SCAR5_MOUSE
ID SCAR5_MOUSE Reviewed; 491 AA.
AC Q8K299; Q8BZZ2; Q8R330; Q91WD6; Q9CUC3; Q9D4G8;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Scavenger receptor class A member 5 {ECO:0000255|HAMAP-Rule:MF_03070};
GN Name=Scara5 {ECO:0000255|HAMAP-Rule:MF_03070};
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 [MRNA], SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=16407294; DOI=10.1074/jbc.m507599200;
RA Jiang Y., Oliver P., Davies K.E., Platt N.;
RT "Identification and characterization of murine SCARA5, a novel class A
RT scavenger receptor that is expressed by populations of epithelial cells.";
RL J. Biol. Chem. 281:11834-11845(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Eye, and 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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19154717; DOI=10.1016/j.devcel.2008.12.002;
RA Li J.Y., Paragas N., Ned R.M., Qiu A., Viltard M., Leete T., Drexler I.R.,
RA Chen X., Sanna-Cherchi S., Mohammed F., Williams D., Lin C.S.,
RA Schmidt-Ott K.M., Andrews N.C., Barasch J.;
RT "Scara5 is a ferritin receptor mediating non-transferrin iron delivery.";
RL Dev. Cell 16:35-46(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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: 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. Ferritin mediates iron uptake in
CC capsule cells of the developing kidney. Preferentially binds ferritin
CC light chain (FTL) compared to heavy chain (FTH1). {ECO:0000255|HAMAP-
CC Rule:MF_03070, ECO:0000269|PubMed:19154717}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_03070,
CC ECO:0000269|PubMed:16407294}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_03070,
CC ECO:0000269|PubMed:19154717}; Single-pass type II membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03070, ECO:0000269|PubMed:19154717}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8K299-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K299-2; Sequence=VSP_023477, VSP_023478;
CC Name=3;
CC IsoId=Q8K299-3; Sequence=VSP_023476, VSP_023477, VSP_023478;
CC -!- TISSUE SPECIFICITY: Expressed in the testis, trachea, lung, bladder and
CC small intestine; especially in epithelial cells associated with mucosal
CC surfaces. {ECO:0000269|PubMed:16407294}.
CC -!- SIMILARITY: Belongs to the SCARA5 family. {ECO:0000255|HAMAP-
CC Rule:MF_03070}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ122126; AAZ41380.1; -; mRNA.
DR EMBL; AK016543; BAB30293.1; -; mRNA.
DR EMBL; AK016912; BAB30492.3; -; mRNA.
DR EMBL; AK033154; BAC28173.1; -; mRNA.
DR EMBL; AK133176; BAE21542.1; -; mRNA.
DR EMBL; BC016096; AAH16096.1; -; mRNA.
DR EMBL; BC023907; AAH23907.1; -; mRNA.
DR EMBL; BC026758; AAH26758.1; -; mRNA.
DR EMBL; BC032159; AAH32159.1; -; mRNA.
DR CCDS; CCDS27214.1; -. [Q8K299-1]
DR CCDS; CCDS49523.1; -. [Q8K299-2]
DR RefSeq; NP_001161790.1; NM_001168318.1. [Q8K299-2]
DR RefSeq; NP_083179.2; NM_028903.2. [Q8K299-1]
DR PDB; 7BZZ; X-ray; 2.50 A; A/D=384-489.
DR PDBsum; 7BZZ; -.
DR AlphaFoldDB; Q8K299; -.
DR SMR; Q8K299; -.
DR IntAct; Q8K299; 1.
DR STRING; 10090.ENSMUSP00000022610; -.
DR GlyGen; Q8K299; 7 sites.
DR iPTMnet; Q8K299; -.
DR PhosphoSitePlus; Q8K299; -.
DR MaxQB; Q8K299; -.
DR PaxDb; Q8K299; -.
DR PeptideAtlas; Q8K299; -.
DR PRIDE; Q8K299; -.
DR ProteomicsDB; 255481; -. [Q8K299-1]
DR ProteomicsDB; 255482; -. [Q8K299-2]
DR ProteomicsDB; 255483; -. [Q8K299-3]
DR Antibodypedia; 10358; 198 antibodies from 30 providers.
DR DNASU; 71145; -.
