ACTNB_DICDI
ID ACTNB_DICDI Reviewed; 1738 AA.
AC O76329; Q54KE8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Interaptin;
DE AltName: Full=Actin-binding protein D;
DE AltName: Full=Alpha-actinin B;
GN Name=abpD; Synonyms=actnB; ORFNames=DDB_G0287291;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, INDUCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9700162; DOI=10.1083/jcb.142.3.735;
RA Rivero F., Kuspa A., Brokamp R., Matzner M., Noegel A.A.;
RT "Interaptin, an actin-binding protein of the alpha-actinin superfamily in
RT Dictyostelium discoideum, is developmentally and cAMP-regulated and
RT associates with intracellular membrane compartments.";
RL J. Cell Biol. 142:735-750(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10704840; DOI=10.1016/s0925-4773(99)00292-0;
RA Ponte E., Rivero F., Fechheimer M., Noegel A., Bozzaro S.;
RT "Severe developmental defects in Dictyostelium null mutants for actin-
RT binding proteins.";
RL Mech. Dev. 91:153-161(2000).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16512674; DOI=10.1021/pr050350q;
RA Reinders Y., Schulz I., Graef R., Sickmann A.;
RT "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT by comparative proteomic approaches.";
RL J. Proteome Res. 5:589-598(2006).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=18266910; DOI=10.1111/j.1600-0854.2008.00721.x;
RA Xiong H., Rivero F., Euteneuer U., Mondal S., Mana-Capelli S.,
RA Larochelle D., Vogel A., Gassen B., Noegel A.A.;
RT "Dictyostelium Sun-1 connects the centrosome to chromatin and ensures
RT genome stability.";
RL Traffic 9:708-724(2008).
CC -!- FUNCTION: May function as linker between cellular membranes and the
CC actin cytoskeleton. Required for normal development of fruiting bodies.
CC {ECO:0000269|PubMed:10704840}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane; Single-pass type IV membrane
CC protein; Cytoplasmic side. Endoplasmic reticulum membrane. Golgi
CC apparatus, Golgi stack membrane. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Cytoplasm, cytoskeleton. Note=The
CC largest part of the protein is cytoplasmic, while its C-terminal part
CC is associated either with the nuclear envelope, the Golgi membrane or
CC the endoplasmic reticulum membrane.
CC -!- DEVELOPMENTAL STAGE: Present at very low levels during early stages of
CC development. Levels increase during late aggregation stage, reach a
CC maximum and remain high during culmination and maturation of the
CC fruiting body. Detected in upper and lower cup structures in late
CC culminants and mature fruiting bodies (at protein level). First
CC detected after 12 hours of development. Highly expressed at 12 to 16
CC hours of development. Levels return to basal levels during maturation
CC of the fruiting body. {ECO:0000269|PubMed:9700162}.
CC -!- INDUCTION: Up-regulated by cAMP. {ECO:0000269|PubMed:9700162}.
CC -!- DISRUPTION PHENOTYPE: Cells have reduced efficiency in fruiting body
CC formation and reduced spore viability. {ECO:0000269|PubMed:10704840}.
CC -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
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DR EMBL; AF057019; AAC34582.1; -; Genomic_DNA.
DR EMBL; AAFI02000100; EAL63713.1; -; Genomic_DNA.
DR PIR; T14867; T14867.
DR RefSeq; XP_637275.1; XM_632183.1.
DR AlphaFoldDB; O76329; -.
DR SMR; O76329; -.
DR IntAct; O76329; 65.
DR STRING; 44689.DDB0191136; -.
DR TCDB; 1.I.1.1.5; the nuclear pore complex (npc) family.
DR PaxDb; O76329; -.
DR EnsemblProtists; EAL63713; EAL63713; DDB_G0287291.
DR GeneID; 8626106; -.
DR KEGG; ddi:DDB_G0287291; -.
DR dictyBase; DDB_G0287291; abpD.
DR eggNOG; KOG0035; Eukaryota.
DR HOGENOM; CLU_239777_0_0_1; -.
DR InParanoid; O76329; -.
DR OMA; HANNSEM; -.
DR PRO; PR:O76329; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:dictyBase.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IDA:dictyBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:dictyBase.
DR GO; GO:0003779; F:actin binding; ISS:dictyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0009847; P:spore germination; IMP:dictyBase.
DR CDD; cd00014; CH; 2.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR Pfam; PF00307; CH; 2.
