ID F1MWF0_BOVIN Unreviewed; 1038 AA. AC F1MWF0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 3. DT 02-SEP-2026, entry version 95. DE RecName: Full=Huntingtin-interacting protein 1 {ECO:0000256|ARBA:ARBA00073538}; DE AltName: Full=Huntingtin-interacting protein I {ECO:0000256|ARBA:ARBA00080332}; GN Name=HIP1 {ECO:0000313|Ensembl:ENSBTAP00000001039.6, GN ECO:0000313|VGNC:VGNC:29857}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000001039.6, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000001039.6} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000001039.6}; RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A., RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C., RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.; RT "ARS-UCD1.2."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSBTAP00000001039.6} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000001039.6}; RG Ensembl; RL Submitted (JAN-2026) to UniProtKB. CC -!- FUNCTION: Plays a role in clathrin-mediated endocytosis and CC trafficking. Involved in regulating AMPA receptor trafficking in the CC central nervous system in an NMDA-dependent manner. Regulates CC presynaptic nerve terminal activity. Enhances androgen receptor (AR)- CC mediated transcription. May act as a proapoptotic protein that induces CC cell death by acting through the intrinsic apoptosis pathway. 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. May play a functional role in the CC cell filament networks. May be required for differentiation, CC proliferation, and/or survival of somatic and germline progenitors. CC {ECO:0000256|ARBA:ARBA00055592}. CC -!- SUBUNIT: Homodimer. Binds actin. Binds HTT (via N-terminus). This CC interaction is restricted to the brain. Binds to IFT57. In normal CC conditions, it poorly interacts with IFT57, HIP1 being strongly CC associated with HTT. However, in mutant HTT proteins with a long poly- CC Gln region, interaction between HTT and HIP1 is inhibited, promoting CC the interaction between HIP1 and IFT57. Interacts with CLTB (via N- CC terminus). Interacts (via coiled coil domain) with AR. Interacts with CC AP2A1, AP2A2, CLTC and HIP1R. Interacts with GRIA1, GRIN2A and GRIN2B. CC {ECO:0000256|ARBA:ARBA00062629}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane CC {ECO:0000256|ARBA:ARBA00004156}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the SLA2 family. CC {ECO:0000256|ARBA:ARBA00010135}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; F1MWF0; -. DR FunCoup; F1MWF0; 1839. DR STRING; 9913.ENSBTAP00000001039; -. DR PaxDb; 9913-ENSBTAP00000001039; -. DR Ensembl; ENSBTAT00000001039.7; ENSBTAP00000001039.6; ENSBTAG00000000781.8. DR VEuPathDB; HostDB:ENSBTAG00000000781; -. DR VGNC; VGNC:29857; HIP1. DR eggNOG; KOG0980; Eukaryota. DR GeneTree; ENSGT00940000153594; -. DR HOGENOM; CLU_006034_0_0_1; -. DR InParanoid; F1MWF0; -. DR OrthoDB; 8178130at2759; -. DR Reactome; R-BTA-8856828; Clathrin-mediated endocytosis. DR Proteomes; UP000009136; Chromosome 25. DR Bgee; ENSBTAG00000000781; Expressed in prefrontal cortex and 110 other cell types or tissues. DR ExpressionAtlas; F1MWF0; baseline. DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central. DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0098793; C:presynapse; IBA:GO_Central. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0035612; F:AP-2 adaptor complex binding; IEA:Ensembl. DR GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central. DR GO; GO:0035615; F:clathrin-cargo adaptor activity; IBA:GO_Central. DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:Ensembl. DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IBA:GO_Central. DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Ensembl. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl. DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl. DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central. DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central. DR GO; GO:0006897; P:endocytosis; IBA:GO_Central. DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IBA:GO_Central. DR GO; GO:2000588; P:positive regulation of platelet-derived growth factor receptor-beta signaling pathway; IBA:GO_Central. DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IEA:Ensembl. DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IEA:Ensembl. DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl. DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IEA:Ensembl. DR CDD; cd17013; ANTH_N_HIP1; 1. 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:000022; huntingtin-interacting protein 1 isoform X1; 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; IPR060021; HIP1R_dom. 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; PF27524; HIP1R; 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 Actin-binding {ECO:0000256|ARBA:ARBA00023203}; KW Activator {ECO:0000256|ARBA:ARBA00023159}; KW Apoptosis {ECO:0000256|ARBA:ARBA00022703}; 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 Differentiation {ECO:0000256|ARBA:ARBA00022782}; KW Endocytosis {ECO:0000256|ARBA:ARBA00022583}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}. FT DOMAIN 32..160 FT /note="ENTH" FT /evidence="ECO:0000259|PROSITE:PS50942" FT DOMAIN 772..1013 FT /note="I/LWEQ" FT /evidence="ECO:0000259|PROSITE:PS50945" FT REGION 1017..1038 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 378..556 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 592..645 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 979..1008 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 1038 AA; 116622 MW; CEB8CD32E0B30CB9 CRC64; MDRMASSMKQ VPNPLPKVLS RRGVGAGMEA AERESFERTQ TVSINKAINT QVVAVKEKHA RTCILGTHHE KGAQTFWSVV NRLPLSSNAV LCWKFCHVFH KLLRDGHPNV LKDSLRYKSE LSDMSRMWGH LSEGYGQLCS IYLKLLRTKM EYHTKNPRFP GNLHMSDRQL EEAGESDVNN FFQLTVEMFD YLECELNLFQ TVFNSLDMSR SVSVTTAGQC RLAPLIQVIL DCSHLYDYAV KLLFKLHSCL PADTLQGHRD RFLEQFTKLK DFFYRSSNLQ YFKRLIQIPQ LPENPPNFLR ASALSEHVSP VVVIPAEASS PDSEPVLEKD DLMGMDASQQ QNSFDSKFDD IFGSSSSSDP FNFNSQNGVN KDEKDQLIDQ LFGETRELKA QLENMKTESQ RAVLQLKGRT SELEAELAEQ QHLRQQAADE SEFLRAELDE LKKKREDTEK AQRSLTEIER KAQANEQRYS KLKEKYNELV QNHAALLRKN AEVTKQVSVA RQAQVDLERE KKELEDSFQR ISDQAQRKTQ EQTEVLENLK QELATSKQEL QIVQGSLENS AQSEAKWTAQ ITDLEKDRDS LMSAMACREE ELSALREQLE YTQLKLSSAQ ESICRLEKDQ HKMLLAEARR AAEQVVQEAL RLFEEPTLSS CAGSADHLLS KVNSTSSCIE QLEKCWSQYL ACPEDISGLL HSVTLLAHLT SDTIVHGSAT CLRAPPESAD SLIDACKQYG KETLTYLSFL EEERIFENAD STAMRSCLTR ITAISEDLLP RGLDIKQEEL GDLVDKEMAA TSAAIEAATA RIEEMLSKSR AGDTGVKLEV NERILGSCTS LMQAIQILVL ASKELQREIV ESGRGTASPK EFYAKNSRWT EGLISAAKAV GWGATVLVDA ADMVVQGRGK FEELMVCSRE IAASTAQLVA ASKVKADKNS PNLAQLLQAS RAVNQATAEV VASTISGKSQ IEDTDSMDFS SITLTQIKRQ EMDSQVRVLE LENELQKERQ KLGELRKKHY ELAGVAEGWE EGTEAPPSTL QEAKTEKE //