ANKL2_RAT
ID ANKL2_RAT Reviewed; 964 AA.
AC Q7TP65; F1LMJ0; F1M1M8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Ankyrin repeat and LEM domain-containing protein 2;
DE AltName: Full=LEM domain-containing protein 4;
DE AltName: Full=Liver regeneration-related protein LRRG057;
GN Name=Ankle2; Synonyms=Lem4; ORFNames=Ab2-034;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Xu C.S., Li W.Q., Li Y.C., Chai L.Q., Yuan J.Y., Yang K.J., Yan H.M.,
RA Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F., Han H.P., Wang G.P.,
RA Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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=2;
CC Name=1;
CC IsoId=Q7TP65-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TP65-2; Sequence=VSP_044174;
CC -!- SIMILARITY: Belongs to the ANKLE2 family. {ECO:0000305}.
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DR EMBL; AY325182; AAP92583.1; -; mRNA.
DR RefSeq; NP_001041366.1; NM_001047901.1. [Q7TP65-2]
DR AlphaFoldDB; Q7TP65; -.
DR SMR; Q7TP65; -.
DR STRING; 10116.ENSRNOP00000053507; -.
DR PhosphoSitePlus; Q7TP65; -.
DR jPOST; Q7TP65; -.
DR PaxDb; Q7TP65; -.
DR PRIDE; Q7TP65; -.
DR GeneID; 360829; -.
DR KEGG; rno:360829; -.
DR CTD; 23141; -.
DR RGD; 1310191; Ankle2.
DR eggNOG; ENOG502QQ4Z; Eukaryota.
DR InParanoid; Q7TP65; -.
DR Reactome; R-RNO-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR PRO; PR:Q7TP65; -.
DR Proteomes; UP000002494; Unplaced.
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 InterPro; IPR011320; RNase_H1_N.
DR PANTHER; PTHR12349:SF4; PTHR12349:SF4; 1.
DR Pfam; PF01693; Cauli_VI; 1.
DR Pfam; PF03020; LEM; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF63451; SSF63451; 1.
DR PROSITE; PS50954; LEM; 1.
PE 2: Evidence at transcript 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_0000280244"
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 72..116
FT /note="LEM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT REPEAT 420..449
FT /note="ANK"
FT REGION 667..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XL3"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XL3"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XL3"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XL3"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XL3"
FT MOD_RES 676
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 892..964
FT /note="SWPSPALKGKFTTELVDLDCCHSCSGRSSPAGSSPSKPGHTTFSSGLHSPGR
FT YSPAHGRHFQRVACMARLAAL -> RGGYNVENKCLQLYGRNQQEMLLNSPSSLLLEEM
FT VKGFVF (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_044174"
SQ SEQUENCE 964 AA; 106439 MW; C290DD424D66B585 CRC64;
MLWQRLAVVE WAALAWELLG ASVLLIAVRW LVRRLENLSR DPNRCGTLSS LPGASAAVSA
QPGEVMTMDA MLARLKLLNP DDLRQEVMKA GLKCGPITST TRFIFEKKLA QALLEQGGLL
TSSLPKHSEV TGTAFIHGTS RTPAFVDRKQ TQQACLSEDR DFGYSVGLNP PEEEAVTSSV
HPIPFSASTR NDNHKAGVTT AKEPLLYYGV CPVYEDGLVR HERIHVYEDK KEALQAVKLI
KGSRFKAFPT REDAEKFARG ICDYLPSPSK NMSLLSPVKA MPLCSNDGPK ADGLCLAESE
TVNKERANSY KNPRTQDLTA KLRKAVERGE EHTFSDLIWS NPRYLIGSGD NPTIVQEGCR
YNVMHVAAKE NQASVCQLTL ETLENPEFMR LMYPDDNMDM LQKRILYIVD LYLNTPDKVG
FDTPLHFACK FGNVDVVNVL SSHPLIVKNP RNKYGKTPED VICERSKNKS VELRERIREY
LMGHYYVPLL RAEDTSPVIG ELWSSDQKAE ASSADHCRSS PRDPVMTLRA FVGPLSPSKA
EDFRKLWKTP PRKKAGLFHS IRKSDPERGI ERVGRELAHE LGYPWVEYWE FLGCFVDLSS
QEGLQRLEEY LIQKELNQKA QHEIGEEEGC LQDRTSDFGS GKKYSNSISV GAFLDGGDDI
SLEEVKNQQN TVPSQSQPSV DKFQNSKSGS PSLGQKADPG EAAVGFYPDN SRNGFCYPLN
SRTADGRETE ATNGEEALPP PVSILTQEFD KLNLQSLGDN LFETPNKNRE LEDKILASSK
GVVESGLASP AAIARLENKQ VRTNSEVSEA MAEMSLGPNS PQLGVQAGLE PGFSSATADP
TKRLFLSGEE PSKLDRDVLA ALECAIIDPG LYPAVHRWKS TVMGYSPSDR QSWPSPALKG
KFTTELVDLD CCHSCSGRSS PAGSSPSKPG HTTFSSGLHS PGRYSPAHGR HFQRVACMAR
LAAL
