SCAR5_HUMAN
ID SCAR5_HUMAN Reviewed; 495 AA.
AC Q6ZMJ2; Q6UXZ1; Q7Z4A1; Q8N4Z7;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Scavenger receptor class A member 5 {ECO:0000255|HAMAP-Rule:MF_03070};
DE AltName: Full=Scavenger receptor hlg;
GN Name=SCARA5 {ECO:0000255|HAMAP-Rule:MF_03070}; ORFNames=UNQ2938/PRO28700;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT HIS-316.
RA Lin L., Yu R., Zheng G., Li H., Zhou G., Shen C., Ke R., Zhong G., Xiao W.,
RA Li M., Yang S.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
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: 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 -!- INTERACTION:
CC Q6ZMJ2-2; Q86Z23: C1QL4; NbExp=3; IntAct=EBI-12823227, EBI-12062109;
CC Q6ZMJ2-2; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-12823227, EBI-11522780;
CC Q6ZMJ2-2; Q08426: EHHADH; NbExp=3; IntAct=EBI-12823227, EBI-2339219;
CC Q6ZMJ2-2; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-12823227, EBI-742102;
CC Q6ZMJ2-2; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-12823227, EBI-2556193;
CC Q6ZMJ2-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12823227, EBI-741158;
CC Q6ZMJ2-2; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-12823227, EBI-10181968;
CC Q6ZMJ2-2; P20618: PSMB1; NbExp=3; IntAct=EBI-12823227, EBI-372273;
CC Q6ZMJ2-2; Q2KHN1: RNF151; NbExp=3; IntAct=EBI-12823227, EBI-12002474;
CC Q6ZMJ2-2; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-12823227, EBI-10281213;
CC Q6ZMJ2-2; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-12823227, EBI-358489;
CC Q6ZMJ2-2; Q9BTX3: TMEM208; NbExp=3; IntAct=EBI-12823227, EBI-12876824;
CC Q6ZMJ2-2; Q99816: TSG101; NbExp=3; IntAct=EBI-12823227, EBI-346882;
CC Q6ZMJ2-2; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-12823227, EBI-712969;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6ZMJ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZMJ2-2; Sequence=VSP_023474, VSP_023475;
CC Name=3;
CC IsoId=Q6ZMJ2-3; Sequence=VSP_023472, VSP_023474, VSP_023475;
CC Name=4;
CC IsoId=Q6ZMJ2-4; Sequence=VSP_023473;
CC -!- SIMILARITY: Belongs to the SCARA5 family. {ECO:0000255|HAMAP-
CC Rule:MF_03070}.
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DR EMBL; AY358150; AAQ88517.1; -; mRNA.
DR EMBL; AK172746; BAD18733.1; -; mRNA.
DR EMBL; AY337579; AAQ17470.1; -; mRNA.
DR EMBL; BC033153; AAH33153.1; -; mRNA.
DR CCDS; CCDS6064.1; -. [Q6ZMJ2-1]
DR RefSeq; NP_776194.2; NM_173833.5. [Q6ZMJ2-1]
DR PDB; 7C00; X-ray; 1.70 A; A=392-495.
DR PDBsum; 7C00; -.
DR AlphaFoldDB; Q6ZMJ2; -.
DR SMR; Q6ZMJ2; -.
DR BioGRID; 130309; 23.
DR IntAct; Q6ZMJ2; 18.
DR STRING; 9606.ENSP00000346990; -.
DR GlyGen; Q6ZMJ2; 6 sites.
DR iPTMnet; Q6ZMJ2; -.
DR PhosphoSitePlus; Q6ZMJ2; -.
DR BioMuta; SCARA5; -.
DR DMDM; 74749535; -.
DR jPOST; Q6ZMJ2; -.
DR MassIVE; Q6ZMJ2; -.
DR PaxDb; Q6ZMJ2; -.
DR PeptideAtlas; Q6ZMJ2; -.
DR PRIDE; Q6ZMJ2; -.
DR ProteomicsDB; 67878; -. [Q6ZMJ2-1]
DR ProteomicsDB; 67879; -. [Q6ZMJ2-2]
DR ProteomicsDB; 67880; -. [Q6ZMJ2-3]
DR ProteomicsDB; 67881; -. [Q6ZMJ2-4]
DR Antibodypedia; 10358; 198 antibodies from 30 providers.
DR DNASU; 286133; -.
DR Ensembl; ENST00000354914.8; ENSP00000346990.3; ENSG00000168079.17. [Q6ZMJ2-1]
DR Ensembl; ENST00000380385.6; ENSP00000369746.2; ENSG00000168079.17. [Q6ZMJ2-4]
DR Ensembl; ENST00000518030.1; ENSP00000430713.1; ENSG00000168079.17. [Q6ZMJ2-3]
DR Ensembl; ENST00000524352.5; ENSP00000428663.1; ENSG00000168079.17. [Q6ZMJ2-2]
DR GeneID; 286133; -.
