SCAR5_BOVIN
ID SCAR5_BOVIN Reviewed; 495 AA.
AC A5PJQ2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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; BC142199; AAI42200.1; -; mRNA.
DR RefSeq; NP_001095969.1; NM_001102499.1.
DR AlphaFoldDB; A5PJQ2; -.
DR SMR; A5PJQ2; -.
DR STRING; 9913.ENSBTAP00000026158; -.
DR PaxDb; A5PJQ2; -.
DR PRIDE; A5PJQ2; -.
DR Ensembl; ENSBTAT00000026158; ENSBTAP00000026158; ENSBTAG00000019636.
DR GeneID; 516087; -.
DR KEGG; bta:516087; -.
DR CTD; 286133; -.
DR VEuPathDB; HostDB:ENSBTAG00000019636; -.
DR VGNC; VGNC:34323; SCARA5.
DR eggNOG; ENOG502QSM1; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR HOGENOM; CLU_041152_1_0_1; -.
DR InParanoid; A5PJQ2; -.
DR OMA; LCDEVST; -.
DR OrthoDB; 711951at2759; -.
DR TreeFam; TF330855; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000019636; Expressed in uterine horn and 101 other tissues.
DR ExpressionAtlas; A5PJQ2; baseline and differential.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0070287; F:ferritin receptor activity; ISS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
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 GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Coiled coil; Disulfide bond; Glycoprotein; Ion transport;
KW Iron; Iron transport; Membrane; Receptor; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..495
FT /note="Scavenger receptor class A member 5"
FT /id="PRO_0000367314"
FT TOPO_DOM 1..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT TRANSMEM 62..82
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT TOPO_DOM 83..495
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DOMAIN 306..357
FT /note="Collagen-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DOMAIN 393..493
FT /note="SRCR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT REGION 303..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 92..112
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT COMPBIAS 367..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DISULFID 418..482
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DISULFID 431..492
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DISULFID 462..472
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
SQ SEQUENCE 495 AA; 53453 MW; FD97DA8ABBEB32D5 CRC64;
MENKAMYLHA TVSDRDSSSI FEEPFDGRSL SKLNLCEDGP CHKGRAGGCC TQLGSLSALK
HAVLGLYLLV FLILVGIFIL AVSRPRSSPD DLKALTRNVN RLNESFRDLQ LRLLQAPLQG
ELSEQVWKAH DALQNQSDSL LALAGAVQRL EGALWGLQAQ AAQSEQAVVL LRERAAQQSD
AAQLELYQLQ VDSNRSQLLL RRHAGLLDGL ARRVGALSDE LADVGGALRG LNLSLSYDVA
LQGTRLRDLR VLVSNASEDA RRLRLAHRGL ELQLKQELAV LNGVTEDLRL KDWEHSIALR
NITLAKGPPG PKGDPGDAGK EGEPGIPGLP GLRGLPGERG TPGLPGPKGD EGKLGATGPM
GMRGFKGDRG PKGEKGEKGD RTVDASGVEA VMVRLVNGSG LHQGRVEVYH ERRWGTVCDD
GWDKKDGDVV CRMLGFPGAE DVHRTAQFGQ GTGRIWMDDV ACKGTEESIF RCSFSKWGVT
NCGHAEDAGV TCKRH