DR Ensembl; ENSMUST00000022610; ENSMUSP00000022610; ENSMUSG00000022032. [Q8K299-1]
DR Ensembl; ENSMUST00000069226; ENSMUSP00000063391; ENSMUSG00000022032. [Q8K299-2]
DR GeneID; 71145; -.
DR KEGG; mmu:71145; -.
DR UCSC; uc007ujm.2; mouse. [Q8K299-2]
DR UCSC; uc007ujn.2; mouse. [Q8K299-1]
DR CTD; 286133; -.
DR MGI; MGI:1918395; Scara5.
DR VEuPathDB; HostDB:ENSMUSG00000022032; -.
DR eggNOG; ENOG502QSM1; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR HOGENOM; CLU_041152_1_0_1; -.
DR InParanoid; Q8K299; -.
DR OMA; LCDEVST; -.
DR OrthoDB; 711951at2759; -.
DR PhylomeDB; Q8K299; -.
DR TreeFam; TF330855; -.
DR BioGRID-ORCS; 71145; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Scara5; mouse.
DR PRO; PR:Q8K299; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8K299; protein.
DR Bgee; ENSMUSG00000022032; Expressed in sciatic nerve and 150 other tissues.
DR Genevisible; Q8K299; MM.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0070287; F:ferritin receptor activity; IDA:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR GO; GO:0034755; P:iron ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IPI: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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coiled coil;
KW Disulfide bond; Glycoprotein; Ion transport; Iron; Iron transport;
KW Membrane; Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..491
FT /note="Scavenger receptor class A member 5"
FT /id="PRO_0000279519"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT TRANSMEM 61..81
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT TOPO_DOM 82..491
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DOMAIN 305..356
FT /note="Collagen-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DOMAIN 389..489
FT /note="SRCR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT REGION 301..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 91..111
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT COMPBIAS 366..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DISULFID 414..478
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DISULFID 427..488
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DISULFID 458..468
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT VAR_SEQ 1..107
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023476"
FT VAR_SEQ 382..387
FT /note="GDMDFT -> ECCRGG (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023477"
FT VAR_SEQ 388..491
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023478"
FT CONFLICT 13
FT /note="D -> Y (in Ref. 2; BAB30492)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="M -> T (in Ref. 3; AAH16096)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..212
FT /note="LARR -> RTRG (in Ref. 3; AAH26758)"
FT /evidence="ECO:0000305"
FT CONFLICT 213..215
FT /note="VGV -> MAK (in Ref. 2; BAB30492)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="E -> D (in Ref. 2; BAC28173)"
FT /evidence="ECO:0000305"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:7BZZ"
FT STRAND 389..396
FT /evidence="ECO:0007829|PDB:7BZZ"
FT STRAND 399..406
FT /evidence="ECO:0007829|PDB:7BZZ"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:7BZZ"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:7BZZ"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:7BZZ"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:7BZZ"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:7BZZ"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:7BZZ"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:7BZZ"
SQ SEQUENCE 491 AA; 53667 MW; 12FF66032D46F722 CRC64;
MDNKAMYLHT VSDRDNGSIF EEPFDGRSLS KLNLCEDGPC HKRRAGGCCT QLGSLSALKH
AVLGLYLLVF LILVGIFILA VSRPRSSPDD LKALTRNVNR LNESLRDMQL RLLQAPLQAD
LTEQVWKVQD ALQNQTDSLL ALAGLVQRLE GTLWGLHAQA AQTEQAMALL RDRTGQQSDS
AQLELYQLQV ESNRSQLLLQ RHAGLLDGLA RRVGVLGEEL ADVGGALRGL NHSLSYDVAL
HSTWLQDLQV LVSNASADTR RMRLVHMDME MQLKQELATL NVVTEDLRLK DWEHSIALRN
ITLAKGPPGP KGDQGNEGKE GKPGSPGLPG SRGLPGERGD PGLPGPKGDD GKLGATGPMG
MRGFKGDRGP KGEKGERGER AGDMDFTMIR LVNGSGPHQG RVEVFHDRRW GTVCDDGWDK
KDGDVVCRML GFHGVEEVYR TARFGQGTGR IWMDDVNCKG TESSIFHCQF SKWGVTNCGH
AEDAGVTCTV P
