GenomeNet

Database: UniProt
Entry: G3V8Y8_RAT
LinkDB: G3V8Y8_RAT
Original site: G3V8Y8_RAT 
ID   G3V8Y8_RAT              Unreviewed;      1038 AA.
AC   G3V8Y8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Huntingtin interacting protein 1 {ECO:0000313|Ensembl:ENSRNOP00000031153.5};
GN   Name=Hip1 {ECO:0000313|Ensembl:ENSRNOP00000031153.5,
GN   ECO:0000313|RGD:620305};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000031153.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000031153.5, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000031153.5,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000031153.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000031153.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the SLA2 family.
CC       {ECO:0000256|ARBA:ARBA00010135}.
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DR   RefSeq; XP_006249160.1; XM_006249098.3.
DR   AlphaFoldDB; G3V8Y8; -.
DR   STRING; 10116.ENSRNOP00000031153; -.
DR   iPTMnet; G3V8Y8; -.
DR   PhosphoSitePlus; G3V8Y8; -.
DR   PaxDb; 10116-ENSRNOP00000031153; -.
DR   Ensembl; ENSRNOT00000030497.5; ENSRNOP00000031153.5; ENSRNOG00000001448.6.
DR   AGR; RGD:620305; -.
DR   CTD; 3092; -.
DR   RGD; 620305; Hip1.
DR   VEuPathDB; HostDB:ENSRNOG00000001448; -.
DR   eggNOG; KOG0980; Eukaryota.
DR   GeneTree; ENSGT00940000153594; -.
DR   HOGENOM; CLU_006034_0_0_1; -.
DR   InParanoid; G3V8Y8; -.
DR   OMA; SSCTEQL; -.
DR   OrthoDB; 7775at2759; -.
DR   TreeFam; TF316860; -.
DR   Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000001448; Expressed in lung and 19 other cell types or tissues.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:BHF-UCL.
DR   GO; GO:0098793; C:presynapse; IDA:SynGO.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:BHF-UCL.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR   GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR   GO; GO:0035612; F:AP-2 adaptor complex binding; ISO:RGD.
DR   GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR   GO; GO:0030276; F:clathrin binding; IDA:RGD.
DR   GO; GO:0032051; F:clathrin light chain binding; ISO:RGD.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISO:RGD.
DR   GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:RGD.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISO:RGD.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:RGD.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR   GO; GO:0097190; P:apoptotic signaling pathway; ISO:RGD.
DR   GO; GO:0048268; P:clathrin coat assembly; IDA:RGD.
DR   GO; GO:0006897; P:endocytosis; ISO:RGD.
DR   GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:RGD.
DR   GO; GO:2000588; P:positive regulation of platelet-derived growth factor receptor-beta signaling pathway; ISO:RGD.
DR   GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:RGD.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:RGD.
DR   CDD; cd17013; ANTH_N_HIP1; 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; 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; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
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          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1016..1038
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          377..488
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          521..555
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          979..1008
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1038 AA;  115961 MW;  9762BC6DB8168358 CRC64;
     MDRMASSMKQ VPNPLPKVLS RRGVGAGMEA AERESFERTQ TVSVNKAINT QEVAVKEKHA
     RTCILGTHHE KGAQTFWSVV NRLPLSSNAM LCWKFCHVFH KLLRDGHPNV LKDSLRYKNE
     LSDMSRMWGH LSEGYGQLCS IYLKLLRTRM EYHTKNPRFP GNLQMSDRQL DEAGESDVNN
     FFQLTVEMFD YLECELNLFQ TVFNSLDMSR SVSVTTAGQC RLAPLIQVIL DCSHLYDYTV
     KLLFKLHSCL PADTLQGHRD RFMEQFTKLK DLFQRSSNLQ YFKRLIQIPQ LPENPPNFLR
     ASALSEHISP VVVIPAEVSS PDSEPVLEKD DLMDMDASQQ SLFDNKFDDI FGSSLSSDPF
     NFNNQNGVNK DEKDHLIERL YREISGLTGQ LDNVKIESQR AMLQLKGRVS ELEAELAEQQ
     HLGRQATDDC EFLRTELDEL KRQREDTEKA QRSLTEIEKK AQANEQRYSK LKEKYSELVQ
     NHADLLRKNA EVTKQVSVAR QAQVDLEREK KELADSFARV SEQTQRKTQE QQDVLETLKH
     ELATSRQELQ VLHGNLETSA QSEAKWLTQI AELEKEQGSL ATAAAQREEE FSALRDQLES
     TQLKLAGAQD SMCQQIKDQR RILLAGARKA AELEIQEALG QLEEPALLIS CAGATDHLLS
     KVNSVSSCLE QLEKSRSQYL ACPEEISELL HSITLLGHLT SDTIIQGTAT SLRAPPESAD
     SLTEACRQYG RETLAYLSSL EEEGAMEKAD TTAIANCLGK IKTIGEELLP RGLDIKQEEL
     GDLVDKEMAA TSAAIEAATT RIEEILSKSR AGDTGVKLEV NERILGSCTS LMQAIKVLVV
     ASKDLQKEIV ESGRGTASPK EFYAKNSRWT EGLISASKAV GWGATIMVDA ADLVVQGKGK
     FEELMVCSHE IAASTAQLVA ASKVKANKGS LNLTQLQQAS RGVNQATAAV VASTISGKSQ
     IEETDSMDFS SMTLTQIKRQ EMDSQVRVLE LENDLQKERQ KLGELRKKHY ELAGVAEGWE
     EGTEASPSAV QEAVPDKE
//
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