GenomeNet

Database: UniProt
Entry: D3ZM69_RAT
LinkDB: D3ZM69_RAT
Original site: D3ZM69_RAT 
ID   D3ZM69_RAT              Unreviewed;       996 AA.
AC   D3ZM69;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 2.
DT   27-MAR-2024, entry version 106.
DE   SubName: Full=Erythrocyte membrane protein band 4.1-like 2 {ECO:0000313|Ensembl:ENSRNOP00000058049.3};
GN   Name=Epb41l2 {ECO:0000313|Ensembl:ENSRNOP00000058049.3,
GN   ECO:0000313|RGD:1563977};
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 {ECO:0000313|Ensembl:ENSRNOP00000058049.3, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000058049.3, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000058049.3,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
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).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
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).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000058049.3}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000058049.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_017443277.1; XM_017587788.1.
DR   RefSeq; XP_017445345.1; XM_017589856.1.
DR   AlphaFoldDB; D3ZM69; -.
DR   SMR; D3ZM69; -.
DR   IntAct; D3ZM69; 1.
DR   STRING; 10116.ENSRNOP00000058049; -.
DR   PaxDb; 10116-ENSRNOP00000058049; -.
DR   Ensembl; ENSRNOT00000061332.6; ENSRNOP00000058049.3; ENSRNOG00000012346.9.
DR   AGR; RGD:1563977; -.
DR   RGD; 1563977; Epb41l2.
DR   eggNOG; KOG3527; Eukaryota.
DR   GeneTree; ENSGT00940000155617; -.
DR   OrthoDB; 5391231at2759; -.
DR   Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000012346; Expressed in lung and 18 other cell types or tissues.
DR   ExpressionAtlas; D3ZM69; baseline and differential.
DR   GO; GO:0005938; C:cell cortex; ISO:RGD.
DR   GO; GO:0008180; C:COP9 signalosome; ISO:RGD.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0042731; F:PH domain binding; ISO:RGD.
DR   GO; GO:0030507; F:spectrin binding; ISO:RGD.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:1904778; P:positive regulation of protein localization to cell cortex; ISO:RGD.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13184; FERM_C_4_1_family; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR008379; Band_4.1_C.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
DR   InterPro; IPR014847; FA.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR007477; SAB_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR   PANTHER; PTHR23280:SF17; BAND 4.1-LIKE PROTEIN 2; 1.
DR   Pfam; PF05902; 4_1_CTD; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF04382; SAB; 1.
DR   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01195; FA; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   1: Evidence at protein level;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
SQ   SEQUENCE   996 AA;  110711 MW;  AE8C9954C4E18CAE CRC64;
     MTTEVASASE VKKGSDPSGA DAHKEKAKEV VENEQTAASE LDEGKASQPG PTAESQSSPH
     RRKRGKDPSE NRGISRFIPP WLKKQKSYSL VVAKDGGDKK EPTQADGEDQ ILDKEDTLPE
     EESRAKGDAE EMAQRKHLEV KVEVREEKSA LKSSAEIQPA EQVRKDKEEE VIQDIQEEKL
     EGGAAKRETK EVQTSELKAE VASQKAAKKT KTVLAKVTLL DGTEFSCDLE KRAKGQALFD
     RVCEHLNLLE KDYFGLIFQE HPEQKNWLDP AKEIKRQLRS LPWLFTFNVK FYPPDPSQLT
     EDITRYFLCL QLRQDISSGR LPCSFVTHAL LGSYTLQAEH GDYDPEEYDS IDLGDFQFAP
     THNKELEEKV AELHKTHRGL SPAQADSQFL ENAKRLSMYG VDLHHAKDSE GVDIKLGVCA
     NGLLIYKDRL RINRFAWPKI LKISYKRSNF YIKVRPGELE QFESTIGFKL PNHRAAKRLW
     KVCVEHHTFY RLVSPEQPPK TKFLTLGSKF RYSGRTQAQT REASTLIDRP APQFERASSK
     RVSRSLDGAP IGVVDQSLMK DFPGPPGEGS VPGPGVVSYT TVQDGRRDGK SPTKVTPLLA
     EGKKNTLRVD GDNIYVRHSN LMLEDLDKAQ EAILKHQASV SELKRNFMES TPEPRPSEWE
     KRRVTPLSCQ ILASSHETLN VVEEKKRAEV GKGESVITEE MNGKELSPGS GPGETRKVEP
     MAHKDSTSLS SESSSSSSES EEDVGEYQPH HRVTEGTIRE EQEYEEELEE EPGQGAKVVE
     REAAMPEAIP DRQAGASVLP VETEAQENVV AQKLPGEKGA HRGTAEQDMS EEAEEDQHRV
     NGEVPHLDID GLPEIVCPSE PPVVKTEMVT ISDASQRTEI STKEVPIVQT ETKTITYESP
     QIDGGAGGDS GVLLTAQTIT SESASTTTTT HITKTVKGGI SETRIEKRIV ITGDAALDHD
     QALAQAIREA REQHPDMSVT RVVVHKETEL AEEGED
//
DBGET integrated database retrieval system