ANKL2_MOUSE
ID ANKL2_MOUSE Reviewed; 964 AA.
AC Q6P1H6; Q3UQF6; Q3UY52; Q3V1X7; Q6ZQ67; Q8BRM7; Q9CTK6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ankyrin repeat and LEM domain-containing protein 2;
DE AltName: Full=LEM domain-containing protein 4;
GN Name=Ankle2; Synonyms=D5Ertd585e, Kiaa0692, Lem4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Head, Olfactory bulb, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-964 (ISOFORM 3).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266 AND SER-275, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in mitotic nuclear envelope reassembly by promoting
CC dephosphorylation of BAF/BANF1 during mitotic exit. Coordinates the
CC control of BAF/BANF1 dephosphorylation by inhibiting VRK1 kinase and
CC promoting dephosphorylation of BAF/BANF1 by protein phosphatase 2A
CC (PP2A), thereby facilitating nuclear envelope assembly. May regulate
CC nuclear localization of VRK1 in non-dividing cells. It is unclear
CC whether it acts as a real PP2A regulatory subunit or whether it is
CC involved in recruitment of the PP2A complex. Involved in brain
CC development. {ECO:0000250|UniProtKB:Q86XL3}.
CC -!- SUBUNIT: Interacts with BAF/BANF1. Interacts with protein phosphatase
CC 2A (PP2A) components PPP2C (PPP2CA or PPP2CB) and PPP2R1A (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type III membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6P1H6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1H6-2; Sequence=VSP_023576;
CC Name=3;
CC IsoId=Q6P1H6-3; Sequence=VSP_023579;
CC Name=4;
CC IsoId=Q6P1H6-4; Sequence=VSP_023577, VSP_023578;
CC -!- SIMILARITY: Belongs to the ANKLE2 family. {ECO:0000305}.
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DR EMBL; AK003234; BAB22659.1; -; mRNA.
DR EMBL; AK132187; BAE21022.1; -; mRNA.
DR EMBL; AK043925; BAC31703.1; -; mRNA.
DR EMBL; AK134966; BAE22361.1; -; mRNA.
DR EMBL; AK142497; BAE25086.1; -; mRNA.
DR EMBL; BC065071; AAH65071.1; -; mRNA.
DR EMBL; AK129192; BAC98002.1; -; Transcribed_RNA.
DR CCDS; CCDS57372.1; -. [Q6P1H6-1]
DR CCDS; CCDS80360.1; -. [Q6P1H6-2]
DR RefSeq; NP_001240743.1; NM_001253814.1. [Q6P1H6-1]
DR RefSeq; NP_082198.1; NM_027922.2. [Q6P1H6-2]
DR AlphaFoldDB; Q6P1H6; -.
DR SMR; Q6P1H6; -.
DR BioGRID; 214925; 2.
DR STRING; 10090.ENSMUSP00000031474; -.
DR iPTMnet; Q6P1H6; -.
DR PhosphoSitePlus; Q6P1H6; -.
DR EPD; Q6P1H6; -.
DR MaxQB; Q6P1H6; -.
DR PaxDb; Q6P1H6; -.
DR PeptideAtlas; Q6P1H6; -.
DR PRIDE; Q6P1H6; -.
DR ProteomicsDB; 296039; -. [Q6P1H6-1]
DR ProteomicsDB; 296040; -. [Q6P1H6-2]
DR ProteomicsDB; 296041; -. [Q6P1H6-3]
DR ProteomicsDB; 296042; -. [Q6P1H6-4]
DR Antibodypedia; 1225; 106 antibodies from 23 providers.
DR DNASU; 71782; -.
DR Ensembl; ENSMUST00000031474; ENSMUSP00000031474; ENSMUSG00000029501. [Q6P1H6-2]
DR Ensembl; ENSMUST00000086674; ENSMUSP00000083878; ENSMUSG00000029501. [Q6P1H6-3]
DR Ensembl; ENSMUST00000197188; ENSMUSP00000143044; ENSMUSG00000029501. [Q6P1H6-1]
DR GeneID; 71782; -.
DR KEGG; mmu:71782; -.
DR UCSC; uc008yqe.2; mouse. [Q6P1H6-4]
DR UCSC; uc008yqf.2; mouse. [Q6P1H6-2]
DR UCSC; uc008yqg.2; mouse. [Q6P1H6-1]
DR CTD; 23141; -.
DR MGI; MGI:1261856; Ankle2.
DR VEuPathDB; HostDB:ENSMUSG00000029501; -.
DR eggNOG; ENOG502QQ4Z; Eukaryota.
DR GeneTree; ENSGT00390000016767; -.
