ID A0A1S3M9Z1_SALSA Unreviewed; 1113 AA.
AC A0A1S3M9Z1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Protein 4.1-like isoform X4 {ECO:0000313|RefSeq:XP_013999834.1};
GN Name=LOC106571359 {ECO:0000313|RefSeq:XP_013999834.1};
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_013999834.1};
RN [1] {ECO:0000313|RefSeq:XP_013999834.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013999834.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_013999834.1; XM_014144359.1.
DR AlphaFoldDB; A0A1S3M9Z1; -.
DR GeneID; 106571359; -.
DR OrthoDB; 5391231at2759; -.
DR Proteomes; UP000087266; Chromosome ssa15.
DR Bgee; ENSSSAG00000080163; Expressed in camera-type eye and 14 other cell types or tissues.
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; 4.
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 244..525
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..963
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 115..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..876
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 123604 MW; 530A0E689707404F CRC64;
MTTEVGSETE VKKEPEKAEE QPAEPEPPAT NQTDEVKAVE AAEQSNESPA LATDSAEAKE
NQEEAQPTDN ATGPAGEDPS VSPPASEKKG ISRFLPPWLK RQKSQSAVGP KESQATPKEE
GDVVLVKEEG EKAEHAKAEQ TSSTTAAVPQ VEEEQVNGEA EQEQKEEVNS EEQEETHSTG
SAETRPAKEE KASEKSQKKS AAEEEKKETE EGGEKKDQEE SLKPEEGRYF IKSPLKLTKK
VKLVICHVTM LDGSQFPCEV EKRAKGQYLF FKVCEALNLL EKDYFGLSYK DNADQTCWLD
PTKEIKRQIC NTSWQLAFNV KFYPPDPSQL TEDITRYLLC LQLRQDIASG RLPCSFVTHS
LLGSYSLQAE LGDHDPDEQR LDYISDFQFA PSQTKEMEEK VVELHKTHRG MTPAQADTQF
LENAKKLSMY GVDLHHAKDS EGVDIMLGVC ANGLLIYKDR LRINRFAWPK ILKISYKRSN
FYIKIRPGET EQFESTVGFK LPNHRSAKRV WKVCVENHTF FRLMTPEAPA KAKFLTLGSK
FRYSGRTQAQ TRQASTLIDR PAPYFERTSS KRISRSLDGA PVINVIEAQD SAPTPVGNGR
EPGLELSSDS SKVEEEPSEG AAATPTEGTE MKRDEPDSSQ QSGKLRVQGE NIYVRHSNLM
LEDLDKTQED VLKHQASTSE LKRSFMEATP ETRPSQWEKR LTASPATSLR LQAQGRSPPP
TTQEPLPDLT VDTVSKSSDD KEKSDKTTLQ AAEVEIEETV VVEEIRVAPK VSVTITPEVV
VTPVAVETEV EKPKEEVMEE VMEEVMEEVK EEVKEEVNEE QKRPVSVSSD SHSESEEEAG
EYHSQVTISA SVDQIKEEPE EEEEEEEVED HEEPEQVAEP EPLPEVKVEA MPSPAVVEET
PMAEPETALV ADALAKEEST EDILVTPDEA PNGHAEDQSG LVAVEEEEEE EEPRVNGDAS
HAETERIPQV ICCSEPPVVK TEMVTISDTF AAQKTEIATK EVPIVHTETK TITYEAAQLD
GSGDGEPGIL MTAQTITSES LCTTTTTHIT KTLKGGLSET RIEKRIVITG DSDIDHDQAL
AQAIKEAKEQ HPDMSVTRVV VHKETELAEE GED
//