DR KEGG; hsa:286133; -.
DR MANE-Select; ENST00000354914.8; ENSP00000346990.3; NM_173833.6; NP_776194.2.
DR UCSC; uc003xgj.4; human. [Q6ZMJ2-1]
DR CTD; 286133; -.
DR DisGeNET; 286133; -.
DR GeneCards; SCARA5; -.
DR HGNC; HGNC:28701; SCARA5.
DR HPA; ENSG00000168079; Tissue enhanced (urinary).
DR MIM; 611306; gene.
DR neXtProt; NX_Q6ZMJ2; -.
DR OpenTargets; ENSG00000168079; -.
DR PharmGKB; PA142670948; -.
DR VEuPathDB; HostDB:ENSG00000168079; -.
DR eggNOG; ENOG502QSM1; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR HOGENOM; CLU_041152_1_0_1; -.
DR InParanoid; Q6ZMJ2; -.
DR OMA; LCDEVST; -.
DR OrthoDB; 711951at2759; -.
DR PhylomeDB; Q6ZMJ2; -.
DR TreeFam; TF330855; -.
DR PathwayCommons; Q6ZMJ2; -.
DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
DR SignaLink; Q6ZMJ2; -.
DR BioGRID-ORCS; 286133; 7 hits in 1074 CRISPR screens.
DR ChiTaRS; SCARA5; human.
DR GenomeRNAi; 286133; -.
DR Pharos; Q6ZMJ2; Tbio.
DR PRO; PR:Q6ZMJ2; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q6ZMJ2; protein.
DR Bgee; ENSG00000168079; Expressed in decidua and 159 other tissues.
DR Genevisible; Q6ZMJ2; HS.
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: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 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..495
FT /note="Scavenger receptor class A member 5"
FT /id="PRO_0000279518"
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..495
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03070"
FT DOMAIN 305..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 301..386
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..383
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 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"
FT VAR_SEQ 38..80
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_023472"
FT VAR_SEQ 81..305
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_023473"
FT VAR_SEQ 386..400
FT /note="GVEAPMMIRLVNGSG -> KDILLGPWDMVLAQG (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_023474"
FT VAR_SEQ 401..495
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_023475"
FT VARIANT 45
FT /note="A -> T (in dbSNP:rs17058374)"
FT /id="VAR_052062"
FT VARIANT 316
FT /note="D -> H (in dbSNP:rs17058207)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_030915"
FT CONFLICT 93
FT /note="A -> S (in Ref. 3; AAQ17470)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="T -> A (in Ref. 3; AAQ17470)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="L -> S (in Ref. 3; AAQ17470)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="Q -> R (in Ref. 3; AAQ17470)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="K -> E (in Ref. 3; AAQ17470)"
FT /evidence="ECO:0000305"
FT STRAND 393..400
FT /evidence="ECO:0007829|PDB:7C00"
FT STRAND 403..410
FT /evidence="ECO:0007829|PDB:7C00"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:7C00"
FT HELIX 424..433
FT /evidence="ECO:0007829|PDB:7C00"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:7C00"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:7C00"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:7C00"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:7C00"
FT STRAND 489..493
FT /evidence="ECO:0007829|PDB:7C00"
SQ SEQUENCE 495 AA; 53994 MW; C37E94B2D2E3F5CF CRC64;
MENKAMYLHT VSDCDTSSIC EDSFDGRSLS KLNLCEDGPC HKRRASICCT QLGSLSALKH
AVLGLYLLVF LILVGIFILA VSRPRSSPDD LKALTRNVNR LNESFRDLQL RLLQAPLQAD
LTEQVWKVQD ALQNQSDSLL ALAGAVQRLE GALWGLQAQA VQTEQAVALL RDRTGQQSDT
AQLELYQLQV ESNSSQLLLR RHAGLLDGLA RRVGILGEEL ADVGGVLRGL NHSLSYDVAL
HRTRLQDLRV LVSNASEDTR RLRLAHVGME LQLKQELAML NAVTEDLRLK DWEHSIALRN
ISLAKGPPGP KGDQGDEGKE GRPGIPGLPG LRGLPGERGT PGLPGPKGDD GKLGATGPMG
MRGFKGDRGP KGEKGEKGDR AGDASGVEAP MMIRLVNGSG PHEGRVEVYH DRRWGTVCDD
GWDKKDGDVV CRMLGFRGVE EVYRTARFGQ GTGRIWMDDV ACKGTEETIF RCSFSKWGVT
NCGHAEDASV TCNRH
