IP13A_DICDI
ID IP13A_DICDI Reviewed; 1064 AA.
AC Q54C85;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Importin-13 homolog A;
GN Name=ipo13A; ORFNames=DDB_G0293110;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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).
CC -!- FUNCTION: Required for nuclear protein import and mediates docking of
CC import substrate to distinct nucleoporins. {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with an importin alpha subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus envelope
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}.
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DR EMBL; AAFI02000199; EAL60907.1; -; Genomic_DNA.
DR RefSeq; XP_629334.1; XM_629332.1.
DR AlphaFoldDB; Q54C85; -.
DR SMR; Q54C85; -.
DR STRING; 44689.DDB0304413; -.
DR PaxDb; Q54C85; -.
DR EnsemblProtists; EAL60907; EAL60907; DDB_G0293110.
DR GeneID; 8629058; -.
DR KEGG; ddi:DDB_G0293110; -.
DR dictyBase; DDB_G0293110; ipo13A.
DR eggNOG; KOG2022; Eukaryota.
DR HOGENOM; CLU_288767_0_0_1; -.
DR InParanoid; Q54C85; -.
DR OMA; DTFMYCY; -.
DR PhylomeDB; Q54C85; -.
DR PRO; PR:Q54C85; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013598; Exportin-1/Importin-b-like.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040520; Importin_rep_3.
DR Pfam; PF18806; Importin_rep_3; 1.
DR Pfam; PF08389; Xpo1; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..1064
FT /note="Importin-13 homolog A"
FT /id="PRO_0000328011"
FT DOMAIN 40..109
FT /note="Importin N-terminal"
FT REGION 695..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1064 AA; 121574 MW; D8FC88DCBD673470 CRC64;
MYNNNGFHEE TNIDESQFTV EKVETVLKSL YFPQNNDYSA LPQIQQWLIQ FQKSFSSWSI
APLLLMSNIK EIQYFGASTI ENKIKNNWLS LSQDMKKEFL DNLLLFLKTQ ITKCSTVVIT
RLCLAVSVIA CHSTTDLWAN PILDVLQLSF QDINNLDCFN PNLVNLTLEL LTIFPEELTN
ADYITQEKRN KVGLQFNKHN SKVFEILCKI MSLPQNQQTL IFMKSSLKCF KSWILFDCSP
REYLIDSDLI LKCFEAVSNN PKLVEDFLMV LDEMFTFMGG KIFRSYTSAF SLVLSRILMI
FPSFYILALQ EENQIFNQIF LLFSHIAENH IKTLLKNPEL SNNFFKALIQ MALKGDFETC
ELLSPVITEI AALHELHSTS STTEATTTTI ATTTTPTTTS DCDISGWYQY LGEMVEVFRL
KSMYPLDKDI SDLYEEDAEK FFAFRVIAGD SVLEVYNILE GKILQQLLNS LWSDIQSFPT
TKCWQSIEAT IYLLSCLSES ITEDTEFVPQ LFSILGQLPI QSTPLIKSTM TLAGNYSNLI
DKSTIFLEKI VKDFFPAFEN PDLKSVASQS FLSISKNSKC ASILSNSITQ LISLCAPILS
NNNKILDDPS NFNILEALLY IISTLPSDSQ VLNYSTQLLY PFILFIKNYY TNQLQQQQQQ
QQQQQTELRL LLSSINLLTK FCKIYDDEQV NEYGTTQQEN NNNNNNNNNN NNNNNNNNNN
NNNNNIKPVF EIINNIIPIY GELLSLNTLE SSIIEAISIF YKKAIMINNN HQNITNIPEI
NRQLTLAFLK HKPLSLVLST LSISIVNLPK EQHLDFLADS LSSISSKMIQ IWSEKSNQNN
KKNNKKINNN IDIDNDNENN NNNNQIQFEN NELNEFKNLK ISIYPDITKE YFTMITQYIR
YNAVSIPQGV ISHLFSIILV NITKIHDKVT ARACFSFMAL IITKSKEMKS QIKWEPLLNE
INGWLSIHGE LFIKQILYSA GGGIPRSVVQ FISEVIASLV SSYPDVFRIS ALKCLSVDGF
PSSNITKEQK EKFLNSLMLY RSKKLPLKIV TDFSLVSLGI ATNQ