DR HOGENOM; CLU_017564_0_0_1; -.
DR InParanoid; Q6P1H6; -.
DR OMA; EYLEDRC; -.
DR OrthoDB; 567264at2759; -.
DR PhylomeDB; Q6P1H6; -.
DR TreeFam; TF317729; -.
DR Reactome; R-MMU-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR BioGRID-ORCS; 71782; 21 hits in 78 CRISPR screens.
DR ChiTaRS; Ankle2; mouse.
DR PRO; PR:Q6P1H6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6P1H6; protein.
DR Bgee; ENSMUSG00000029501; Expressed in spermatocyte and 224 other tissues.
DR Genevisible; Q6P1H6; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0042326; P:negative regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:UniProtKB.
DR CDD; cd12944; LEM_ANKL2; 1.
DR Gene3D; 1.10.720.40; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR035007; ANKLE2.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011015; LEM/LEM-like_dom_sf.
DR InterPro; IPR035006; LEM_ANKL2.
DR InterPro; IPR003887; LEM_dom.
DR PANTHER; PTHR12349:SF4; PTHR12349:SF4; 1.
DR Pfam; PF03020; LEM; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF63451; SSF63451; 1.
DR PROSITE; PS50954; LEM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell cycle; Cell division;
KW Endoplasmic reticulum; Membrane; Mitosis; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..964
FT /note="Ankyrin repeat and LEM domain-containing protein 2"
FT /id="PRO_0000280243"
FT TOPO_DOM 1..7
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..964
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 71..115
FT /note="LEM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT REPEAT 419..448
FT /note="ANK"
FT REGION 666..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XL3"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XL3"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XL3"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XL3"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XL3"
FT MOD_RES 940
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XL3"
FT VAR_SEQ 290
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023576"
FT VAR_SEQ 419..423
FT /note="GFDTP -> VSTPH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023577"
FT VAR_SEQ 424..964
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023578"
FT VAR_SEQ 667..744
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_023579"
FT CONFLICT 82
FT /note="L -> H (in Ref. 1; BAE21022)"
FT /evidence="ECO:0000305"
FT CONFLICT 871
FT /note="L -> R (in Ref. 1; BAE22361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 964 AA; 106198 MW; 2A2A4E480B24D4E0 CRC64;
MLWQRLAVVE WAALAWELLG ASVLFIAVRW LVRRLEKRPR DLNRCGTLSS PPSASEAVAA
QPGEVTMDAM MARLKLLNPD DLRKEVMKAG LKCGPITSTT RFIFEKKLAQ ALLEQGGLLT
SSLPKPSAVT AMAFIQGTSR TPPSVDGKQT QQACFSEDRD FGYSVGLNPP EEEAVASSVH
PVPFSASTRN DNHKAGVTAP KEPLVYYGVC PVYEDGPVRH ERIHVYEDKK EALQAAKLIK
GSRFKAFRTR EDAEKFARGI CDYLPSPNKT TPLLSPVKAV PLGGSDGLKA DGLCLAESET
VNKERANSYK NPRTQDLTAK LRKAVENGEE HTFSDLIWSN PRYLIGSGDN PTIVQEGCRY
NVMHVAAKEN QASMCQLTLE TLENPEFMRL MYPDDNMDML QKRILYVVDL YLNTPDKVGF
DTPLHFACKF GNVDVVNVLS SHPLIVKNRK NKYGKTPEEV ICERSQNKSP ALKERIREYL
MGHYYVPLLR AEDTSPVIGE LWSSDQKAEA SNTAHCRSSP RDPVMTLRAF VGPLSPSKAE
DFRKLWKTPP RKKAGFFHSI RKSDPERGIE RVGRELAHEL GYPWVEYWEF LGCFVDLSSQ
EGLQRLEEYL IQKELSKKAQ QEIRENEGCL QDRTSDFGSG KKYSNSISVG AFLDGDDDSS
LEEIKNQQNT VPSQSQPTTD KFQTSKSGSL PLGQKVDPGE TSVGTYPDKG RNGFCHPLNH
RTADGRGLEA TNGEEALPPP VSVLTQELNK LNLQSLGDSL HETPDKNGKL EDEVLPSRKG
AADSDLLASP PAIASLGKKQ VRTNTEVSEA MAEMSLGPKS PQLGVQAGLE PILSSATVDS
TKRLFLSGEE PSKLDRDVLA ALECANIDPG LYPAIHRWKS TVMCYSPSDR QSWPSPALKG
KFTTELVDLD CSHSCSGRCS PAGSSPSKPG HTSSSSGLHS PGRYSPAHGR HFQRVAHVAR
LAAL
