GenomeNet

Database: UniProt
Entry: F7E260_MONDO
LinkDB: F7E260_MONDO
Original site: F7E260_MONDO 
ID   F7E260_MONDO            Unreviewed;       981 AA.
AC   F7E260;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Huntingtin interacting protein 1 related {ECO:0000313|Ensembl:ENSMODP00000015462.3};
GN   Name=HIP1R {ECO:0000313|Ensembl:ENSMODP00000015462.3};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000015462.3, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000015462.3, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000015462.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the SLA2 family.
CC       {ECO:0000256|ARBA:ARBA00010135}.
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DR   AlphaFoldDB; F7E260; -.
DR   STRING; 13616.ENSMODP00000015462; -.
DR   Ensembl; ENSMODT00000015748.4; ENSMODP00000015462.3; ENSMODG00000012341.4.
DR   eggNOG; KOG0980; Eukaryota.
DR   GeneTree; ENSGT00940000153594; -.
DR   HOGENOM; CLU_006034_0_0_1; -.
DR   InParanoid; F7E260; -.
DR   OMA; PPTNNGF; -.
DR   TreeFam; TF316860; -.
DR   Proteomes; UP000002280; Chromosome 3.
DR   Bgee; ENSMODG00000012341; Expressed in cerebellum and 18 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR   GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate 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:0005546; F:phosphatidylinositol-4,5-bisphosphate 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:0017124; F:SH3 domain binding; IEA:Ensembl.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR   GO; GO:0055123; P:digestive system development; IEA:Ensembl.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:1905445; P:positive regulation of clathrin coat assembly; IEA:Ensembl.
DR   GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:2000588; P:positive regulation of platelet-derived growth factor receptor-beta signaling pathway; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR   GO; GO:0030100; P:regulation of endocytosis; IEA:Ensembl.
DR   GO; GO:0060453; P:regulation of gastric acid secretion; IEA:Ensembl.
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; 2.
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; 2.
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   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280}.
FT   DOMAIN          38..209
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
FT   DOMAIN          699..924
FT                   /note="I/LWEQ"
FT                   /evidence="ECO:0000259|PROSITE:PS50945"
FT   REGION          930..981
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          277..462
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          491..543
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          883..919
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   981 AA;  109541 MW;  BE54DCC4F793078A CRC64;
     LARGGRAVPG GDGGRMNTIK NVPARVLSRR PGHSLEAERE QFDKTQAISI SKAINTQEAP
     VKEKHARRII LGTHHEKGAF TFWSYAIGLP LPSSSILSWK FCHVLHKVLR DGHPNVLHDC
     QRYRSNIREI GDLWVSVENQ ACSFLAPFLS ALHRLLRWPL IHSSCPPGLP ADTLQGHRDR
     FHEQFHSLRN FFRRASDMLY FKRLIQIPRL PEGPPNFLRA SALAEHIKPV VVIPDEAPED
     EEPENLIEIS SGPPAGEPPV VADLFEQTFG PPNGTVKDDR DLQIENLKRE VEMLRAELDK
     IKLEAQRYIT QLKGQVNGLE AELEEQRKQK QKALVDNEQL RDELEQLRKA RLEQEKAQGL
     YQEAEKKASA TEARYNKLKE KHSELINTHA ELLRKNADTA KQLTVTQQSQ EEVARVKEQL
     AFQMEQVKRE SEMKLEDQSY QLEKLKRELE AKAGELVRVQ ETLSHKEQSG SELSSKLDAM
     HLEKESLSST MRQRESELQS AQSLVEEKEA ALIREQERSS REIGELQGKL AEKDAQHQGL
     QQRLLDEQLS VLQAAVTEAE NTVKDAVSKL DDPLHLRCTS SPDYLVSRAQ AALDALSALE
     KGHRKYVASM TDSSALVAAL AQFSHLAADT IVNGSATSHL APTDHADRLT DTCRDCGARS
     LEYLGLLKDR QSLDQADPSL MRGPLQGILQ LGQELKPKSL DVRQEELGDL VDKEMAATSA
     AIENAVQRIE DMMNQARHES SGVKLEVNER WGPPALSVSS LALHQGAATQ QEFYAKNSRW
     TEGLISASKA VGWGATQLVE SADKVVLHTG KYEELIVCSH EIAASTAQLV AASKVKADKN
     SRNLSRLQEC SRAVNEMAAN VVASTKSGQE QIEDRDTMDF SGMSLIKLKK EEMETQVKVL
     ELEKTLENER RRLGELRKRH YALAGVIDDG AEDEPLGRPV ASPRKGILKK PPLAQKPSVG
     PKPDCQLEKE DGISQAQLMN S
//
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