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 03-AUG-2022, entry version 82.
DE RecName: Full=Band 4.1-like protein 4B;
DE AltName: Full=Erythrocyte membrane protein band 4.1-like 4B {ECO:0000312|RGD:1562988};
GN Name=Epb41l4b {ECO:0000312|RGD:1562988};
GN Synonyms=Lulu2 {ECO:0000250|UniProtKB:Q9H329};
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].
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 project:
RT 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 cellular
CC adhesion, migration and motility in vitro and may play a role in wound
CC healing. May have a role in mediating cytoskeletal changes associated
CC with steroid-induced cell differentiation.
CC {ECO:0000250|UniProtKB:Q9H329, ECO:0000250|UniProtKB:Q9JMC8}.
CC -!- SUBUNIT: Interacts (via FERM domain) with ARHGEF18 (via C-terminus);
CC the interaction activates ARHGEF18. {ECO:0000250|UniProtKB:Q9JMC8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H329}. Cell
CC junction, tight junction {ECO:0000250|UniProtKB:Q9H329}.
CC Note=Accumulates along apical cell-cell boundaries and is also detected
CC in the cytoplasm in a punctate manner. {ECO:0000250|UniProtKB:Q9H329}.
CC -!- PTM: May be negatively regulated by phosphorylation.
CC {ECO:0000250|UniProtKB:Q9JMC8}.
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DR EMBL; BC166749; AAI66749.1; -; mRNA.
DR RefSeq; NP_001121037.1; NM_001127565.1.
DR AlphaFoldDB; B2RYE5; -.
DR SMR; B2RYE5; -.
DR STRING; 10116.ENSRNOP00000015114; -.
DR iPTMnet; B2RYE5; -.
DR PhosphoSitePlus; B2RYE5; -.
DR PaxDb; B2RYE5; -.
DR PeptideAtlas; B2RYE5; -.
DR PRIDE; B2RYE5; -.
DR Ensembl; ENSRNOT00000088169; ENSRNOP00000068924; ENSRNOG00000056550.
DR GeneID; 500464; -.
DR KEGG; rno:500464; -.
DR UCSC; RGD:1562988; rat.
DR CTD; 54566; -.
DR RGD; 1562988; Epb41l4b.
DR eggNOG; KOG3530; Eukaryota.
DR GeneTree; ENSGT00940000158331; -.
DR InParanoid; B2RYE5; -.
DR OrthoDB; 241659at2759; -.
DR PhylomeDB; B2RYE5; -.
DR PRO; PR:B2RYE5; -.
DR Proteomes; UP000002494; Chromosome 5.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; ISO:RGD.
DR GO; GO:0042060; P:wound healing; ISO:RGD.
DR CDD; cd14473; FERM_B-lobe; 1.
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_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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23280:SF18; PTHR23280:SF18; 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 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; SSF54236; SSF54236; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cytoplasm; Phosphoprotein; Reference proteome;
KW Tight junction.
FT CHAIN 1..527
FT /note="Band 4.1-like protein 4B"
FT /id="PRO_0000352794"
FT DOMAIN 85..369
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 23..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
