ID A0A164K733_9CRUS Unreviewed; 498 AA.
AC A0A164K733;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 15.
DE SubName: Full=Ganglioside-induced differentiation-associated protein 2 {ECO:0000313|EMBL:KZS03003.1};
GN ORFNames=APZ42_034442 {ECO:0000313|EMBL:KZS03003.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS03003.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS03003.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS03003.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS03003.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GDAP2 family.
CC {ECO:0000256|ARBA:ARBA00008355}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZS03003.1}.
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DR EMBL; LRGB01003375; KZS03003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164K733; -.
DR STRING; 35525.A0A164K733; -.
DR EnsemblMetazoa; XM_032931513.2; XP_032787404.1; LOC116924910.
DR OrthoDB; 1105329at2759; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR CDD; cd02905; Macro_GDAP2-like; 1.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR035793; Macro_GDAP2.
DR PANTHER; PTHR11106; GANGLIOSIDE INDUCED DIFFERENTIATION ASSOCIATED PROTEIN 2-RELATED; 1.
DR PANTHER; PTHR11106:SF72; GANGLIOSIDE-INDUCED DIFFERENTIATION-ASSOCIATED PROTEIN 2; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF01661; Macro; 1.
DR SMART; SM00506; A1pp; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076858}.
FT DOMAIN 31..212
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 329..486
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
SQ SEQUENCE 498 AA; 57553 MW; 4E1879C81B4C0B53 CRC64;
MEVESLARWS ETNATNSSFL RILGLESYHE SAPFKYRPDL NKKIILWEGD ITALSVNALV
HPTNESFTES SQLSQKVIEC AGSKLKEELT TKIKYCRTGE AKITQGFDLP ARYIIHTVGP
KYNARYKTAA ETALYFCYRN VMELVHEYHL SSVAIPIIYT VKRGYPPDEG AHLALRTIRR
FLEQYGDSIE SVILVLDANN YGIYQVLSPL YFPRSVQEAE FSRYQLPFEI GDPVNGEPII
SDRRIRIIDN PQHAFQDSWE EPQDLSAKFG CSVSVGEHSF AQMEDDVDRQ KLLGQPSHQR
VGQPVTDIDH LTLQVQHHER YERLLRRAKT EDLSEVSGIG CLYQSGTDKF GRPVVVFIGK
WFNFNEINLD KALLYLISLL DPLVKGDYII LYFHTLTEGH NHPSMTWMRE VYNVLEYRHK
KNLKGFYIIH PTFWTKVMTW WFLTFMAPAI KHKVHSVPGV EYLYNIINMD QLEIPAFITE
YDMTVNGVRY VEQPSSDE
//