ID HIP1R_MOUSE Reviewed; 1068 AA. AC Q9JKY5; Q3UJ14; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 22-FEB-2023, entry version 164. DE RecName: Full=Huntingtin-interacting protein 1-related protein; DE Short=HIP1-related protein; GN Name=Hip1r; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX 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). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP DISRUPTION PHENOTYPE. RX PubMed=17452370; DOI=10.1093/hmg/ddm076; RA Bradley S.V., Hyun T.S., Oravecz-Wilson K.I., Li L., Waldorff E.I., RA Ermilov A.N., Goldstein S.A., Zhang C.X., Drubin D.G., Varela K., RA Parlow A., Dlugosz A.A., Ross T.S.; RT "Degenerative phenotypes caused by the combined deficiency of murine HIP1 RT and HIP1r are rescued by human HIP1."; RL Hum. Mol. Genet. 16:1279-1292(2007). RN [4] RP SUBUNIT, AND INTERACTION WITH F-ACTIN. RX PubMed=18790740; DOI=10.1074/jbc.m802863200; RA Wilbur J.D., Chen C.-Y., Manalo V., Hwang P.K., Fletterick R.J., RA Brodsky F.M.; RT "Actin binding by Hip1 (huntingtin-interacting protein 1) and Hip1R (Hip1- RT related protein) is regulated by clathrin light chain."; RL J. Biol. Chem. 283:32870-32879(2008). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). 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. CC -!- SUBUNIT: Homodimer (PubMed:18790740). Interacts with actin; CC homodimerization promotes actin binding (PubMed:18790740). Interacts CC with CLTB (By similarity). Interacts with HIP1 (By similarity). CC Interacts (via ENTH and I/LWEQ domains) with BCL2L10 (By similarity). CC {ECO:0000250|UniProtKB:O75146, ECO:0000269|PubMed:18790740}. CC -!- INTERACTION: CC Q9JKY5; Q60598: Cttn; NbExp=4; IntAct=EBI-642457, EBI-397955; CC Q9JKY5; G3V6K6: Egfr; Xeno; NbExp=2; IntAct=EBI-642457, EBI-27088566; CC Q9JKY5; Q96B97: SH3KBP1; Xeno; NbExp=3; IntAct=EBI-642457, EBI-346595; CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Endomembrane CC system. Cytoplasmic vesicle, clathrin-coated vesicle membrane. CC Note=Membrane-associated protein, mainly localized at the endocytic CC compartments and in the 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: Binds F-actin via the talin-like I/LWEQ domain. CC -!- DISRUPTION PHENOTYPE: Hip1 and Hip1r double knockout mice are dwarfed, CC afflicted with severe vertebral defects and die in early adulthood. CC {ECO:0000269|PubMed:17452370}. CC -!- SIMILARITY: Belongs to the SLA2 family. {ECO:0000305}. 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; -; mRNA. DR EMBL; AK146663; BAE27341.1; -; mRNA. DR CCDS; CCDS39276.1; -. DR RefSeq; NP_659507.3; NM_145070.3. DR AlphaFoldDB; Q9JKY5; -. DR SMR; Q9JKY5; -. DR BioGRID; 205896; 24. DR IntAct; Q9JKY5; 7. DR MINT; Q9JKY5; -. DR STRING; 10090.ENSMUSP00000000939; -. DR iPTMnet; Q9JKY5; -. DR PhosphoSitePlus; Q9JKY5; -. DR EPD; Q9JKY5; -. DR MaxQB; Q9JKY5; -. DR PaxDb; Q9JKY5; -. DR ProteomicsDB; 269597; -. DR Antibodypedia; 31710; 309 antibodies from 32 providers. DR DNASU; 29816; -. DR Ensembl; ENSMUST00000000939.15; ENSMUSP00000000939.9; ENSMUSG00000000915.16. DR GeneID; 29816; -. DR KEGG; mmu:29816; -. DR UCSC; uc008zos.2; mouse. DR AGR; MGI:1352504; -. DR CTD; 9026; -. DR MGI; MGI:1352504; Hip1r. DR VEuPathDB; HostDB:ENSMUSG00000000915; -. DR eggNOG; KOG0980; Eukaryota. DR GeneTree; ENSGT00940000153594; -. DR HOGENOM; CLU_006034_0_0_1; -. DR InParanoid; Q9JKY5; -. DR OMA; IREYVYF; -. DR OrthoDB; 7775at2759; -. DR PhylomeDB; Q9JKY5; -. DR TreeFam; TF316860; -. DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis. DR BioGRID-ORCS; 29816; 3 hits in 78 CRISPR screens. DR ChiTaRS; Hip1r; mouse. DR PRO; PR:Q9JKY5; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q9JKY5; protein. DR Bgee; ENSMUSG00000000915; Expressed in urinary bladder urothelium and 332 other tissues. DR ExpressionAtlas; Q9JKY5; baseline and differential. DR Genevisible; Q9JKY5; MM. DR GO; GO:0016324; C:apical plasma membrane; IDA:ParkinsonsUK-UCL. DR GO; GO:0005938; C:cell cortex; IDA:ParkinsonsUK-UCL. DR GO; GO:0005905; C:clathrin-coated pit; IDA:ParkinsonsUK-UCL. DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:ParkinsonsUK-UCL. DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005856; C:cytoskeleton; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0032839; C:dendrite cytoplasm; ISS:ParkinsonsUK-UCL. DR GO; GO:0043197; C:dendritic spine; ISS:ParkinsonsUK-UCL. