SGIP1_RAT
ID SGIP1_RAT Reviewed; 827 AA.
AC P0DJJ3;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=SH3-containing GRB2-like protein 3-interacting protein 1;
DE AltName: Full=Endophilin-3-interacting protein;
GN Name=Sgip1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
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]
RP FUNCTION IN ENERGY HOMEOSTASIS.
RX PubMed=15919751; DOI=10.1210/en.2005-0282;
RA Trevaskis J., Walder K., Foletta V., Kerr-Bayles L., McMillan J.,
RA Cooper A., Lee S., Bolton K., Prior M., Fahey R., Whitecross K.,
RA Morton G.J., Schwartz M.W., Collier G.R.;
RT "Src homology 3-domain growth factor receptor-bound 2-like (endophilin)
RT interacting protein 1, a novel neuronal protein that regulates energy
RT balance.";
RL Endocrinology 146:3757-3764(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=17626015; DOI=10.1074/jbc.m703815200;
RA Uezu A., Horiuchi A., Kanda K., Kikuchi N., Umeda K., Tsujita K.,
RA Suetsugu S., Araki N., Yamamoto H., Takenawa T., Nakanishi H.;
RT "SGIP1alpha is an endocytic protein that directly interacts with
RT phospholipids and Eps15.";
RL J. Biol. Chem. 282:26481-26489(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-104; SER-105;
RP SER-107; SER-169; SER-236; THR-247; SER-287; SER-300; SER-316; SER-319;
RP THR-324; THR-335; SER-371; SER-398 AND THR-409, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May function in clathrin-mediated endocytosis. Has both a
CC membrane binding/tubulating activity and the ability to recruit
CC proteins essential to the formation of functional clathrin-coated pits.
CC Has a preference for membranes enriched in phosphatidylserine and
CC phosphoinositides and is required for the endocytosis of the
CC transferrin receptor. May also bind tubulin. May play a role in the
CC regulation of energy homeostasis. {ECO:0000269|PubMed:15919751}.
CC -!- SUBUNIT: Interacts with proteins essential or regulating the formation
CC of functional clathrin-coated pits (Probable). Interacts with CANX (By
CC similarity). Interacts with AP2A1 (By similarity). Interacts with EPS15
CC (By similarity). Interacts with SH3GL3 (By similarity). Interacts with
CC AMPH (By similarity). Interacts with ITSN1 (via SH3 domains) (By
CC similarity). Interacts with and REPS1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8VD37, ECO:0000250|UniProtKB:Q9BQI5,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000250|UniProtKB:Q9BQI5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9BQI5}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9BQI5}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain (at protein level).
CC {ECO:0000269|PubMed:17626015}.
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DR EMBL; AABR03040176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03040554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017449253.1; XM_017593764.1.
DR RefSeq; XP_017458523.1; XM_017603034.1.
DR AlphaFoldDB; P0DJJ3; -.
DR SMR; P0DJJ3; -.
DR IntAct; P0DJJ3; 1.
DR MINT; P0DJJ3; -.
DR STRING; 10116.ENSRNOP00000048424; -.
DR iPTMnet; P0DJJ3; -.
DR PaxDb; P0DJJ3; -.
DR PRIDE; P0DJJ3; -.
DR Ensembl; ENSRNOT00000106500; ENSRNOP00000096859; ENSRNOG00000006357.
DR GeneID; 313413; -.
DR CTD; 84251; -.
DR RGD; 1564957; Sgip1.
DR eggNOG; KOG2398; Eukaryota.
DR GeneTree; ENSGT00940000156301; -.
DR InParanoid; P0DJJ3; -.
DR OrthoDB; 638761at2759; -.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P0DJJ3; -.
DR Proteomes; UP000002494; Chromosome 5.
DR GO; GO:0030122; C:AP-2 adaptor complex; ISS:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:RGD.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
DR GO; GO:0015631; F:tubulin binding; IPI:UniProtKB.
DR GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
DR GO; GO:1904000; P:positive regulation of eating behavior; IMP:RGD.
DR GO; GO:2000253; P:positive regulation of feeding behavior; IMP:UniProtKB.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:RGD.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0002021; P:response to dietary excess; IMP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR CDD; cd09266; SGIP1_MHD; 1.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR InterPro; IPR037984; SGIP1_MHD.
DR Pfam; PF10291; muHD; 1.
DR SUPFAM; SSF49447; SSF49447; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW Coated pit; Endocytosis; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..827
FT /note="SH3-containing GRB2-like protein 3-interacting
FT protein 1"
FT /id="PRO_0000418108"
FT DOMAIN 558..826
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..566
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI5"
FT REGION 592..594
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI5"
FT REGION 648..827
FT /note="Necessary and sufficient to mediate interaction with
FT CANX"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT REGION 666..669
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI5"
FT REGION 812..817
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI5"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..472
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 247
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 409
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
SQ SEQUENCE 827 AA; 88585 MW; 6235D2DB926B4ED2 CRC64;
MMEGLKKRTR KAFGIRKKEK DTDSTGSPDR DGMQPSPHEP PYHSKAECAR EGGKKASKKS
NGAPNGFYAE IDWERYNSPE LDEEGYSIRP EEPGSTKGKH FYSSSESEEE EESHKKFNIK
IKPLQSKDVL KNAATVDELK ASIGNIALSP SPVRKSPRRS PGAIKRNLSS EEVARPRRST
PTPELTSKKP LDDTLALAPL FGPPLESAFD EQKTEVLLDQ PEIWGSGQPI NPSMESPKLA
RPFPTGTPPP LPPKAVPATP PRTGSPLTVA TGNDQAATEA KIEKLPSISD LDSIFGPVLS
PKSVAVNTEE KWVHFSDASP EHVTPELTPR EKVVTPPAAS DIPADSPAPG PPGPPGSAGP
PGPPGPRHVP SPLNLEEVQK KVAEQTFIKD DYLETLSSPK ECGLGQRATP PPPPPPTYRT
VVSSPGPGSG SGTGTASGAS SPARPATPLV PCSSTTPPPP PPRPPSRPKL PPGKPGVGDV
SRPFSPPIHS SSPPPIAPLA RAESTSSISS TNSLSAATTP TVENEQPSLV WFDRGKFYLT
FEGSSRGPSP LTMGAQDTLP VAAAFTETVN AYFKGADPSK CIVKITGEMV LSFPAGITRH
FANNPSPAAL TFRVINSSRL EHVLPNPQLL CCDNTQNDAN TKEFWVNMPN LMTHLKKVSE
QKPQATYYNV DMLKYQVSAQ GIQSTPLNLA VNWRCEPGST DLRIDYKYNT DAMTTAVALN
NVQFLVPIDG GVTKLQAVLP PAVWNAEQQR ILWKIPDISQ KSENGGVGSL LARFQLSEGP
SKPSPLVVQF TSEGSTLSGC DIELVGAGYR FSLIKKRFAA GKYLADN
