ID G3RU21_GORGO Unreviewed; 828 AA.
AC G3RU21;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=SH3-containing GRB2-like protein 3-interacting protein 1 {ECO:0000256|ARBA:ARBA00014150};
DE AltName: Full=Endophilin-3-interacting protein {ECO:0000256|ARBA:ARBA00030485};
GN Name=SGIP1 {ECO:0000313|Ensembl:ENSGGOP00000019298.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000019298.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000019298.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000019298.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000019298.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00003346}.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000256|ARBA:ARBA00004283}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004283}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004283}.
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DR EMBL; CABD030003727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030003728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030003729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030003730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030003731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030003732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030003733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030003734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_018874943.1; XM_019019398.1.
DR RefSeq; XP_018874947.1; XM_019019402.1.
DR AlphaFoldDB; G3RU21; -.
DR Ensembl; ENSGGOT00000031458.2; ENSGGOP00000019298.2; ENSGGOG00000022052.2.
DR GeneID; 101141674; -.
DR KEGG; ggo:101141674; -.
DR CTD; 84251; -.
DR eggNOG; KOG2398; Eukaryota.
DR GeneTree; ENSGT00940000156301; -.
DR OrthoDB; 2996449at2759; -.
DR TreeFam; TF328986; -.
DR Proteomes; UP000001519; Chromosome 1.
DR Bgee; ENSGGOG00000022052; Expressed in prefrontal cortex and 5 other cell types or tissues.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
DR CDD; cd09266; SGIP1_MHD; 1.
DR Gene3D; 2.60.40.1170; Mu homology domain, subdomain B; 2.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR InterPro; IPR037984; SGIP1_MHD.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF9; PROLINE-SERINE-THREONINE PHOSPHATASE-INTERACTING PROTEIN 2; 1.
DR Pfam; PF10291; muHD; 1.
DR SUPFAM; SSF49447; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 1.
DR PROSITE; PS51072; MHD; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT DOMAIN 559..827
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..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 313..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 226..240
FT /note="Polar 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 340..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..473
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 89067 MW; 84B078183B23DBFE CRC64;
MMEGLKKRTR KAFGIRKKEK DTDSTGSPDR DGIQPSPHEP PYNSKAECAR EGGKKVSKKS
NGAPNGFYAE IDWERYNSPE LDEEGYSIRP EEPGSTKGKH FYSSSESEEE EESHKKFNIK
IKPLQSKDIL KNAATVDELK ASIGNIALSP SPVRKSPRRS PGAIKRNLSS EEVARPRRST
PTPELISKKP ADDTTALAPL FGPPLESAFD EQKTEVLLDQ PEIWGSGQPI NPSMESPKLT
RPFPTGTPPP LPPKNVPATP PRTGSPLTIG PGNDQSATEV KIEKLPSIND LDSIFGPVLS
PKSVAVNAEE KWVHFSDTSP EHVTPELTPR EKVVSPPATP DNPADSPAPG PLGPPGPTGP
PGPPGPPRNV PSPLNLEEVQ KKVAEQTFIK DDYLETISSP KDFGLGQRAT PPPPPPPTYR
TVVSSPGPGS GPGPGTTSGA SSPARPATPL VPCRSTTPPP PPPRPPSRPK LPPGKPGVGD
VSRPFSPPIH SSSPPPIAPL ARAESTSSIS STNSLSAATT PTVENEQPSL VWFDRGKFYL
TFEGSSRGPS PLTMGAQDTL PVAAAFTETV NAYFKGADPS KCIVKITGEM VLSFPAGITR
HFANNPSPAA LTFRVINFSR LEHVLPNPQL LCCDNTQNDA NTKEFWVNMP NLMTHLKKVS
EQKPQATYYN VDMLKYQVSA QGIQSTPLNL AVNWRCEPSS TDLRIDYKYN TDAMTTAVAL
NNVQFLVPID GGVTKLQAVL PPAVWNAEQQ RILWKIPDIS QKSENGGVGS LLARFQLSEG
PSKPSPLVVQ FTSEGSTLSG CDIELVGAGY RFSLIKKRFA AGKYLADN
//
