TOIP1_PONAB
ID TOIP1_PONAB Reviewed; 598 AA.
AC Q5R7A3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Torsin-1A-interacting protein 1;
DE AltName: Full=Lamina-associated polypeptide 1B;
DE Short=LAP1B;
GN Name=TOR1AIP1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for nuclear membrane integrity. Induces TOR1A and
CC TOR1B ATPase activity and is required for their location on the nuclear
CC membrane. Binds to A- and B-type lamins. Possible role in membrane
CC attachment and assembly of the nuclear lamina (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ATP1B4. Interacts with TOR1A (ATP-bound).
CC Interacts with TOR1B, TOR2A and TOR3A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TOR1AIP family. {ECO:0000305}.
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DR EMBL; CR860215; CAH92357.1; -; mRNA.
DR RefSeq; NP_001126388.1; NM_001132916.2.
DR AlphaFoldDB; Q5R7A3; -.
DR SMR; Q5R7A3; -.
DR STRING; 9601.ENSPPYP00000000522; -.
DR GeneID; 100173369; -.
DR KEGG; pon:100173369; -.
DR CTD; 26092; -.
DR eggNOG; ENOG502QUV7; Eukaryota.
DR InParanoid; Q5R7A3; -.
DR OrthoDB; 575658at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR Gene3D; 3.40.50.12190; -; 1.
DR InterPro; IPR038599; LAP1C-like_C_sf.
DR InterPro; IPR008662; TOIP1/2.
DR PANTHER; PTHR18843; PTHR18843; 1.
DR Pfam; PF05609; LAP1C; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Glycoprotein; Isopeptide bond; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..598
FT /note="Torsin-1A-interacting protein 1"
FT /id="PRO_0000228837"
FT TOPO_DOM 1..351
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..598
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT REGION 19..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..598
FT /note="Interaction with TOR1A"
FT /evidence="ECO:0000250"
FT COILED 374..450
FT /evidence="ECO:0000255"
FT COMPBIAS 51..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q921T2"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQX1"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQX1"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
SQ SEQUENCE 598 AA; 67589 MW; C68E812B8EC2FBC7 CRC64;
MAGEGRRAEA VREGWGVYVT PRAPIREGRG RLAPQNGGSS DAPAYRTSLS RQGRREVRFS
DEPPEVYGDF EPLVDKERSP VGKRTRLEEF RSDSAKEEVR ESAYYLRSRQ RRQPRPQEAE
EMKTRRTTRL QQQHSQQPPL QPSPVMTRRG LRDSHSSEED EPSSPTDLSQ TISKKTVRSI
QEAPAESEDL VISLRRPPLR YPRSEATSVQ QKVNFSEEGE TEDDQDSSHS SVTTVKSRSR
DSDESGDKTT RSSSQYIESF WQSSQSQNFT AHDKQPSVLS SGYQKTPQEW APQTARMRTR
MQTSSPGKSS IYGSFSDDDS ILKSELGNQS PSTSSQQVTG QPQNASFVKR NWWWLLPLIA
ALASGSFWFF STPEVETTAV QEFQNQMNQL KNKYQGQDEK LWKRSQTFLE KHLNSSHPRS
QPAILLLTAA RDAEEALRCL SEQIADAYSS FHSVRAIRID GTDKATQDSD TVKLEVDQEL
SNGLKNGQNA AVVHRFESFP AGSTLIFYKY CDHENAAFKD VALVLTVLLE EETLGTSLGL
KEVEEKVRDF LKVKFTNSNT PNSYNHMDPD KLNGLWSRIS HLVLPVQPEN ALKRGICL
