GULP1_RAT
ID GULP1_RAT Reviewed; 304 AA.
AC Q5PQS4; Q0PYK2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 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 [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, INTERACTION
RP WITH CLATHRIN, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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).
CC -!- FUNCTION: May function as an adapter protein. Required for efficient
CC phagocytosis of apoptotic cells. Modulates cellular glycosphingolipid
CC and cholesterol transport. May play a role in the internalization and
CC endosomal trafficking of various LRP1 ligands, such as PSAP. Increases
CC cellular levels of GTP-bound ARF6 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with GDP-bound ARF6, but not with GTP-
CC bound ARF6. Part of a complex composed of GULP1, ACAP1 and ARF6.
CC Interacts with ACAP1, LRP1, MEGF10 and STAB2 (By similarity). Interacts
CC with clathrin. {ECO:0000250, ECO:0000269|PubMed:17007823}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=May associate with
CC the cytoplasmic side of the plasma membrane and early endosomes (By
CC similarity). Detected in synapses. {ECO:0000250,
CC ECO:0000269|PubMed:17007823}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5PQS4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5PQS4-2; Sequence=VSP_027253, VSP_027254;
CC -!- TISSUE SPECIFICITY: Detected throughout adult and fetal brain. Detected
CC in cerebellum, cortex and hippocampus (at protein level).
CC {ECO:0000269|PubMed:17007823}.
CC -!- SIMILARITY: Belongs to the ced-6 family. {ECO:0000305}.
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DR EMBL; DQ668344; ABG66963.1; -; mRNA.
DR EMBL; BC087053; AAH87053.1; -; mRNA.
DR RefSeq; NP_001013189.1; NM_001013171.2. [Q5PQS4-1]
DR RefSeq; XP_006244866.1; XM_006244804.3. [Q5PQS4-1]
DR RefSeq; XP_017451886.1; XM_017596397.1. [Q5PQS4-2]
DR AlphaFoldDB; Q5PQS4; -.
DR SMR; Q5PQS4; -.
DR BioGRID; 260751; 1.
DR STRING; 10116.ENSRNOP00000004463; -.
DR CarbonylDB; Q5PQS4; -.
DR PaxDb; Q5PQS4; -.
DR PRIDE; Q5PQS4; -.
DR GeneID; 314543; -.
DR KEGG; rno:314543; -.
DR UCSC; RGD:1306380; rat. [Q5PQS4-1]
DR CTD; 51454; -.
DR RGD; 1306380; Gulp1.
DR VEuPathDB; HostDB:ENSRNOG00000003242; -.
DR eggNOG; KOG3536; Eukaryota.
DR HOGENOM; CLU_024530_0_0_1; -.
DR InParanoid; Q5PQS4; -.
DR OMA; CLDPVDS; -.
DR OrthoDB; 920757at2759; -.
DR PhylomeDB; Q5PQS4; -.
DR TreeFam; TF314159; -.
DR PRO; PR:Q5PQS4; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000003242; Expressed in ovary and 18 other tissues.
DR ExpressionAtlas; Q5PQS4; baseline and differential.
DR Genevisible; Q5PQS4; RN.
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:RGD.
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_0000296681"
FT DOMAIN 21..176
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT COILED 159..202
FT /evidence="ECO:0000255"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP9"
FT VAR_SEQ 172
FT /note="R -> RSSRGSRCW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17007823"
FT /id="VSP_027253"
FT VAR_SEQ 282..304
FT /note="EGFKMGLTLEGTVFCLDPLDSRC -> RQRWRGSKWD (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:17007823"
FT /id="VSP_027254"
SQ SEQUENCE 304 AA; 34285 MW; C5EBEC29A3FF8802 CRC64;
MNRAFSRKKD KTWMHMPEAL SKHYVPYNAK FLGSTEVEQP KGTEVVRDAV RKLKFARHIK
KSEGQKIPKV ELQISIYGVK ILEPKTKEVQ HNCQLHRISF CADDKTDKRI FTFICKDSES
NKHLCFVFDS EKCAEEITLT IGQAFDLAYR KFLESGGKDV ETRKQIAGMQ KRIQDLETEN
MELKNKVQDL ENRLRTTQVS STPAGGVTVT SPSTDIFDMI PFSPISHPSP TSAGNGTQLP
PIPSRSSEIK RDLFGAEPFD PFNCGAGDFP PDIQSKLDEM QEGFKMGLTL EGTVFCLDPL
DSRC
