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 13-NOV-2019, entry version 148. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT HIP1 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 RT (Hip1-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, RC Pancreas, 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 RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Component of clathrin-coated pits and vesicles, that may CC link the endocytic machinery to the actin cytoskeleton. Binds 3- CC phosphoinositides (via ENTH domain). May act through the ENTH CC domain to promote cell survival by stabilizing receptor tyrosine CC kinases following ligand-induced endocytosis. CC -!- SUBUNIT: Interacts with actin. Does not interact with huntingtin CC (By similarity). Interacts with CLTB and HIP1. Homodimer. CC Homodimerization promotes actin binding. {ECO:0000250, CC ECO:0000269|PubMed:18790740}. CC -!- INTERACTION: CC Q60598:Cttn; NbExp=4; IntAct=EBI-642457, EBI-397955; CC 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 CC endocytic 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 CC dwarfed, afflicted with severe vertebral defects and die in early CC adulthood. {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 SMR; Q9JKY5; -. DR BioGrid; 205896; 13. DR IntAct; Q9JKY5; 8. DR MINT; Q9JKY5; -. DR STRING; 10090.ENSMUSP00000000939; -. DR iPTMnet; Q9JKY5; -. DR PhosphoSitePlus; Q9JKY5; -. DR EPD; Q9JKY5; -. DR MaxQB; Q9JKY5; -. DR PaxDb; Q9JKY5; -. DR PRIDE; Q9JKY5; -. DR Ensembl; ENSMUST00000000939; ENSMUSP00000000939; ENSMUSG00000000915. DR GeneID; 29816; -. DR KEGG; mmu:29816; -. DR UCSC; uc008zos.2; mouse. DR CTD; 9026; -. DR MGI; MGI:1352504; Hip1r. DR eggNOG; KOG0980; Eukaryota. DR eggNOG; ENOG410XRXQ; LUCA. DR GeneTree; ENSGT00940000153594; -. DR InParanoid; Q9JKY5; -. DR KO; K20040; -. DR OMA; KRKHVRS; -. DR OrthoDB; 104219at2759; -. DR TreeFam; TF316860; -. DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis. DR ChiTaRS; Hip1r; mouse. DR PRO; PR:Q9JKY5; -. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; ENSMUSG00000000915; Expressed in 340 organ(s), highest expression level in submandibular gland. DR ExpressionAtlas; Q9JKY5; baseline and differential. DR Genevisible; Q9JKY5; MM. DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central. 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: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: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:0006915; P:apoptotic process; IEA:InterPro. 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: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:0048260; P:positive regulation of receptor-mediated endocytosis; IBA:GO_Central. 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; 1.25.40.90; -; 1. DR InterPro; IPR011417; ANTH_dom. DR InterPro; IPR013809; ENTH. DR InterPro; IPR008942; ENTH_VHS. DR InterPro; IPR032422; HIP1_clath-bd. DR InterPro; IPR030555; HIP1R. DR InterPro; IPR035964; I/LWEQ_dom_sf. DR InterPro; IPR002558; ILWEQ_dom. DR InterPro; IPR030224; Sla2_fam. DR PANTHER; PTHR10407; PTHR10407; 1. DR PANTHER; PTHR10407:SF10; PTHR10407:SF10; 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; SSF109885; SSF109885; 1. DR SUPFAM; SSF48464; SSF48464; 1. DR PROSITE; PS50942; ENTH; 1. DR PROSITE; PS50945; I_LWEQ; 1. PE 1: Evidence at protein level; KW Acetylation; Actin-binding; Coiled coil; Complete proteome; Cytoplasm; KW Cytoplasmic vesicle; Endocytosis; Membrane; Reference proteome. FT CHAIN 1 1068 Huntingtin-interacting protein 1-related FT protein. FT /FTId=PRO_0000083985. FT DOMAIN 23 151 ENTH. {ECO:0000255|PROSITE- FT ProRule:PRU00243}. FT DOMAIN 771 1012 I/LWEQ. {ECO:0000255|PROSITE- FT ProRule:PRU00292}. FT REGION 867 924 Important for actin binding. FT {ECO:0000250}. FT COILED 346 644 {ECO:0000255}. FT COMPBIAS 311 316 Poly-Glu. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000250|UniProtKB:O75146}. FT CONFLICT 746 746 P -> R (in Ref. 1; AAF34662). FT {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 //