ID HIP1R_MOUSE STANDARD; PRT; 1068 AA. AC Q9JKY5; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 01-MAY-2005 (Rel. 47, Last annotation update) DE Huntingtin interacting protein 1 related (Hip1-related). GN Name=Hip1r; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain; RX MEDLINE=20082888; PubMed=10613908; DOI=10.1083/jcb.147.7.1503; RA Engqvist-Goldstein A.E.Y., Kessels M.M., Chopra V.S., Hayden M.R., RA Drubin D.G.; RT "An actin-binding protein of the Sla2/Huntingtin interacting protein 1 RT family is a novel component of clathrin-coated pits and vesicles."; RL J. Cell Biol. 147:1503-1518(1999). CC -!- FUNCTION: Component of clathrin-coated pits and vesicles, that may CC link the endocytic machinery to the actin cytoskeleton. CC -!- SUBUNIT: Interacts with actin and huntingtin interacting protein 1 CC (HIP1). Does not interact with huntingtin (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated protein, CC mainly localized at the endocytic compartments and in the CC perinuclear region. CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at lower levels in CC skeletal muscle and heart. The level of expression does not change CC appreciably during development. CC -!- DOMAIN: The talin-like domain binds F-actin. CC -!- SIMILARITY: Belongs to the SLA2 family. CC -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain. CC -!- SIMILARITY: Contains 1 I/LWEQ domain. 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 EMBL; AF221713; AAF34662.1; -. DR SMR; Q9JKY5; 773-966. DR Ensembl; ENSMUSG00000000915; Mus musculus. DR MGI; MGI:1352504; Hip1r. DR GO; GO:0005905; C:coated pit; IDA. DR GO; GO:0005856; C:cytoskeleton; IDA. DR GO; GO:0003779; F:actin binding; IDA. DR GO; GO:0006898; P:receptor mediated endocytosis; IDA. DR InterPro; IPR002558; ILWEQ. DR InterPro; IPR008943; PI_bind_N. DR Pfam; PF01417; ENTH; 1. DR Pfam; PF01608; I_LWEQ; 1. DR ProDom; PD011820; ILWEQ; 1. DR PROSITE; PS50942; ENTH; 1. DR PROSITE; PS50945; I_LWEQ; 1. KW Actin-binding; Coiled coil. FT DOMAIN 23 151 ENTH. FT DOMAIN 311 316 Poly-Glu. FT DOMAIN 346 644 Coiled coil (Potential). FT DOMAIN 818 1012 I/LWEQ. SQ SEQUENCE 1068 AA; 119485 MW; 97CEE9D92CDF5DB1 CRC64; MNSIKNVPAR VLSRRPGHSL EAEREQFDKT QAISISKAIN SQEAPVKEKH ARRIILGTHH EKGAFTFWSY AIGLPLSSSS ILSWKFCHVL HKVLRDGHPN VLHDYQRYRS NIREIGDLWG HLRDQYGHLV NIYTKLLLTK ISFHLKHPQF PAGLEVTDEV LEKAAGTDVN NIFQLTVEMF DYMDCELKLS ESVFRQLNTA IAVSQMSSGQ CRLAPLIQVI QDCSHLYHYT VKLMFKLHSC LPADTLQGHR DRFHEQFHSL KNFFRRASDM LYFKRLIQIP RLPEGPPNFL RASALAEHIK PVVVIPEEAP EEEEPENLIE ISSAPPAGEP VVVADLFDQT FGPPNGSMKD DRDLQIENLK REVETLRAEL EKIKMEAQRY ISQLKGQVNG LEAELEEQRK QKQKALVDNE QLRHELAQLK ALQLEGARNQ GLREEAERKA SATEARYSKL KEKHSELINT HAELLRKNAD TAKQLTVTQQ SQEEVARVKE QLAFQMEQAK RESEMKMEEQ SDQLEKLKRE LAARAGELAR AQEALSRTEQ SGSELSSRLD TLNAEKEALS GVVRQREAEL LAAQSLVREK EEALSQEQQR SSQEKGELRG QLAEKESQEQ GLRQKLLDEQ LAVLRSAAAE AEAILQDAVS KLDDPLHLRC TSSPDYLVSR AQAALDSVSG LEQGHTQYLA SSEDASALVA ALTRFSHLAA DTIVNGAATS HLAPTDPADR LMDTCRECGA RALELVGQLQ DQTVLRRAQP SLMRAPLQGI LQLGQDLKPK SLDVRQEELG AMVDKEMAAT SAAIEDAVRR IEDMMSQARH ESSGVKLEVN ERILNSCTDL MKAIRLLVMT STSLQKEIVE SGRGAATQQE FYAKNSRWTE GLISASKAVG WGATQLVESA DKVVLHMGKY EELIVCSHEI AASTAQLVAA SKVKANKNSP HLSRLQECSR TVNERAANVV ASTKSGQEQI EDRDTMDFSG LSLIKLKKQE METQVRVLEL EKTLEAERVR LGELRKQHYV LAGGMGTPSE EEPSRPSPAP RSGATKKPPL AQKPSIAPRT DNQLDKKDGV YPAQLVNY //