ID A0A0D9RR62_CHLSB Unreviewed; 518 AA.
AC A0A0D9RR62;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Motile sperm domain containing 2 {ECO:0000313|Ensembl:ENSCSAP00000011101.1};
GN Name=MOSPD2 {ECO:0000313|Ensembl:ENSCSAP00000011101.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000011101.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000011101.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000011101.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AQIB01143462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007989271.1; XM_007991080.1.
DR AlphaFoldDB; A0A0D9RR62; -.
DR STRING; 60711.ENSCSAP00000011101; -.
DR Ensembl; ENSCSAT00000013089.1; ENSCSAP00000011101.1; ENSCSAG00000014995.1.
DR GeneID; 103231628; -.
DR KEGG; csab:103231628; -.
DR CTD; 158747; -.
DR eggNOG; KOG1470; Eukaryota.
DR GeneTree; ENSGT00390000016713; -.
DR OMA; CHTVENS; -.
DR OrthoDB; 2168468at2759; -.
DR BioGRID-ORCS; 103231628; 3 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome X.
DR Bgee; ENSCSAG00000014995; Expressed in fibroblast and 7 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0140284; C:endoplasmic reticulum-endosome membrane contact site; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0033149; F:FFAT motif binding; IEA:Ensembl.
DR GO; GO:0140042; P:lipid droplet formation; IEA:Ensembl.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IEA:Ensembl.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000535; MSP_dom.
DR InterPro; IPR008962; PapD-like_sf.
DR PANTHER; PTHR46384; MOTILE SPERM DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR46384:SF1; MOTILE SPERM DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF00635; Motile_Sperm; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR SUPFAM; SSF49354; PapD-like; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50202; MSP; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 493..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..239
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 327..445
FT /note="MSP"
FT /evidence="ECO:0000259|PROSITE:PS50202"
FT REGION 252..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 59747 MW; A691FDC2E6C901B5 CRC64;
MAENHAQNKA KLISETRRRF EAEYVTDKSE KYDARDVERL QQDDNWVESY LSWRHNIVDE
TLKMLDESFQ WRKEISVNDL NESSIPRWLL EIGVIYLHGY DKEGNKLFWI RVKYHIKDQK
TISDKKKLIA FWLERYAKRE NGKPVTVMFD LSETGINSID MDFVRFIINC FKVYYPKYLS
KIVIFDMPWL MNAAFKIVKT WLGPEAVSLL KFTSKNEVQD YVSVEYLPPH MGGTDPFKYS
YPPLVDDDFQ TPLCENGPIT SEDETSSKED IESDGKETLE TISSEEQTPL VKKINPTEST
SKAEENEKVD SKMKAFKKPL SVFKGPLLHI SPAEELYFGN TESGEKKTLI VLTNVTKNIV
AFKVRTTAPE KYRVKPSNSS CDPGASVDIV VSPHGGLTVS AQDRFLIMAA EMEQSSGTGP
AELTQFWKEV PRNKVMEHRL RCHTVESSKP NTLTLKDNAF NMSDKTSEDI CLQLSHLLES
NRKLEDQVQR CIWFQQLLLS LTMLLLAFVT SFFYLLYS
//
