ID A0A673TVS2_SURSU Unreviewed; 927 AA.
AC A0A673TVS2;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Erythrocyte membrane protein band 4.1 like 2 {ECO:0000313|Ensembl:ENSSSUP00005013121.1};
OS Suricata suricatta (Meerkat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Herpestidae; Suricata.
OX NCBI_TaxID=37032 {ECO:0000313|Ensembl:ENSSSUP00005013121.1, ECO:0000313|Proteomes:UP000472268};
RN [1] {ECO:0000313|Ensembl:ENSSSUP00005013121.1, ECO:0000313|Proteomes:UP000472268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dudchenko O., Lieberman Aiden E., Tung J., Barreiro L.B.,
RA Clutton-Brock T.H.;
RT "A Chromosome-scale Meerkat (S. suricatta) Genome Assembly.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSUP00005013121.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A673TVS2; -.
DR Ensembl; ENSSSUT00005014996.1; ENSSSUP00005013121.1; ENSSSUG00005008237.1.
DR Proteomes; UP000472268; Chromosome 7.
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 CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13184; FERM_C_4_1_family; 1.
DR CDD; cd17202; FERM_F1_EPB41L2; 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; 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 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 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Reference proteome {ECO:0000313|Proteomes:UP000472268}.
FT DOMAIN 210..491
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 103016 MW; 172B7FA4C5A036AE CRC64;
MTTEVGSTSE VKKDPEQLGA DADTAKEKSK EAAENQQNQS SSGSEEEKGS QSPPAAESQS
SPRRQKREKD SSESRGISRF IPPWLKKQKS YTLVVAKDGG DKKEPTQAVA EEILDKEESL
PEGEREAKGD AGETAQRKQE IKADVKEEKP SVSGPVAQPA EEVNKEREEK AKEIQEDKSE
EAKRETKEVQ TNELKSEKAA QKATKKAKTV QCKVTLLDGT EYSCDLEKRA KGQVLFDKVC
EHLNLLEKDY FGLLFQESPE QKNWLDPAKE IKRQLRNLPW LFTFNVKFYP PDPSQLTEDI
TRYFLCLQLR QDIASGRLPC SFVTHALLGS YTLQAELGDY DPEEHGSSDL TDFQFAPTQT
RELEEKVAEL HKTHRGLSPA QADSQFLENA KRLSMYGVDL HHAKDSEGVD IKLGVCANGL
LIYKDRLRIN RFAWPKILKI SYKRSNFYIK VRPAELEQFE STIGFKLPNH RAAKRLWKVC
VEHHTFYRLV SPEQPPKAKF LTLGSKFRYS GRTQAQTRQA STLIDRPAPH FERTSSKRVS
RSLDGAPVGV VDQSLMKEFP GPAGEVSAYG PGAVSPAMVQ DGDGRRDLRS PAKIPHVQFI
EGKSSHETLN VVEEKQQAEV GKDERVITEE TNGKELSPGS GPGETRKVEP LTQKDSTSLS
SESSSGSESE EEEDVGEYRP HHRVTQGTIR EEQEEYDEEV EEEAGRAAKV VEREDPVPEA
SPVRQAGASV SAVDTVTREN VVAPKLSAEK SVHEGAIKQD MSEEPEDEQH KVNGEVSHVD
IDVLPQVICC SEPPVVKTEM VTISDASQRT EISTKEVPIV QTETKTITYE SPQIDGGAGG
DSGTLLTAQT ITSESVSTTT TTHITKTVKG GISETRIEKR IVITGDADID HDQALAQAIR
EAREQHPDMS VTRVVVHKET ELEEGEE
//
