CED7_CAEEL
ID CED7_CAEEL Reviewed; 1704 AA.
AC P34358; O76287; P34359;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 6.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=ABC transporter ced-7;
DE AltName: Full=Cell death protein 7;
GN Name=ced-7; ORFNames=C48B4.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, AND MUTAGENESIS OF
RP LYS-586; GLU-639 AND LYS-1417.
RC STRAIN=Bristol N2;
RX PubMed=9635425; DOI=10.1016/s0092-8674(00)81201-5;
RA Wu Y.-C., Horvitz H.R.;
RT "The C. elegans cell corpse engulfment gene ced-7 encodes a protein similar
RT to ABC transporters.";
RL Cell 93:951-960(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-1012 AND ASN-1045, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Functions in the engulfment of cell corpses during embryonic
CC programmed cell death to translocate molecules that mediate homotypic
CC adhesion between cell surfaces of the dying and engulfing cells.
CC {ECO:0000269|PubMed:9635425}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=c;
CC IsoId=P34358-1; Sequence=Displayed;
CC Name=a;
CC IsoId=P34358-2; Sequence=VSP_000044, VSP_000045;
CC Name=b;
CC IsoId=P34358-3; Sequence=VSP_000044;
CC -!- TISSUE SPECIFICITY: Ubiquitous in embryos. Expressed in larval germline
CC precursors. Expression in larvae and adults is seen in amphid sheath
CC cells, pharyngeal-intestinal valve and phasmid sheath cells. Low levels
CC of expression are also seen in gonadal sheath cells.
CC -!- DOMAIN: Multifunctional polypeptide with two homologous halves, each
CC containing a hydrophobic membrane-anchoring domain and an ATP binding
CC cassette (ABC) domain.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
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DR EMBL; AF049142; AAC24116.1; -; mRNA.
DR EMBL; Z29117; CAA82384.2; -; Genomic_DNA.
DR EMBL; Z29117; CAA82383.2; -; Genomic_DNA.
DR EMBL; Z29117; CAC42271.1; -; Genomic_DNA.
DR PIR; F88559; F88559.
DR PIR; T42749; T42749.
DR RefSeq; NP_001021225.1; NM_001026054.2. [P34358-3]
DR RefSeq; NP_001021226.1; NM_001026055.2.
DR RefSeq; NP_499115.2; NM_066714.3. [P34358-2]
DR AlphaFoldDB; P34358; -.
DR SMR; P34358; -.
DR STRING; 6239.C48B4.4d; -.
DR TCDB; 3.A.1.211.4; the atp-binding cassette (abc) superfamily.
DR iPTMnet; P34358; -.
DR EPD; P34358; -.
DR PaxDb; P34358; -.
DR PeptideAtlas; P34358; -.
DR EnsemblMetazoa; C48B4.4a.1; C48B4.4a.1; WBGene00000421. [P34358-2]
DR EnsemblMetazoa; C48B4.4a.2; C48B4.4a.2; WBGene00000421. [P34358-2]
DR EnsemblMetazoa; C48B4.4b.1; C48B4.4b.1; WBGene00000421. [P34358-3]
DR EnsemblMetazoa; C48B4.4c.1; C48B4.4c.1; WBGene00000421. [P34358-1]
DR GeneID; 176352; -.
DR UCSC; C48B4.4b; c. elegans. [P34358-1]
DR CTD; 176352; -.
DR WormBase; C48B4.4a; CE24856; WBGene00000421; ced-7. [P34358-2]
DR WormBase; C48B4.4b; CE24857; WBGene00000421; ced-7. [P34358-3]
DR WormBase; C48B4.4c; CE27867; WBGene00000421; ced-7. [P34358-1]
DR eggNOG; KOG0059; Eukaryota.
DR InParanoid; P34358; -.
DR PhylomeDB; P34358; -.
DR Reactome; R-CEL-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:P34358; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000421; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; P34358; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; ISS:WormBase.
DR GO; GO:1902742; P:apoptotic process involved in development; IMP:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:UniProtKB.
DR GO; GO:0070986; P:left/right axis specification; IGI:UniProtKB.
DR GO; GO:0006869; P:lipid transport; ISS:WormBase.
DR GO; GO:0033700; P:phospholipid efflux; IMP:WormBase.
DR GO; GO:1904747; P:positive regulation of apoptotic process involved in development; IMP:UniProtKB.
DR GO; GO:1903356; P:positive regulation of distal tip cell migration; IGI:UniProtKB.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; IMP:WormBase.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Glycoprotein; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1704
FT /note="ABC transporter ced-7"
FT /id="PRO_0000093377"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1126..1146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1153..1173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1176..1196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1201..1221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1234..1254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1266..1286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1311..1331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 546..777
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1379..1603
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 511..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 580..587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1411..1418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 986
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1012
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 1045
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 1597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1632
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 496..508
FT /note="Missing (in isoform a and isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_000044"
FT VAR_SEQ 992..993
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_000045"
FT MUTAGEN 586
FT /note="K->R: Cell corpses not engulfed."