DR SMART; SM00033; CH; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Nucleus;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1738
FT /note="Interaptin"
FT /id="PRO_0000327607"
FT TOPO_DOM 1..1705
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1706..1726
FT /note="Helical; Anchor for type IV membrane protein"
FT DOMAIN 22..128
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 146..249
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..248
FT /note="Actin-binding"
FT REGION 285..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 373..1598
FT /evidence="ECO:0000255"
FT COMPBIAS 1589..1623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1738 AA; 204427 MW; 577A99D2EC79AF5C CRC64;
MEHSTPLNEE IVHKKNDENW VIAQKKVFTN WCNIFLNQRS QKIEDLETDL YDGILLGSLL
EILSGKNVIL SKCKQLKTRL HYINNLNFSL KFIGDEGLRL VGVASEDITD GNLKLILGLV
WTLILRYQIQ SMQNSKSSQQ NLHSSTKPSE LMLNWVKSQI SDYGHHIKDL TTSFQNGLLF
CALVHKLVPE KLDYKSLSES DSLGNLTLAF EVANKELGIP SILDPHDIIT TPDELSILTY
ISLFPKVYQQ TLEPLNNNNN ISPSLSSSSS SLLNTPNKRN SIQLSKSTSF EQQNQQQQQQ
NLLSPNSYRN SISFSKSPSF EGSQSTGSSR SISPISSPIK NSTTGNSNLS KSTSFEKIEA
SNTTNNNTII IAEESRVIEK IVEKIIEVEK IVEVEKIVEV EKIVEVEKIV EVEKIVKVDD
IEKLTNLQDQ LTEQQQQYQE KSLKLVNLEL ELQEKSNQLV DKSNQLSTMQ ATNSELMEKI
GGLMNDLTDI PTQDIKEKDE IIANLKIESE KNLKCFQDDF NALQSRYSLT IEQTSQLQDR
IKQLINELQE RDDKFIEFTN SSNQSLADNQ RVIDQLTNEK QSITLQLQDQ QDIKEKEFQF
EKQQLLSQID SITTNIQEYQ DKFNNLQQEF NTQQTLNQQE THRLTQQLYQ INTDYNEKQT
QLQSEIKDNQ TINEQLNKQL SEKDKEIEKL SNQQEQQQDE KINNLLLEIK EKDCLIERIN
QQLLENIDLN SKYQQLLLEF ENFKLNSSKE KENQLNELQS KQDERFNQLN DEKLEKEKQL
QSIEDEFNQY KQQQLSSNSN IDQQLQSTII ELSELKEQKE LNDSKLIEKE KQLQQLQQEF
DQLNEKNQKD HQDQLELLEK QLKQLQQEYD QLNETNQSIE NQLNQQNLIN KENLNEKEQE
LLKLQNQLNQ QIEKIQFDQQ EFSKQNSINI ELVNEKNEKL IQLQQDYDQL KQQNRSNDEK
DENDLIEKEN QLKSIQNELN QLIEKNESDH KEQQLKQQSI ENDLIEKENQ IQQLQSQLNE
QRQQQSNQLS EKDQQLNQLI EKNQFDQKEQ QLKQQSIEND LFEKENQIQQ LQSQLNEQRQ
QQSNQLSEKD QQLNQLIEKN ESDQKEQQLK QQSIENDLIE KENQIQQLQL QLNEQRQLQS
EVSIDNDKIL ELEKQLKQCQ SDLLKLNDEK QQQDKQLQDK QIEFDQLQLT FNQFKNDKDS
QFIQLQDDQK QQLQSIQQDL NQLKQENQEK EKQLSEKDEK LQSIQFENQE KEKQLSEKDE
KLQSIQQNLN QLNDENQEKV KQFSEKDEKL QSIQQDLNQL KQENQEKEKQ LSEKDEKLQS
IQQDLNQLND DQIKKNEKLK EKEEQLLKLQ QDFNDQQSQQ LKQLEEKLSE KENQLQQLKQ
ENEINQLNQQ QQSNEIIQQL KDQLLKQQQQ EQQENNNEKE IERLIQEIEQ LKQQQEIDQS
ELSNKEIKIQ TTQQEFDQLS HNRSKDQLHL QQLQQELDQL KQSFDDQDHQ FKKVIDERYN
LQLQLEQSTL SNNQLDQLLK EKLKPLELDS NEKQKTIDDL LSNISNLQIS LQNDKDLISE
RNNSIKTLES RITQQLSLLD EKDNLIKDLQ QQKQQQQQPP TASSSPSSSP SLLSSTPTPK
PQRPNQIEID RLVNEIVNRN QDLIRKNKTK FYKLENGDYI VNSIIYRLSL DDDNDSDLIA
QEYENGNSTT FEKSLRIFPS KNTRPIFDWR ALFFIGAAVL AISTLFSSSR PIKYEKPT
