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TOIP1_BOVIN
ID   TOIP1_BOVIN             Reviewed;         600 AA.
AC   F1N4E5;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Torsin-1A-interacting protein 1;
DE   AltName: Full=Lamin-associated protein 1B;
DE            Short=LAP1B;
GN   Name=TOR1AIP1;
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 GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
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. Interacts with VIM (By
CC       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; DAAA02043477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F1N4E5; -.
DR   SMR; F1N4E5; -.
DR   STRING; 9913.ENSBTAP00000033870; -.
DR   PaxDb; F1N4E5; -.
DR   PRIDE; F1N4E5; -.
DR   Ensembl; ENSBTAT00000033967; ENSBTAP00000033870; ENSBTAG00000035226.
DR   VEuPathDB; HostDB:ENSBTAG00000035226; -.
DR   VGNC; VGNC:36224; TOR1AIP1.
DR   eggNOG; ENOG502QUV7; Eukaryota.
DR   GeneTree; ENSGT00390000012166; -.
DR   HOGENOM; CLU_034263_0_1_1; -.
DR   InParanoid; F1N4E5; -.
DR   TreeFam; TF329438; -.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000035226; Expressed in spermatid and 104 other tissues.
DR   ExpressionAtlas; F1N4E5; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR   GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR   GO; GO:0071763; P:nuclear membrane organization; IBA:GO_Central.
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   3: Inferred from homology;
KW   Coiled coil; Glycoprotein; Isopeptide bond; Membrane; Nucleus;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
FT   CHAIN           1..600
FT                   /note="Torsin-1A-interacting protein 1"
FT                   /id="PRO_0000417025"
FT   TOPO_DOM        1..354
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        372..600
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255"
FT   REGION          1..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..600
FT                   /note="Interaction with TOR1A"
FT                   /evidence="ECO:0000250"
FT   COILED          376..452
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        52..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         61
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921T2"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT   MOD_RES         145
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         158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT   MOD_RES         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT   MOD_RES         223
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT   MOD_RES         230
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PQX1"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PQX1"
FT   MOD_RES         322
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT   MOD_RES         332
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        325
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JTV8"
SQ   SEQUENCE   600 AA;  67468 MW;  0BDC048C3B12CD28 CRC64;
     MAGEGQRAEP EREGWALYVT PRAPLREGRP RLAPQNGGSG DVPAYGTPTP SRHGRREVRF
     SEEPPEVYGD FEPRAAKEKA RVGRQIPLEG FRPDSAKEEV RESAYYLRSR QRRQPRLHEA
     EEMQTRRAAL LQQQPHSPPP PLRPSPVTTR RGLRDSHSSE EDEPPSQTVL SQTVTKKAIR
     RTQETPVMSE DPLISLRRPP LRSSRSEAAS VQQKVNFLEE GETEENDQDS FDSDVTVKVR
     SGDSVESGDQ TTRSSSQYKE SFWQSSQSGD FTAFDEQPLK LSSGYQKTPQ EWAEKTVRIR
     TRMLTSSPGM RSIYGSFSDD DSVQKSELGN QSPSTSNQQM TGQPKSVSSV KTKRYWPFAV
     IAALLIGGFL YTRPPEAETT AVQEFQNQMK QLMNKYQGQD EKLWKRSQTF LEKHLNGSQS
     RPQPAILLLT AARDAEEALR CLSEQIADAY SSFRSVPAIR IDGASKATRD SDTVKEEVDQ
     ELSNGFRNGQ NAAVVHRFES LPAGSTLIFY KYCDHESAAF KDVALVLTVL LEEETLGTSL
     GLKEIEEKVR DFLQVKFTNS DTPNSYKHMD PDKLSGLWSR ISHLVLPVQP ENDLKKGICL
 
 
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