LAP2_RAT
ID LAP2_RAT Reviewed; 452 AA.
AC Q62733;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Lamina-associated polypeptide 2, isoform beta;
DE AltName: Full=Thymopoietin isoform beta;
DE Short=TP beta;
GN Name=Tmpo; Synonyms=Lap2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 158-172; 270-284 AND
RP 347-361.
RC TISSUE=Liver;
RX PubMed=7737115; DOI=10.1002/j.1460-2075.1995.tb07151.x;
RA Furukawa K., Pante N., Aebi U., Gerace L.;
RT "Cloning of a cDNA for lamina-associated polypeptide 2 (LAP2) and
RT identification of regions that specify targeting to the nuclear envelope.";
RL EMBO J. 14:1626-1636(1995).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74; SER-155;
RP THR-159; SER-167 AND SER-183, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Binds directly to lamin B1 and chromosomes in a mitotic
CC phosphorylation-regulated manner. May play an important role in nuclear
CC envelope reassembly at the end of mitosis and/or anchoring of the
CC nuclear lamina and interphase chromosomes to the nuclear envelope.
CC -!- SUBUNIT: Interacts with LMNB1, LMNB2, BANF1, AKAP8L, GMCL and
CC chromosomes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass type II
CC membrane protein. Chromosome {ECO:0000250}. Note=Tightly associated
CC with the nuclear lamina.
CC -!- DOMAIN: Has two structurally independent, non-interacting domains: LEM-
CC like (also called LAP2-N or LEM-D) and LEM (also called LAP2-C or LEM-
CC B). LEM-like binds DNA while LEM interacts with BANF1 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Mitosis-specific phosphorylation specifically abolishes its
CC binding to lamin B and chromosomes.
CC -!- SIMILARITY: Belongs to the LEM family. {ECO:0000305}.
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DR EMBL; U18314; AAC52209.1; -; mRNA.
DR PIR; S55255; S55255.
DR RefSeq; NP_037019.1; NM_012887.1.
DR AlphaFoldDB; Q62733; -.
DR BioGRID; 247398; 1.
DR STRING; 10116.ENSRNOP00000012715; -.
DR iPTMnet; Q62733; -.
DR PhosphoSitePlus; Q62733; -.
DR jPOST; Q62733; -.
DR PaxDb; Q62733; -.
DR PRIDE; Q62733; -.
DR Ensembl; ENSRNOT00000012715; ENSRNOP00000012715; ENSRNOG00000008797.
DR GeneID; 25359; -.
DR KEGG; rno:25359; -.
DR UCSC; RGD:3875; rat.
DR CTD; 7112; -.
DR RGD; 3875; Tmpo.
DR eggNOG; ENOG502QWCI; Eukaryota.
DR GeneTree; ENSGT00390000008708; -.
DR HOGENOM; CLU_032534_1_0_1; -.
DR InParanoid; Q62733; -.
DR OMA; METTSIN; -.
DR OrthoDB; 323585at2759; -.
DR PhylomeDB; Q62733; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000008797; Expressed in thymus and 20 other tissues.
DR Genevisible; Q62733; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005521; F:lamin binding; TAS:RGD.
DR GO; GO:0031468; P:nuclear membrane reassembly; NAS:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR Gene3D; 1.10.720.40; -; 2.
DR InterPro; IPR013146; LEM-like_dom.
DR InterPro; IPR011015; LEM/LEM-like_dom_sf.
DR InterPro; IPR003887; LEM_dom.
DR Pfam; PF03020; LEM; 1.
DR Pfam; PF08198; Thymopoietin; 1.
DR SMART; SM00540; LEM; 1.
DR SMART; SM01261; Thymopoietin; 1.
DR SUPFAM; SSF63451; SSF63451; 2.
DR PROSITE; PS50954; LEM; 1.
DR PROSITE; PS50955; LEM_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Direct protein sequencing; DNA-binding; Membrane;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..452
FT /note="Lamina-associated polypeptide 2, isoform beta"
FT /id="PRO_0000206147"
FT TRANSMEM 410..430
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..452
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 5..48
FT /note="LEM-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313,
FT ECO:0000255|PROSITE-ProRule:PRU00314"
FT DOMAIN 108..152
FT /note="LEM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT REGION 1..409
FT /note="Nucleoplasmic"
FT /evidence="ECO:0000255"
FT REGION 48..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..107
FT /note="Linker"
FT REGION 137..242
FT /note="NAKAP95-binding N"
FT REGION 149..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..370
FT /note="Binds lamins B"
FT REGION 299..373
FT /note="NAKAP95-binding C"
FT COMPBIAS 92..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61029"
FT MOD_RES 85
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61029"
FT MOD_RES 87
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61029"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61029"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61029"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61029"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61029"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 206
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61029"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61029"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61029"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61029"
FT MOD_RES 388
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61029"
SQ SEQUENCE 452 AA; 50278 MW; D56C9B51DB9D3DA4 CRC64;
MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLAAGANSK
GPPDFSSDEE REPTPVLGSG ASVGRGRGAV GRKATKKTDK PRPEDKDDLD VTELSNEELL
EQLVRYGVNP GPIVGTTRKL YEKKLLKLRE QGAESRSSTP LPTVSSSAEN TRQNGSNDSD
RYSDNDEDSK IELKLEKREP LKGRAKTPVT LKQRRIEHNQ SYSEAGVTET EWTSGSSKGG
PLQALTREST RGSRRTPRRR VEPSQHFRVD GAVISESTPI AETIKASSND SLVANRLTGN
FKHASSILPI TEFSDITRRT PKKPLTRAEV GEKTEERRVE RDILKEMFPY EASTPTGISA
SCRRPIKGAA GRPLELSDFR MEESFSSKYV PKYVPLADVK SEKTKKGRSV PMWIKMLLFA
LVAGFLFLVY QAMETNQGNP FTNFLQDTKI SN
