SGIP1_PSAOB
ID SGIP1_PSAOB Reviewed; 827 AA.
AC Q6IZA3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 02-JUN-2021, entry version 55.
DE RecName: Full=SH3-containing GRB2-like protein 3-interacting protein 1;
DE AltName: Full=Endophilin-3-interacting protein;
GN Name=SGIP1;
OS Psammomys obesus (Fat sand rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Gerbillinae; Psammomys.
OX NCBI_TaxID=48139;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH SH3GL3.
RC TISSUE=Hypothalamus;
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).
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 (PubMed:15919751). Interacts
CC with 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:0000269|PubMed:15919751, 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. Also detected at
CC lower levels in spleen and adipose tissue.
CC {ECO:0000269|PubMed:15919751}.
CC -!- MISCELLANEOUS: Brain-specific depletion by RNAi leads to body weight
CC reduction due to reduction of food intake without concomitant reduction
CC in metabolic rate.
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DR EMBL; AY611625; AAT37968.1; -; mRNA.
DR GO; GO:0030122; C:AP-2 adaptor complex; ISS:UniProtKB.
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:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
DR GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
DR GO; GO:2000253; P:positive regulation of feeding behavior; IMP:UniProtKB.
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:UniProtKB.
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.
FT CHAIN 1..827
FT /note="SH3-containing GRB2-like protein 3-interacting
FT protein 1"
FT /id="PRO_0000248398"
FT DOMAIN 558..826
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..505
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 75..116
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 261..275
FT /note="Polar 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..442
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 MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
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:0000250|UniProtKB:P0DJJ3"
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:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 247
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
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:0000250|UniProtKB:Q8VD37"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 409
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
SQ SEQUENCE 827 AA; 88451 MW; FDE1EFCB07339A60 CRC64;
MMEGLKKRTR KAFGIRKKEK DTDSTGSPDR DGMQPSPHEL PYHSKAECAR EGGNKASKKS
NGAPNGFYAE IDWERYNSPE LDEEGYSIRP EEPGSTKGKH FYSSSESEEE EESHKKFNIK
IKPLQSKDIL KNAATVDELK ASIGNIALSP SPVRKSPRRS PGAIKRNLSS EEVARPRRST
PTPELTSKKP LDDTLALAPL FGPPLESAFD GHKTEVLLDQ PEIWGSGQPV NPSMESPKLA
RPFPTGTPPP LPPKTVPATP PRTGSPLTVA TGNDQAATEA KIEKLPSISD LDSIFGPVLS
PKSVAVNTEE TWVHFSDASP EHVTPELTPR EKVVTPPAAS DIPADSPTPG PPGPPGSAGP
PGPPGPRNVP SPLNLEEVQK KVAEQTFIKD DYLETLSSPK ECGLGQRATP PPPPPPTYRT
VVSSPGPGSG SGTGTASGAS SPARPATPLV PCSCSTPPPP PPRPPSRPKL PPGKPGVGDV
SRPFSPPIHS SSPPPIAPLA RAESTSSISS TNSLSAATTP TVENEQXSLV WFDRGKFYLT
FEGSSRGPSP LTMGAQDTLP VAAAFTETVN AYFKGADPSK CIVKITGEMV LSFPAGITRH
FANNPSPAAL TFRVINSSRL EHVLPNPQLL CCDNTQNDAN TKEFWVNMPN LMTHLKKVSE
QKPQATYYNV DMLKYQVSAQ GIQSTPLNLA VNWRCEPSST DLRIDYKYNT DAMSTAVALN
NVQFLVPIDG GVTKLQAVLP PAVWNAEQQR ILWKIPDISQ KSENGGVGSL LARFQLAEGP
SKPSPLVVQF TSEGSTLSGC DIELVGAGYG FSLIKKRFAA GKYLADN
