GULP1_MOUSE
ID GULP1_MOUSE Reviewed; 304 AA.
AC Q8K2A1; Q9CRV4; Q9CYD2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=PTB domain-containing engulfment adapter protein 1;
DE AltName: Full=Cell death protein 6 homolog;
DE AltName: Full=PTB domain adapter protein CED-6;
DE AltName: Full=Protein GULP;
GN Name=Gulp1; Synonyms=Ced6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 3-304 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH LRP1.
RX PubMed=11729193; DOI=10.1074/jbc.m109336200;
RA Su H.P., Nakada-Tsukui K., Tosello-Trampont A.-C., Li Y., Bu G.,
RA Henson P.M., Ravichandran K.S.;
RT "Interaction of CED-6/GULP, an adapter protein involved in engulfment of
RT apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-
RT related protein (LRP).";
RL J. Biol. Chem. 277:11772-11779(2002).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17007823; DOI=10.1016/j.brainres.2006.08.064;
RA Martins-Silva C., Ferreira L.T., Cyr M., Koenen J., Fernandes D.R.,
RA Carvalho N.R., Ribeiro C.B., Marion S., Chavez-Olortegui C., Prado M.A.,
RA Prado V.F.;
RT "A rat homologue of CED-6 is expressed in neurons and interacts with
RT clathrin.";
RL Brain Res. 1119:1-12(2006).
RN [5]
RP FUNCTION, INTERACTION WITH ARF6 AND ACAP1, AND IDENTIFICATION IN A COMPLEX
RP WITH ACAP1 AND ARF6.
RX PubMed=17398097; DOI=10.1016/j.cub.2007.03.014;
RA Ma Z., Nie Z., Luo R., Casanova J.E., Ravichandran K.S.;
RT "Regulation of Arf6 and ACAP1 signaling by the PTB-domain-containing
RT adaptor protein GULP.";
RL Curr. Biol. 17:722-727(2007).
RN [6]
RP INTERACTION WITH STAB2.
RX PubMed=18230608; DOI=10.1074/jbc.m709105200;
RA Park S.Y., Kang K.B., Thapa N., Kim S.Y., Lee S.J., Kim I.S.;
RT "Requirement of adaptor protein GULP during stabilin-2-mediated cell corpse
RT engulfment.";
RL J. Biol. Chem. 283:10593-10600(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Modulates cellular glycosphingolipid and cholesterol
CC transport. May play a role in the internalization of various LRP1
CC ligands, such as PSAP (By similarity). May function as an adapter
CC protein. Required for efficient phagocytosis of apoptotic cells.
CC Increases cellular levels of GTP-bound ARF6. {ECO:0000250,
CC ECO:0000269|PubMed:17398097}.
CC -!- SUBUNIT: Homodimer. Interacts with clathrin and MEGF10 (By similarity).
CC Interacts with GDP-bound ARF6, but not with GTP-bound ARF6. Part of a
CC complex composed of GULP1, ACAP1 and ARF6. Interacts with ACAP1, LRP1
CC and STAB2. {ECO:0000250, ECO:0000269|PubMed:11729193,
CC ECO:0000269|PubMed:17398097, ECO:0000269|PubMed:18230608}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=May associate with
CC the cytoplasmic side of the plasma membrane and early endosomes.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K2A1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K2A1-2; Sequence=VSP_027252;
CC -!- TISSUE SPECIFICITY: Detected throughout the brain, particularly in
CC Purkinje cells, hippocampal and cortical neurons (at protein level).
CC {ECO:0000269|PubMed:17007823}.
CC -!- SIMILARITY: Belongs to the ced-6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29151.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK014093; BAB29151.2; ALT_INIT; mRNA.
DR EMBL; AK017798; BAB30939.1; -; mRNA.
DR EMBL; BC032154; AAH32154.1; -; mRNA.
DR CCDS; CCDS48250.1; -. [Q8K2A1-1]
DR RefSeq; NP_082726.2; NM_028450.3. [Q8K2A1-1]
DR AlphaFoldDB; Q8K2A1; -.
DR SMR; Q8K2A1; -.
DR BioGRID; 214196; 2.
DR STRING; 10090.ENSMUSP00000074115; -.
DR iPTMnet; Q8K2A1; -.
DR PhosphoSitePlus; Q8K2A1; -.
DR MaxQB; Q8K2A1; -.
DR PaxDb; Q8K2A1; -.
DR PeptideAtlas; Q8K2A1; -.
DR PRIDE; Q8K2A1; -.
DR ProteomicsDB; 271114; -. [Q8K2A1-1]
DR ProteomicsDB; 271115; -. [Q8K2A1-2]
DR Antibodypedia; 19788; 199 antibodies from 32 providers.
DR DNASU; 70676; -.
DR Ensembl; ENSMUST00000074525; ENSMUSP00000074115; ENSMUSG00000056870. [Q8K2A1-1]
DR Ensembl; ENSMUST00000160854; ENSMUSP00000125506; ENSMUSG00000056870. [Q8K2A1-2]
DR GeneID; 70676; -.
DR KEGG; mmu:70676; -.
DR UCSC; uc007awl.2; mouse. [Q8K2A1-2]
DR UCSC; uc007awm.2; mouse. [Q8K2A1-1]
DR CTD; 51454; -.
DR MGI; MGI:1920407; Gulp1.
DR VEuPathDB; HostDB:ENSMUSG00000056870; -.
DR eggNOG; KOG3536; Eukaryota.
DR GeneTree; ENSGT00940000156186; -.
DR HOGENOM; CLU_024530_0_0_1; -.
DR InParanoid; Q8K2A1; -.
DR OMA; CLDPVDS; -.
DR PhylomeDB; Q8K2A1; -.
DR TreeFam; TF314159; -.
DR BioGRID-ORCS; 70676; 0 hits in 70 CRISPR screens.
DR ChiTaRS; Gulp1; mouse.
DR PRO; PR:Q8K2A1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8K2A1; protein.
DR Bgee; ENSMUSG00000056870; Expressed in sciatic nerve and 215 other tissues.
DR ExpressionAtlas; Q8K2A1; baseline and differential.
DR Genevisible; Q8K2A1; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISO:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Coiled coil; Cytoplasm; Lipid transport;
KW Phagocytosis; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..304
FT /note="PTB domain-containing engulfment adapter protein 1"
FT /id="PRO_0000296680"
FT DOMAIN 21..176
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT COILED 159..200
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP9"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP9"
FT VAR_SEQ 282..304
FT /note="EGFKMGLTLEGTVFCLDPLDSRC -> VTILKDYLFLLIWNNNKMFLPTLSP
FT LLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027252"
FT CONFLICT 17
FT /note="P -> L (in Ref. 1; BAB29151)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="F -> L (in Ref. 1; BAB29151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 34470 MW; D99154EF53EFDC45 CRC64;
MNRAFSRKKD KTWMHTPEAL SKHYIPYNAK FLGSTEVEQP KGTEVVRDAV RKLKFARHIK
KSEGQKIPKV ELQISIYGVK ILEPKTKEVQ HNCQLHRISF CADDKTDKRI FTFICKDSES
NKHLCFVFDS EKCAEEITLT IGQAFDLAYR KFLESGGKDV ETRKQIAGMQ KRIQDLETEN
MELKNKVQDL ESRLRTTQVS TSPAHGVTVM SPSTDIFDMI PFSPISHQSP TSARNGTQLP
PIPSRSAETK RDLFGAEPFD PFNCGSGDFP PDIQSKLDEM QEGFKMGLTL EGTVFCLDPL
DSRC
