ID A0A3B3HVX5_ORYLA Unreviewed; 1047 AA.
AC A0A3B3HVX5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 18-JUN-2025, entry version 31.
DE RecName: Full=Huntingtin-interacting protein 1-related protein {ECO:0000256|ARBA:ARBA00073599};
GN Name=hip1 {ECO:0000313|Ensembl:ENSORLP00000035880.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000035880.1, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000035880.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000035880.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000035880.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000035880.1};
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 RefSeq; XP_023817056.1; XM_023961288.1.
DR AlphaFoldDB; A0A3B3HVX5; -.
DR Ensembl; ENSORLT00000032342.1; ENSORLP00000035880.1; ENSORLG00000011517.2.
DR GeneID; 101174446; -.
DR GeneTree; ENSGT00940000153594; -.
DR OrthoDB; 8178130at2759; -.
DR Proteomes; UP000001038; Chromosome 13.
DR Bgee; ENSORLG00000011517; Expressed in heart and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
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:SF14; HUNTINGTIN-INTERACTING PROTEIN 1; 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:UP000001038}.
FT DOMAIN 31..159
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT DOMAIN 792..1033
FT /note="I/LWEQ"
FT /evidence="ECO:0000259|PROSITE:PS50945"
FT REGION 551..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 370..422
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 552..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1047 AA; 117003 MW; DCD30E5FAC4D0FC6 CRC64;
MDRVKSSMQQ VPNAIPKVIR RTGGANSLET ERENFERVQA VSINKAINTQ EVAVKEKHAR
TCILGTHHEK GAHTFWAVVH RLPLSSNAVL CWKFCHVFHK LLRDGHPNVI KDSMRNKADL
TDMSRMWGHL SEGYGKLCSI YLKLLITKIE FHIKNPRFPG NLQMSNRQLD EVGENDVNNF
FQLTVEMFDY LECELNLFLA VFSSLDMSRS VSVTAAGQCR LAPLIQVILD CSHLYDYTVK
LLFKLHSCLP ADTLQGHRDR FQEQFKKLKS LFYRSSNLQY FKRLIQIPQL PENPPNFLRA
SALSEHISPV VVIPAESSSP ESEHVVETDD LVDTDIPVLP APAETKFDDL FGTSAAIDPF
NFTSQNGMRK DDKDRLIEQL TREIQALKEE LESFRLESGR LCQALRGRVS ELEAELAEQS
HLRMQAVGES EFLKAELDDV RRVREYTEKE QRSLTEIEKK AQANEQRYTK LKEKYTELVQ
SHADLLRKNA EVTRQMTVAR AAQDEVEVLK KEMQEKVKAV QDVADRQERE QQRQLEDIQK
ELVCTREELD TLKSSVTSSQ QSREALSSQM AALESEKAEL VQSMSKVEAE LEAQRQELQR
AQSSLATERE SGVKAAEALQ NQLNEKESRE QALESQLVAA RWSSLRGAVE EAEKIVQDSL
SQIDDPAHIS CTSSADYLAS RCQASLDSLD HLNSSIKTFM DDNSAVLELV RAVTRSGHLV
GETIVQGSAT SHMVPVEKSD ALLETVKTCG AEVLLMLGQM KQQDHLAAAD STKLRVALEA
ILATAEKLRP RGLELQQGEL GDLVEQEMAA TSAAVESAAS RIEEMLNKSR AVDTGVKMEV
NERILASCTE LMEAIKALVL SSKDLQRDIV ESGRGAASMK EFYAKNSRWT EGLISASKAV
GWGATVLVDA ADLVVQGKGK FEELMVCSHE IAASTAQLVA ASKVKADKDS TNLQRLQRAS
RGVTQATAVV VASTKSGKSQ IEDTETMDFS SMTLTQIKRQ EMDAQVLVLE LETRLQKERE
RLGELRKKHY ELAGVAEGWG GDDEGTG
//
