TNPO1_BOVIN
ID TNPO1_BOVIN Reviewed; 898 AA.
AC Q3SYU7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Transportin-1;
DE AltName: Full=Importin beta-2;
DE AltName: Full=Karyopherin beta-2;
GN Name=TNPO1; Synonyms=KPNB2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for nuclear localization signals (NLS) in
CC cargo substrates. May mediate docking of the importin/substrate complex
CC to the nuclear pore complex (NPC) through binding to nucleoporin and
CC the complex is subsequently translocated through the pore by an energy
CC requiring, Ran-dependent mechanism. At the nucleoplasmic side of the
CC NPC, Ran binds to the importin, the importin/substrate complex
CC dissociates and importin is re-exported from the nucleus to the
CC cytoplasm where GTP hydrolysis releases Ran. The directionality of
CC nuclear import is thought to be conferred by an asymmetric distribution
CC of the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC nucleus. Involved in nuclear import of M9-containing proteins. In
CC vitro, binds directly to the M9 region of the heterogeneous nuclear
CC ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear
CC import. Involved in hnRNP A1/A2 nuclear export. Mediates the nuclear
CC import of ribosomal proteins RPL23A, RPS7 and RPL5. In vitro, mediates
CC nuclear import of H2A, H2B, H3 and H4 histones, and SRP19. Mediates
CC nuclear import of ADAR/ADAR1 in a RanGTP-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q8BFY9,
CC ECO:0000250|UniProtKB:Q92973}.
CC -!- SUBUNIT: Identified in a complex that contains TNPO1, RAN and RANBP1
CC (By similarity). Binds HNRPA1, HNRPA2, HNRNPDL, RPS7, RPL5 and RAN.
CC Interacts with H2A, H2B, H3 and H4 histones (By similarity). Interacts
CC with ADAR/ADAR1 (via DRBM 3 domain). Interacts with SNAI1 (via zinc
CC fingers); the interaction mediates SNAI1 nuclear import. Interacts with
CC SNAI2 (via zinc fingers) (By similarity). Interacts with RPL23A (via
CC BIB domain) AND SRP19; this interaction is involved in RPL23A and SRP19
CC import into the nucleus (By similarity). {ECO:0000250|UniProtKB:Q8BFY9,
CC ECO:0000250|UniProtKB:Q92973}.
CC -!- INTERACTION:
CC Q3SYU7; P52293: Kpna2; Xeno; NbExp=3; IntAct=EBI-8469003, EBI-3043908;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI03375.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC103374; AAI03375.1; ALT_INIT; mRNA.
DR RefSeq; NP_001070008.1; NM_001076540.1.
DR AlphaFoldDB; Q3SYU7; -.
DR SMR; Q3SYU7; -.
DR IntAct; Q3SYU7; 3.
DR MINT; Q3SYU7; -.
DR STRING; 9913.ENSBTAP00000010491; -.
DR PaxDb; Q3SYU7; -.
DR PeptideAtlas; Q3SYU7; -.
DR PRIDE; Q3SYU7; -.
DR Ensembl; ENSBTAT00000010491; ENSBTAP00000010491; ENSBTAG00000007979.
DR GeneID; 767620; -.
DR KEGG; bta:767620; -.
DR CTD; 3842; -.
DR VEuPathDB; HostDB:ENSBTAG00000007979; -.
DR VGNC; VGNC:36199; TNPO1.
DR eggNOG; KOG2023; Eukaryota.
DR GeneTree; ENSGT00940000155389; -.
DR InParanoid; Q3SYU7; -.
DR OMA; MFPLLEC; -.
DR OrthoDB; 525700at2759; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000007979; Expressed in granulosa cell and 112 other tissues.
DR ExpressionAtlas; Q3SYU7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IBA:GO_Central.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
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; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040122; Importin_beta.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..898
FT /note="Transportin-1"
FT /id="PRO_0000383650"
FT REPEAT 19..46
FT /note="HEAT 1"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT DOMAIN 41..109
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 51..89
FT /note="HEAT 2"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 98..131
FT /note="HEAT 3"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 137..174
FT /note="HEAT 4"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 181..211
FT /note="HEAT 5"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 224..251
FT /note="HEAT 6"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 263..290
FT /note="HEAT 7"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 306..397
FT /note="HEAT 8"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 405..433
FT /note="HEAT 9"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 445..472
FT /note="HEAT 10"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 486..519
FT /note="HEAT 11"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 527..560
FT /note="HEAT 12"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 568..606
FT /note="HEAT 13"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 614..665
FT /note="HEAT 14"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 676..707
FT /note="HEAT 15"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 715..748
FT /note="HEAT 16"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 756..791
FT /note="HEAT 17"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 799..832
FT /note="HEAT 18"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 841..872
FT /note="HEAT 19"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 875..895
FT /note="HEAT 20"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REGION 347..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..374
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 468
FT /note="Important for interaction with cargo nuclear
FT localization signals"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT SITE 738
FT /note="Important for interaction with cargo nuclear
FT localization signals"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
SQ SEQUENCE 898 AA; 102383 MW; 43A39A7FB542C832 CRC64;
MVWDRQTKME YEWKPDEQGL QQILQLLKES QSPDTTIQRT VQQKLEQLNQ YPDFNNYLIF
VLTKLKSEDE PTRSLSGLIL KNNVKAHFQN FPNGVTDFIK SECLNNIGDS SPLIRATVGI
LITTIASKGE LQNWPDLLPK LCSLLDSEDY NTCEGAFGAL QKICEDSAEI LDSDVLDRPL
NIMIPKFLQF FKHSSPKIRS HAVACVNQFI ISRTQALMLH IDSFIENLFA LAGDEEPEVR
KNVCRALVML LEVRMDRLLP HMHNIVEYML QRTQDQDENV ALEACEFWLT LAEQPICKDV
LIRHLPKLIP VLVNGMKYSD IDIILLKGDV EEDETIPDSE QDIRPRFHRS RTVAQQHDED
GIEEEEDDDD EIDDDDTISD WNLRKCSAAA LDVLANVYRD ELLPHILPLL KELLFHHEWV
VKESGILVLG AIAEGCMQGM IPYLPELIPH LIQCLSDKKA LVRSITCWTL SRYAHWVVSQ
PPDTYLKPLM TELLKRILDS NKRVQEAACS AFATLEEEAC TELVPYLAYI LDTLVFAFSK
YQHKNLLILY DAIGTLADSV GHHLNKPEYI QMLMPPLIQK WNMLKDEDKD LFPLLECLSS
VATALQSGFL PYCEPVYQRC VNLVQKTLAQ AMLNNAQPDQ YEAPDKDFMI VALDLLSGLA
EGLGGNIEQL VARSNILTLM YQCMQDKMPE VRQSSFALLG DLTKACFQHV KPCIADFMPI
LGTNLNPEFI SVCNNATWAI GEISIQMGIE MQPYIPMVLH QLVEIINRPN TPKTLLENTA
ITIGRLGYVC PQEVAPMLQQ FIRPWCTSLR NIRDNEEKDS AFRGICTMIS VNPSGVIQDF
IFFCDAVASW INPKDDLRDM FCKILHGFKN QVGDENWRRF SDQFPLPLKE RLAAFYGV