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; IEA:GOC. DR GO; GO:0043025; C:neuronal cell body; ISS:ParkinsonsUK-UCL. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ParkinsonsUK-UCL. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0098794; C:postsynapse; ISO:MGI. DR GO; GO:0014069; C:postsynaptic density; ISS:ParkinsonsUK-UCL. DR GO; GO:0032587; C:ruffle membrane; ISO:MGI. DR GO; GO:0097060; C:synaptic membrane; ISS:ParkinsonsUK-UCL. DR GO; GO:0003779; F:actin binding; IDA:MGI. DR GO; GO:0051015; F:actin filament binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0035615; F:clathrin adaptor activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0030276; F:clathrin binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0032051; F:clathrin light chain binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB. DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI. DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:MGI. DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISO:MGI. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0017124; F:SH3 domain binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central. DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI. DR GO; GO:0048268; P:clathrin coat assembly; IDA:ParkinsonsUK-UCL. DR GO; GO:0055123; P:digestive system development; IMP:ParkinsonsUK-UCL. DR GO; GO:0006897; P:endocytosis; IBA:GO_Central. DR GO; GO:0061024; P:membrane organization; IMP:ParkinsonsUK-UCL. DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:ParkinsonsUK-UCL. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ParkinsonsUK-UCL. DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA:ParkinsonsUK-UCL. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI. DR GO; GO:1905445; P:positive regulation of clathrin coat assembly; IDA:ParkinsonsUK-UCL. DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IC:ParkinsonsUK-UCL. DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:MGI. DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISO:MGI. DR GO; GO:2000588; P:positive regulation of platelet-derived growth factor receptor-beta signaling pathway; ISO:MGI. DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI. DR GO; GO:0099173; P:postsynapse organization; ISO:MGI. DR GO; GO:0050821; P:protein stabilization; ISO:MGI. DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:MGI. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:ParkinsonsUK-UCL. DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; NAS:ParkinsonsUK-UCL. DR GO; GO:0030100; P:regulation of endocytosis; ISO:MGI. DR GO; GO:0060453; P:regulation of gastric acid secretion; IMP:ParkinsonsUK-UCL. 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 1: Evidence at protein level; KW Acetylation; Actin-binding; Coiled coil; Cytoplasm; Cytoplasmic vesicle; KW Endocytosis; Membrane; Reference proteome. FT CHAIN 1..1068 FT /note="Huntingtin-interacting protein 1-related protein" FT /id="PRO_0000083985" FT DOMAIN 23..151 FT /note="ENTH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243" FT DOMAIN 771..1012 FT /note="I/LWEQ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00292" FT REGION 582..610 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 867..924 FT /note="Important for actin binding" FT /evidence="ECO:0000250" FT REGION 1011..1068 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 346..644 FT /evidence="ECO:0000255" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:O75146" FT CONFLICT 746 FT /note="P -> R (in Ref. 1; AAF34662)" FT /evidence="ECO:0000305" SQ SEQUENCE 1068 AA; 119426 MW; 992FD4D3FA3F8A6C 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 DQTVLPRAQP 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 //