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Database: UniProt
Entry: A0A3B5Q092_XIPMA
LinkDB: A0A3B5Q092_XIPMA
Original site: A0A3B5Q092_XIPMA 
ID   A0A3B5Q092_XIPMA        Unreviewed;      1385 AA.
AC   A0A3B5Q092;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
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};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000024535.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000024535.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000024535.1};
RG   Ensembl;
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   Ensembl; ENSXMAT00000040841.1; ENSXMAP00000024535.1; ENSXMAG00000010314.2.
DR   GeneTree; ENSGT00940000157833; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; IPR019749; Band_41_domain.
DR   InterPro; IPR021187; EPB4.1_FERM_F1.
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:SF12; PROTEIN 4.1; 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   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   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          544..825
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          848..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          915..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1128..1155
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..541
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        921..943
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1385 AA;  159978 MW;  B0373DC987B0F460 CRC64;
     MATMTTEASA VNEADTEGKQ KSSRAPPEAE SVQQETTATE QEGEQSSKKA QEQAAEPGPV
     DVATSPEEEQ LKPRTRTSAG KGLSRLFSSF LKRRSQCSDG EGFEAERASD EKADKEKADN
     VEEEKVEEVK SEDKESKIVE EKLDVKEVKK KEEDKIEQKE EKKKVEEKVE KKGSKKKKKE
     AKKKAEEKDE GKVKKDEAKK EEEKPEEQKD EKIKTIVEKE EAKPETKVEE KKQVTQIKEK
     GTESGKKEEG KVDKKEAKKK EKEEKLKKKE EEKTKRKAEE DERVRKREEE KAKKREEEKA
     REVEKLKKKE EVKAKKKEEE KAKEEKTKKK EEEKAKEEKA KKEEEKTKEE KTKKKDEKAK
     EDQEKKKEED KPKEEKQEEK VKHLEKTEKE EEKTEETQQK EEEKGKKREK GKDKGKKEDK
     EENKPSEEQV KAPIAAPEPE LKLELDTEQA GDHQSVSSAE TQPAPEEQKE EPKVKEELEI
     KKEPEVEEEI KEGIEKKKEP TEQQEVTKGE EKTTEKTKKE KPPKQKKTEK KAEEAKGPKR
     PKAMQCKVTL LDDTLFECEL DKHAKGQELL TKVCDHVNLL EKDYFGLAIW ETPTGKTWLE
     PIKEIRKQVS GGVYEFTFNV KFYPPDPAQL TEDLTRYFLC LQLRKDIMQG VLPCSFVTLS
     LLGSYTAQSE LGEYDPEVHG TDYVKDLNLA PGQSKELEEK VMELHRTYRS MSPAQADLLF
     LENAKKLAMY GVDLHQAKDL DGVDITLGVC SSGLMVYKDK LRINRFPWPK VLKISYKRSS
     FFIKIRASEQ EQYESTIGFK LPNYKASKKL WKVCVEHHTF FRVPSVEPPS SRRFLALGSK
     FRYSGRTQAQ TRQASSMIDR PAPRFTRSAS KRLSRNLDGA GDETLQFLQL LSASSRSEAD
     DWSLLITTHK SRPSVEFPAR GESEQASSQS REEEQSVTWK GTETVDGGSQ IISEQQHQHL
     KEGEWSDLLY RQPSVATVET FDFVEHQAKP SFGYSSSPDP LHKPAPFQQD DWFLYFGRFL
     SESEENILSS SKIQSQIRLE ELATSVVKQE ETTEQVIERL QKSVILIDTL TEIEDLEGKL
     RKVRDLEERL QEAGEVSERI LRVIEEQLGQ EEVERLRAEE GDLDHVVLQR FMKRMETDED
     EVDELEEQIK DVFLKGLVPE EENELNQLDG SLRTKVREIQ KEWQEEQRKF DSSDVSGATS
     VVILQKVERR DGKRVMIVDE SGESNGMLEK QTQREVTERR HFGNPAQEEN EDEWYLLFYR
     PPVFSPSDES TYLRSVVKRQ VGEEEIKEQP WILQQPALME RVDDWFVLLA GPPRETKYVE
     AVAMKEAQMD EGQFVSVVEV SEDYKVEIEE RQMIQETQRE TWMERGTAKT VCAGFALLPC
     ILLAC
//
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