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Database: UniProt
Entry: A0A2Y9R7R7_TRIMA
LinkDB: A0A2Y9R7R7_TRIMA
Original site: A0A2Y9R7R7_TRIMA 
ID   A0A2Y9R7R7_TRIMA        Unreviewed;       637 AA.
AC   A0A2Y9R7R7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Protein 4.1 {ECO:0000256|ARBA:ARBA00023658};
DE   AltName: Full=Band 4.1 {ECO:0000256|ARBA:ARBA00030419};
DE   AltName: Full=Erythrocyte membrane protein band 4.1 {ECO:0000256|ARBA:ARBA00032586};
GN   Name=LOC101353656 {ECO:0000313|RefSeq:XP_023587809.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023587809.1};
RN   [1] {ECO:0000313|RefSeq:XP_023587809.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_023587809.1; XM_023732041.1.
DR   AlphaFoldDB; A0A2Y9R7R7; -.
DR   Proteomes; UP000248480; Unplaced.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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   CDD; cd17105; FERM_F1_EPB41; 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; IPR021187; EPB4.1_FERM_F1.
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:SF12; PROTEIN 4.1; 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; 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   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..282
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          325..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   637 AA;  72053 MW;  A8C5C8983D4EF130 CRC64;
     MHCKVYLLDD TVYECSVEKH AKGQDLLKQV CQHLNLLEKD YFGLAVWDNG TSKTWLDPAK
     EIRKQISGFP WNFTFNVKFY PPDPAQLTED ITRYYLCLQL RQDIVAGRLP CSFATLALLG
     SYTIQSELGD YDQELHGADY VSDFKLAPNQ TKELEEKVME LHKSYRSMTP AQADLEFLEN
     AKKLSMYGVD LHRAKDLEGV DIILGVCSSG LLVYKDKLRI NRFPWPKVLK ISYKRSSFFI
     KIRPGEQEQY ESTIGFKLPS YRAAKKLWKV CVEHHTFFRL TSTDTIPKSK FLALGSKFRY
     SGRTQAQTRQ ASALIDRPAP YFERTASKRA SRSLDGAAAD SADRSPWPTS APALAESQIP
     EDSDSGSQKK REEMPPEEVE PEPTEAWKVE KTHIKVTVPT SNGDQTQKPA EKTEDLIRMR
     KKKRERLDGE NIYIRHSNLM LEDLDKNQEE IKKHHASISE LKKNFMESVP EPRPSEWDKR
     LSTHSPFRTL SINGQVPTGE GPPLVKTQTV TISDSANAVK SEIPTKDVPI VHTETKTITY
     EAAQTDDNNG DLDPGVLLTA QTITSETTSG TTTTQITKTV KGGMSETRIE KRIVITGDTD
     IDHDQVLAQA IKEAKEQHPD MSVTKVVVHQ ETEIAEE
//
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