SCAR5_DANRE
ID SCAR5_DANRE Reviewed; 499 AA.
AC Q5RFW0;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Scavenger receptor class A member 5 {ECO:0000255|HAMAP-Rule:MF_03070};
GN Name=scara5 {ECO:0000255|HAMAP-Rule:MF_03070}; ORFNames=si:ch211-200p13.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Ferritin receptor that mediates non-transferrin-dependent
CC delivery of iron. Mediates cellular uptake of ferritin-bound iron by
CC stimulating ferritin endocytosis from the cell surface with consequent
CC iron delivery within the cell. Delivery of iron to cells by ferritin is
CC required for the development of specific cell types, suggesting the
CC existence of cell type-specific mechanisms of iron traffic in
CC organogenesis, which alternatively utilize transferrin or non-
CC transferrin iron delivery pathways. {ECO:0000255|HAMAP-Rule:MF_03070}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_03070}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_03070};
CC Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_03070}.
CC -!- SIMILARITY: Belongs to the SCARA5 family. {ECO:0000255|HAMAP-
CC Rule:MF_03070}.
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DR EMBL; CR536610; CAI11749.1; -; Genomic_DNA.
DR RefSeq; NP_001025361.1; NM_001030190.1.
DR RefSeq; XP_005160375.1; XM_005160318.3.
DR AlphaFoldDB; Q5RFW0; -.
DR SMR; Q5RFW0; -.
DR STRING; 7955.ENSDARP00000126688; -.
DR PaxDb; Q5RFW0; -.
DR Ensembl; ENSDART00000152373; ENSDARP00000126688; ENSDARG00000010425.
DR Ensembl; ENSDART00000181830; ENSDARP00000150337; ENSDARG00000010425.
DR GeneID; 564500; -.
DR KEGG; dre:564500; -.
DR CTD; 286133; -.
DR ZFIN; ZDB-GENE-041210-258; scara5.
DR eggNOG; ENOG502QSM1; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR HOGENOM; CLU_041152_1_0_1; -.
DR InParanoid; Q5RFW0; -.
DR OMA; TRMEDRS; -.
DR OrthoDB; 711951at2759; -.
DR PhylomeDB; Q5RFW0; -.
DR TreeFam; TF330855; -.
DR Reactome; R-DRE-3000480; Scavenging by Class A Receptors.
DR PRO; PR:Q5RFW0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000010425; Expressed in testis and 13 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0070287; F:ferritin receptor activity; ISS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0034755; P:iron ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR Gene3D; 3.10.250.10; -; 1.
DR HAMAP; MF_03070; SCARA5; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR034726; SCARA5.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Iron;
KW Iron transport; Membrane; Receptor; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..499
FT /note="Scavenger receptor class A member 5"
FT /id="PRO_0000279520"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT TRANSMEM 64..84
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT TOPO_DOM 85..499
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DOMAIN 307..359
FT /note="Collagen-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DOMAIN 398..498
FT /note="SRCR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT REGION 305..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DISULFID 423..487
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DISULFID 436..497
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DISULFID 467..477
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
SQ SEQUENCE 499 AA; 55221 MW; 734BD961B341A4BD CRC64;
MENRAMYLTT THEDRENSSF YEESYDGMNL SKLNLCEEVN STKYRRKTDN RCGQLDSLTS
IKYAIVSLYI LVLLTIFGLC IAVSKSHASW RREEALLENV TRLGEQSETL QMSLSQIPSQ
SDLLENIWKL ESLFHNHTEQ LRLLGLLTQG LERDIKDLQA FAEHTTDSVA QLWDHLSMIS
HSSQRNSTHL GDELASTAGS IREQDALLKT MVGNVETLQE RLEDMGWTLQ TLNHSLGGDV
SLHQIKIYEL QEKIVNVTHD TLGMKITQTH LEDQLRNEIQ VLNVVTADLR LKEWEHSMAL
KNLTIFQGPP GPKGEKGDVG PLGPDGIPGW IGPRGLTGEK GVQGPRGLAG RNGQDGHNGD
KGEVGPEGPK GVRGERGPKG EKGERGDKQG EKVEDAVVRL VNGSGPHEGR VEVLHDLRWG
TVCDDVWDIK DGDVVCRMLG FRGAKEIHKT GRFGQGTGLI WMDDVACVGT EDSIDLCKFS
GWGKTNCGHV EDAGVTCNV
