ID A0A4W6GBP4_LATCA Unreviewed; 1050 AA.
AC A0A4W6GBP4;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 18-JUN-2025, entry version 23.
DE RecName: Full=Huntingtin-interacting protein 1-related protein {ECO:0000256|ARBA:ARBA00073599};
GN Name=hip1rb {ECO:0000313|Ensembl:ENSLCAP00010060833.1};
OS Lates calcarifer (Barramundi) (Holocentrus calcarifer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangaria incertae sedis; Centropomidae; Lates.
OX NCBI_TaxID=8187 {ECO:0000313|Ensembl:ENSLCAP00010060833.1, ECO:0000313|Proteomes:UP000314980};
RN [1] {ECO:0000313|Proteomes:UP000314980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sai Rama Sridatta P.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLCAP00010060833.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Component of clathrin-coated pits and vesicles, that may link
CC the endocytic machinery to the actin cytoskeleton. Binds 3-
CC phosphoinositides (via ENTH domain). May act through the ENTH domain to
CC promote cell survival by stabilizing receptor tyrosine kinases
CC following ligand-induced endocytosis. {ECO:0000256|ARBA:ARBA00059997}.
CC -!- SUBUNIT: Homodimer. Interacts with actin; homodimerization promotes
CC actin binding. Interacts with CLTB. Interacts with HIP1. Interacts (via
CC ENTH and I/LWEQ domains) with BCL2L10. {ECO:0000256|ARBA:ARBA00061714}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}. Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004156}.
CC -!- SIMILARITY: Belongs to the SLA2 family.
CC {ECO:0000256|ARBA:ARBA00010135}.
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DR AlphaFoldDB; A0A4W6GBP4; -.
DR Ensembl; ENSLCAT00010062482.1; ENSLCAP00010060833.1; ENSLCAG00010028282.1.
DR GeneTree; ENSGT00940000153594; -.
DR Proteomes; UP000314980; Unassembled WGS sequence.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:TreeGrafter.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:TreeGrafter.
DR GO; GO:0051015; F:actin filament binding; IEA:TreeGrafter.
DR GO; GO:0035615; F:clathrin adaptor activity; IEA:TreeGrafter.
DR GO; GO:0032051; F:clathrin light chain binding; IEA:TreeGrafter.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IEA:TreeGrafter.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:TreeGrafter.
DR GO; GO:0007015; P:actin filament organization; IEA:TreeGrafter.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:TreeGrafter.
DR GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR FunFam; 1.20.1410.10:FF:000002; Huntingtin interacting protein 1; 1.
DR FunFam; 1.20.5.1700:FF:000002; Huntingtin interacting protein 1; 1.
DR FunFam; 1.25.40.90:FF:000012; Huntingtin interacting protein 1-related; 1.
DR Gene3D; 1.20.5.1700; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 6.10.250.920; -; 1.
DR Gene3D; 1.20.1410.10; I/LWEQ domain; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR032422; HIP1_clath-bd.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR030224; Sla2_fam.
DR PANTHER; PTHR10407; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR10407:SF10; HUNTINGTIN-INTERACTING PROTEIN 1-RELATED PROTEIN; 1.
DR Pfam; PF07651; ANTH; 1.
DR Pfam; PF16515; HIP1_clath_bdg; 1.
DR Pfam; PF01608; I_LWEQ; 1.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF109885; I/LWEQ domain; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000314980}.
FT DOMAIN 23..151
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT DOMAIN 764..1005
FT /note="I/LWEQ"
FT /evidence="ECO:0000259|PROSITE:PS50945"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 964..1000
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 553..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..581
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 119635 MW; B6FADEE4B8A1863D CRC64;
MNSIRQVPTR VKSRRTEANL GAEREHFDKQ QLSSISKAIN STETPVKEKH ARRIILGTHR
EKGAYTFWSY ALGFPLASSS ILSWKFCHVL HKVLRDGHRN VLQDCMRHHS SLVEVGKLWG
NLHDKYGQLV ALYTRLLCTK LEFHVKHSEI PPNLEVTDEV LERTAGTDIN NVTQQNIWQV
LRGYLTCVLL SLIFPLVLRQ LNTSIAISTL TSGQCRLSPL IQVIQDCSHL YHFTVKLLFK
LHACLPADTL QGHRERFHDQ FHSLKTFFNK ARDMMYFKRL IQIPKLPDSP PNFLHAASLA
KHVKPVVVIP DEDEPEQQDD DDDEPEPLIE QLDIFDQTFG PPNGGFDDRD LQIESLKRDL
ELLRAELDRV KQEAQRYITQ LKSQINSLEA ELEEQRAQKQ RALVENEQLR MELEATRRRN
AEHESLQTTF IEAEKRAQAT EQRYNKLKEK HTELVASHAE LLRKSADTVK MLSVTQQTQE
EVERTKQQLS FEIDRIKQES DMRLEEQKFE MEKLKRELEE KMAEVTHMKA SLQSSETVSM
HLSSMTALQA EKERLMRSVS EKEAELSSLR QSAQVQQSSL QQERERSSRE LGELQGKLQE
KEEQLKQKLL EEQFALLQGT VTEAENIIQD AVAKLDDPLH VRCTSSPDYL ISRAEATLGS
IDKVKKGHAD YLSNMGDAGG LLRALTQFSH LAADTIINGS ATAHMAPTDH ADRLTENCRG
CATQSLQYLK DLKSKTTLQR ADPASIRIIV QKILHLGQDL RPKSMDVRQD ELGDLVDKEM
AATSAAIEEA VRRIDEMMNQ ARKDTTGVKL EVNERILNSC TDLMKAIRML VIASTDLQKE
IVESGRGAAT IKEFYARNSR WTEGLISAAK AVGWGATEMV ESADKVVLHT GKYEELIVCS
HEIAASTAQL VAASKVKADR NSKRLPVLQQ ASRHVNEMAA KVVASTKTGQ EHLEDKDTMD
FSGMSLIKLR KEEMESQVKV LELESQLENE RLRLGELRKK HYDLAGVPPE QKPALAQKPN
IPPKTSVRAK KKGQYYSFRL CEHFLHHRYF
//
