ID W5MS79_LEPOC Unreviewed; 1299 AA.
AC W5MS79;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=MIA SH3 domain ER export factor 2 {ECO:0000313|Ensembl:ENSLOCP00000011238.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000011238.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000011238.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; AHAT01003895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01003896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01003897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01003898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01003899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01003900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000011238; -.
DR Ensembl; ENSLOCT00000011254.1; ENSLOCP00000011238.1; ENSLOCG00000009207.1.
DR eggNOG; ENOG502QUND; Eukaryota.
DR GeneTree; ENSGT00950000182767; -.
DR HOGENOM; CLU_258922_0_0_1; -.
DR InParanoid; W5MS79; -.
DR OMA; GPDCLYL; -.
DR Proteomes; UP000018468; Linkage group LG7.
DR Bgee; ENSLOCG00000009207; Expressed in muscle tissue and 13 other cell types or tissues.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0035459; P:vesicle cargo loading; IBA:GO_Central.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23158:SF38; MELANOMA INHIBITORY ACTIVITY PROTEIN 2; 1.
DR PANTHER; PTHR23158; MELANOMA INHIBITORY ACTIVITY-RELATED; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1299
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004868204"
FT DOMAIN 38..100
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 128..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1185..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 648..724
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 867..986
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 129..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..827
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1299 AA; 145889 MW; 790C82CA7DC8398B CRC64;
FLYIGLHSGC ALLFLLNTRQ SLGLLSDYKT CGDLECESSI NRVRAIRNYK NPDCRFLNFR
SGDVIFVYHK LSGKRDDLWA GTIGKRFGYF PKDAVEVEET YATKEVQVPT KEHDFFCLDG
NGAFIESDSS HWDSEEHQEE TARDETESPE ASGSGRGSVT KFKNSEGIAK GQENGPAVPH
TTDRSEEPKT VERGGSHWLG SGITGWLGIG GQESRKIALD LKDNDLDGNK LETVAEAKKS
GWLGGQLSNI FGLSQETPSE VGGPDAPEKQ GVKVTLQDRG QSPATSNKRV IAETETTKEE
DAQSKSWLSF GVGDLLSYGQ KNSDKEGERN SEQSSQMSEL KAEMKESNAV PEVVITKDEE
HKKEENTGEE SLAKFSDEDK EHALSKEEPI ISGAINISGL NQNSQEEKNR LKEEEPPAVQ
LDVESVMEHD VISSYSEDIT ENVSDLQGDS EAKVRIEETS ASENTENMVD EARTTSVPED
TEGQKLQADE ARTTSVPEDN DSQKLQVDEA HITKDGRFKE EVTSSSGIGA VSFRMLSWVY
MLEDILQCVK CFRKAVSSLP EDMRPGPDLY GLPWEAVILT AFLGGMTVLM FFCRSCRSVK
SRLYVGKERK LGEKVAELLE EKCKVLETLS ECKSQYEKLE TTLKHGGLSE QATEKENLQV
MSKKLEQSNA ELKDEIERLK QDLDSQKATR SQQGELLAGM QLSLKSLEEE ARDVKSQMEQ
AQTTLKVYDI NSERLKKSIQ TALEENSHLH ESESQLAQEA EGWEERLSEL AEELKMCESS
RRDMQADSSN KEEQIKTLTD CLLKMKDWDS ELEEDANEEE EEGTSTTENG DLDMHQKQKV
QKLIYAARMN ADLKSMEEEK TRVFARLADE VKTKEDLRDR IGKLQTEKSS LQVESAKYTD
ETQKLQQKLQ IMTEMYQENE LKLHRKLTVE EKERLQKEQK LTKADEKISL AAEELNTYRQ
RTKDLEEELE RTYQAYKNQI SSHEKKAHDN WLAARAADRD LGDIKRENSH LRQKLTDAQF
RLELVEKDPY ALDVPGRPLF RGERSPFGPS PLGRPSSETR AFLSPPTLLD GPARLSPQFP
GGPGGRASRG PPVLSEGLDC DRILENHGSH SDSGSLSPTW ERDRRVQVPP PESFFPILEL
FFFSIIDNTE LGFKSKRCFF HFFSIIDNTE LGFKRYPYPD PNVPYRRPPP MPTLPPRLPG
PAEPHGYNPQ PADRPGLRMR GPPRDHFPRR PPFGPPELFH PRVAGAPPMG LRGPLPPPPP
PGMFPRFAPP PPPPPHHLGY PPPRPPSDGS PRPCPAGGE
//