FT /evidence="ECO:0000269|PubMed:9635425"
FT MUTAGEN 639
FT /note="E->G: Cell corpses not engulfed."
FT /evidence="ECO:0000269|PubMed:9635425"
FT MUTAGEN 1417
FT /note="K->R: Some cell corpses not engulfed."
FT /evidence="ECO:0000269|PubMed:9635425"
SQ SEQUENCE 1704 AA; 191412 MW; B7502A0B24507CFE CRC64;
MNRLRQFSLL LWKDWVLLRR NKVWTLFELI IPCLLLGPLV YLVVKNADHT SSPENIYDNF
QVKGTVEDVF LESNFIKPIY KRWCLRSDVV VGYTSKDAAA KRTVDDLMKK FAERFQSAKL
KLSVKNESSE EQLLTVLRND LPMLNETFCA INSYAAGVVF DEVDVTNKKL NYRILLGKTP
EETWHLTETS YNPYGPSSGR YSRIPSSPPY WTSAFLTFQH AIESSFLSSV QSGAPDLPIT
LRGLPEPRYK TSSVSAFIDF FPFIWAFVTF INVIHITREI AAENHAVKPY LTAMGLSTFM
FYAAHVVMAF LKFFVIFLCS IIPLTFVMEF VSPAALIVTV LMYGLGAVIF GAFVASFFNN
TNSAIKAILV AWGAMIGISY KLRPELDQIS SCFLYGLNIN GAFALAVEAI SDYMRREREL
NLTNMFNDSS LHFSLGWALV MMIVDILWMS IGALVVDHIR TSADFSLRTL FDFEAPEDDE
NQTDGVTAQN TRINEQVRNR VRRSDMEIQM NPMASTSLNP PNADSDSLLE GSTEADGARD
TARADIIVRN LVKIWSTTGE RAVDGLSLRA VRGQCSILLG HNGAGKSTTF SSIAGIIRPT
NGRITICGYD VGNEPGETRR HIGMCPQYNP LYDQLTVSEH LKLVYGLKGA REKDFKQDMK
RLLSDVKLDF KENEKAVNLS GGMKRKLCVC MALIGDSEVV LLDEPTAGMD PGARQDVQKL
VEREKANRTI LLTTHYMDEA ERLGDWVFIM SHGKLVASGT NQYLKQKFGT GYLLTVVLDH
NGDKRKMAVI LTDVCTHYVK EAERGEMHGQ QIEIILPEAR KKEFVPLFQA LEAIQDRNYR
SNVFDNMPNT LKSQLATLEM RSFGLSLNTL EQVFITIGDK VDKAIASRQN SRISHNSRNA
SEPSLKPAGY DTQSSTKSAD SYQKLMDSQA RGPEKSGVAK MVAQFISIMR KKFLYSRRNW
AQLFTQVLIP IILLGLVGSL TTLKSNNTDQ FSVRSLTPSG IEPSKVVWRF ENGTIPEEAA
NFEKILRKSG GFEVLNYNTK NPLPNITKSL IGEMPPATIG MTMNSDNLEA LFNMRYYHVL
PTLISMINRA RLTGTVDAEI SSGVFLYSKS TSNSNLLPSQ LIDVLLAPML ILIFAMVTST
FVMFLIEERT CQFAHQQFLT GISPITFYSA SLIYDGILYS LICLIFLFMF LAFHWMYDHL
AIVILFWFLY FFSSVPFIYA VSFLFQSPSK ANVLLIIWQV VISGAALLAV FLIFMIFNID
EWLKSILVNI FMFLLPSYAF GSAIITINTY GMILPSEELM NWDHCGKNAW LMGTFGVCSF
ALFVLLQFKF VRRFLSQVWT VRRSSHNNVQ PMMGDLPVCE SVSEERERVH RVNSQNSALV
IKDLTKTFGR FTAVNELCLA VDQKECFGLL GVNGAGKTTT FNILTGQSFA SSGEAMIGGR
DVTELISIGY CPQFDALMLD LTGRESLEIL AQMHGFENYK AKAELILECV GMIAHADKLV
RFYSGGQKRK ISVGVALLAP TQMIILDEPT AGIDPKARRE VWELLLWCRE HSNSALMLTS
HSMDECEALC SRIAVLNRGS LIAIGSSQEL KSLYGNNYTM TLSLYEPNQR DMVVQLVQTR
LPNSVLKTTS TNKTLNLKWQ IPKEKEDCWS AKFEMVQALA KDLGVKDFIL AQSSLEETFL
RLAGLDEDQL DTHSTVEISH STHV
