ID A0A1S3S881_SALSA Unreviewed; 1136 AA.
AC A0A1S3S881;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Band 4.1-like protein 2 isoform X1 {ECO:0000313|RefSeq:XP_014060546.1, ECO:0000313|RefSeq:XP_014060547.1};
GN Name=LOC100380760 {ECO:0000313|RefSeq:XP_014060546.1,
GN ECO:0000313|RefSeq:XP_014060547.1, ECO:0000313|RefSeq:XP_014060548.1,
GN ECO:0000313|RefSeq:XP_014060549.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014060549.1};
RN [1] {ECO:0000313|RefSeq:XP_014060546.1, ECO:0000313|RefSeq:XP_014060547.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014060546.1,
RC ECO:0000313|RefSeq:XP_014060547.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014060546.1; XM_014205071.1.
DR RefSeq; XP_014060547.1; XM_014205072.1.
DR RefSeq; XP_014060548.1; XM_014205073.1.
DR RefSeq; XP_014060549.1; XM_014205074.1.
DR GeneID; 100380760; -.
DR KEGG; sasa:100380760; -.
DR CTD; 2037; -.
DR OrthoDB; 5391231at2759; -.
DR Proteomes; UP000087266; Chromosome ssa06.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
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; 3.
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 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 251..532
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..901
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 125190 MW; C14736699B8338FB CRC64;
MTTEVGSETE VRKEPEKAEE QPAAPESEPA ATNQTDEAKA AEQSANDHPA PATDSAEAPT
EAKEKQEEAQ PADNATPQEG EDTPASPPTS EKKGISRFLP PWLKKQKSQS QVGPKESQAA
PKEEAGVASV KEEDGEKGEQ AEAEQTSLAT AAEPQVEEEK INGEPKPEQK EEVKSEEKEE
ENHSTGSADS QPAKEEKAAE ESQEKSAAEE ENKEAEEGGE EKKDEEESPK PEGGHSFIKS
PLKLTKKVKM VMCHVTMLDG SQFPCEVEKR AKGQYLFFKV YEALNLLEKD YFGLSYKDNS
DQTCWLDPTK EIKRQIRNAT WQFAFNVKFY PPDPSQLTED ITRYLLCLQL RQDIVSGRLP
CSFVTHSLLG SYALQAELGD HDSGEHRLDY ISDFQFAPSQ TKEMEEKVVE LHKTHRGMTP
AQADAQFLEN AKKLSMYGVD LHHAKDSEGV DIMLGVCANG LLIYKDRLRI NRFAWPKILK
ISYKRSNFYI KIRPGETEQF ESSVGFKLPN HRAAKRVWKV CVENHTFFRL MTPEAPTKAK
FLTLGSKFRY SGRTQAQTRQ ASTLIDRPAP YFERTSSKRI SRSLDGAPVI NVTEARESAP
TSGENGREPG LELSSDSKVE EEPSEGAAAT PTEGTEMKGD EPDSSQQDLD KTQEDVLKHQ
ASISELKRSF MEATPEPRPS QWEKRLTASP ATSLRLQAQG SLEEEMTSIL FSKFACESGL
VDPGCTTTRR AAEGAVVTAS VPLASALLTT EVLSTDESKP RKHQRCPPSR TQEPLPDLTV
DTVAKSADDK QKSGEAAWQA AEVEIEETVV VEEIRVAPKG SVTVTTPEVI TPVAVETEVE
KPKEEVKEEQ KRPVSVSSDS EEEEEEEEAG EYHPQVTVSA SVDQIKEEPE EEEEEEQQVN
EEPVAEPLPK PVVEVKAQPV PAVVEETSAT EPQLAPVAEE SPEDILVTPD EAPNGHAESP
EGHPGPVPLE EEEEEPRVNG DASHSETERL PQVMCCSEPP VVKTEMVTIS DTFAAQKTEI
ATKEVPIVHT ETKTITYEAA QLDGSGDGEP GVLMTAQTIT SESLCTTTTT HITKTLKGGL
SETRIEKRIV ITGDSDIDHD QALAQAIKEA KEQHPDMSVT RVVVHKETEL AEEGED
//
