GenomeNet

Database: UniProt
Entry: A0A093H1Z0_STRCA
LinkDB: A0A093H1Z0_STRCA
Original site: A0A093H1Z0_STRCA 
ID   A0A093H1Z0_STRCA        Unreviewed;       636 AA.
AC   A0A093H1Z0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Macoilin {ECO:0000256|ARBA:ARBA00021882};
DE   AltName: Full=Transmembrane protein 57 {ECO:0000256|ARBA:ARBA00031129};
DE   Flags: Fragment;
GN   ORFNames=N308_09423 {ECO:0000313|EMBL:KFV73112.1};
OS   Struthio camelus australis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV73112.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV73112.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV73112.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in the regulation of neuronal activity.
CC       {ECO:0000256|ARBA:ARBA00003440}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Nucleus membrane
CC       {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004232}. Rough endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004269}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004269}.
CC   -!- SIMILARITY: Belongs to the macoilin family.
CC       {ECO:0000256|ARBA:ARBA00008298}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KL205698; KFV73112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093H1Z0; -.
DR   STRING; 441894.ENSSCUP00000000439; -.
DR   Proteomes; UP000053584; Unassembled WGS sequence.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0023041; P:neuronal signal transduction; IEA:InterPro.
DR   InterPro; IPR019130; Macoilin.
DR   PANTHER; PTHR47464; MACOILIN; 1.
DR   PANTHER; PTHR47464:SF2; MACOILIN; 1.
DR   Pfam; PF09726; Macoilin; 1.
DR   SUPFAM; SSF46579; Prefoldin; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        47..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          180..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          606..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          356..523
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          565..592
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        221..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV73112.1"
FT   NON_TER         636
FT                   /evidence="ECO:0000313|EMBL:KFV73112.1"
SQ   SEQUENCE   636 AA;  73037 MW;  4855FD68B18E54BC CRC64;
     STFLYLKFLV VWALVLLADF VLEFRFEYLW PFWLFIRSVY DSFRYQGLAF SVFFVCVAFT
     SNIICLLFIP IQWLFFAAST YVWVQYVWHT ERGVCLPTVS LWILFVYIEA AIRFKDLKNF
     HVDLCRPFAA HCIGYPVVTL GFGFKSYVSY KMRLRKQKEV QKENEFYMQL LQQALPPEQQ
     MLQRQEREAE EGKGLSDMDP SILLQHNGGI PANKKLSSAT LPELEYREKG KEKDKDAKKH
     NLGINNNILQ PVDSKIQEIE YMENHINSKR LNNDLVGSTE NLLKEDSCTA SSKNYKNVSG
     VVNSSPRSHS ATNGSIPSSS TKNEKKQKCA SKSPSTHKDL MENCIPNNQL SKPDALVRLE
     QDIKKLKADL QASRQIEQEL RSQISSLTNT ERGIRSEIGQ LRQENELLQN KLHNAVQMKQ
     KDKQMISQLE KKLKAEQEAR AFVEKQLMEE KKRKKLEEAS AARAVAFAAT RGECTETLRN
     RIRELETECK KLTIDIKLKE DQIRELEMKV QELRKYKENE KDTEVLMSAL SAMQDKTQHL
     ENSLSAETRI KLDLFSALGD AKRQLEIAQG QIIQKDQEIK DLKQKIAEVM AVMPSITYTA
     ATSTLSPVSP HYSSKFVETS PSGLDPNASV YQPLKK
//
DBGET integrated database retrieval system