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, INDUCTION, SUBCELLULAR LOCATION.
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"Severe developmental defects in Dictyostelium null mutants for actin-binding proteins." Ponte E., Rivero F., Fechheimer M., Noegel A., Bozzaro S. Mech. Dev. 91:153-161(2000) [PubMed: 10704840] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[4]	"Identification of novel centrosomal proteins in Dictyostelium discoideum by comparative proteomic approaches." Reinders Y., Schulz I., Graef R., Sickmann A. J. Proteome Res. 5:589-598(2006) [PubMed: 16512674] [Abstract] Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]	"Dictyostelium Sun-1 connects the centrosome to chromatin and ensures genome stability." Xiong H., Rivero F., Euteneuer U., Mondal S., Mana-Capelli S., Larochelle D., Vogel A., Gassen B., Noegel A.A. Traffic 9:708-724(2008) [PubMed: 18266910] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF057019 Genomic DNA. Translation: AAC34582.1. AAFI02000100 Genomic DNA. Translation: EAL63713.1.
PIR	T14867.
RefSeq	XP_637275.1.
3D structure databases
HSSP	HSSP built from PDB template 1HF9 based on UniProtKB P01096.
ModBase	Search...
Genome annotation databases
GeneID	3388842.
GenomeReviews	Gene locus abpD in contig CM000154_GR.
KEGG	ddi:DDB_0191136.
Organism-specific databases
dictyBase	DDB_G0287291. abpD.
Phylogenomic databases
OMA	IEKNESD.
Family and domain databases
InterPro	IPR001589. Actinin_actin-bd_CS. IPR016146. Calponin-homology. IPR001715. Calponin_act_bd. [Graphical view]
Gene3D	G3DSA:1.10.418.10. Calponin-homology. 2 hits.
Pfam	PF00307. CH. 2 hits. [Graphical view]
SMART	SM00033. CH. 2 hits. [Graphical view]
PROSITE	PS00019. ACTININ_1. 1 hit. PS00020. ACTININ_2. 1 hit. PS50021. CH. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACTNB_DICDI

Accession

Primary (citable) accession number: O76329
Secondary accession number(s): Q54KE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	November 1, 1998
Last modified:	December 15, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)