GenomeNet

Database: UniProt
Entry: E41LB_RAT
LinkDB: E41LB_RAT
Original site: E41LB_RAT 
ID   E41LB_RAT               Reviewed;         527 AA.
AC   B2RYE5;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   02-NOV-2016, entry version 61.
DE   RecName: Full=Band 4.1-like protein 4B;
GN   Name=Epb41l4b; Synonyms=Lulu2 {ECO:0000250|UniProtKB:Q9H329};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Up-regulates the activity of the Rho guanine nucleotide
CC       exchange factor ARHGEF18. Involved in the regulation of the
CC       circumferential actomyosin belt in epithelial cells. Promotes
CC       cellular adhesion, migration and motility in vitro and may play a
CC       role in wound healing. May have a role in mediating cytoskeletal
CC       changes associated with steroid-induced cell differentiation.
CC       {ECO:0000250|UniProtKB:Q9H329, ECO:0000250|UniProtKB:Q9JMC8}.
CC   -!- SUBUNIT: Interacts (via FERM domain) with ARHGEF18 (via C-
CC       terminus); the interaction activates ARHGEF18.
CC       {ECO:0000250|UniProtKB:Q9JMC8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H329}.
CC       Cell junction, tight junction {ECO:0000250|UniProtKB:Q9H329}.
CC       Note=Accumulates along apical cell-cell boundaries and is also
CC       detected in the cytoplasm in a punctate manner.
CC       {ECO:0000250|UniProtKB:Q9H329}.
CC   -!- PTM: May be negatively regulated by phosphorylation.
CC       {ECO:0000250|UniProtKB:Q9JMC8}.
CC   -!- SIMILARITY: Contains 1 FERM domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00084}.
DR   EMBL; BC166749; AAI66749.1; -; mRNA.
DR   RefSeq; NP_001121037.1; NM_001127565.1.
DR   UniGene; Rn.21106; -.
DR   ProteinModelPortal; B2RYE5; -.
DR   STRING; 10116.ENSRNOP00000015114; -.
DR   iPTMnet; B2RYE5; -.
DR   PhosphoSitePlus; B2RYE5; -.
DR   PaxDb; B2RYE5; -.
DR   PeptideAtlas; B2RYE5; -.
DR   PRIDE; B2RYE5; -.
DR   GeneID; 500464; -.
DR   KEGG; rno:500464; -.
DR   UCSC; RGD:1562988; rat.
DR   CTD; 54566; -.
DR   RGD; 1562988; Epb41l4b.
DR   eggNOG; ENOG410IQ5Y; Eukaryota.
DR   eggNOG; ENOG410YG1S; LUCA.
DR   HOGENOM; HOG000231632; -.
DR   HOVERGEN; HBG051435; -.
DR   InParanoid; B2RYE5; -.
DR   PhylomeDB; B2RYE5; -.
DR   PRO; PR:B2RYE5; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0019898; C:extrinsic component of membrane; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR030698; Band4.1-like4B.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
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_dom-like.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   PANTHER; PTHR23280:SF18; PTHR23280:SF18; 2.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 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; SSF47031; SSF47031; 1.
DR   SUPFAM; SSF50729; SSF50729; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Complete proteome; Cytoplasm; Phosphoprotein;
KW   Reference proteome; Tight junction.
FT   CHAIN         1    527       Band 4.1-like protein 4B.
FT                                /FTId=PRO_0000352794.
FT   DOMAIN       85    369       FERM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00084}.
SQ   SEQUENCE   527 AA;  59571 MW;  04D364E3AE85555D CRC64;
     MLRFLRRTFG RRSMQRYARG AAGRGAAGLG DERDGGPRGG PAAAASSSVL PAAPGGSVFP
     AGGGPLLTGG AAVHISASGA AKATLYCRVF LLDGTEVSVD LPKHAKGQDL FDQIVYHLDL
     VETDYFGLQF LDSAQVTHWL DHSKPIKKQM KVGPAYALHF RVKYYSSEPN NLREEFTRYL
     FVLQLRHDIL SGKLKCPYET AVELAALCLQ AELGECELPE HTPELVSEFR FIPNQTEAME
     FDIFQRWKEY RGKSPAQAEL SYLNKAKWLE MYGVDMHVVR GRDGCEYSLG LTPTGILIFE
     GANKIGLFFW PKITKMDFKK SKLTLVVVED DDQGREQEHT FVFRLDSART CKHLWKCAVE
     HHAFFRLRTP SNSKSARSDF IRLGSRFRFS GRTEYQATHG SRLRRTSTFE RKPSKRYPSR
     RHSTFKASNP VIAAQLCSKT NPEVHNYQPQ FHPNVHPSQP RWRPHSPNVS NHSTCKQNKP
     SFQDDRPHWK ASASGDDGHF DYVHDQNQRN LGGAYSVTYR DKLMTAL
//
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