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   24-JUL-2024, entry version 160.
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; 24.
DR   IntAct; Q6ZMJ2; 18.
DR   STRING; 9606.ENSP00000346990; -.
DR   GlyCosmos; Q6ZMJ2; 6 sites, No reported glycans.
DR   GlyGen; Q6ZMJ2; 6 sites.
DR   iPTMnet; Q6ZMJ2; -.
DR   PhosphoSitePlus; Q6ZMJ2; -.
DR   SwissPalm; Q6ZMJ2; -.
DR   BioMuta; SCARA5; -.
DR   DMDM; 74749535; -.
DR   jPOST; Q6ZMJ2; -.
DR   MassIVE; Q6ZMJ2; -.
DR   PaxDb; 9606-ENSP00000346990; -.
DR   PeptideAtlas; Q6ZMJ2; -.
DR   ProteomicsDB; 67878; -. [Q6ZMJ2-1]
DR   ProteomicsDB; 67879; -. [Q6ZMJ2-2]
DR   ProteomicsDB; 67880; -. [Q6ZMJ2-3]
DR   ProteomicsDB; 67881; -. [Q6ZMJ2-4]
DR   Antibodypedia; 10358; 199 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   AGR; HGNC:28701; -.
DR   CTD; 286133; -.
DR   DisGeNET; 286133; -.
DR   GeneCards; SCARA5; -.
DR   HGNC; HGNC:28701; SCARA5.
DR   HPA; ENSG00000168079; Tissue enhanced (heart).
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; 5354783at2759; -.
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; 10 hits in 1154 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 160 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0070287; F:ferritin receptor activity; ISS:UniProtKB.
DR   GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR   GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; 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; SRCR-like domain; 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   InterPro; IPR050686; SRCR-S1_Scavenger_Rcptor.
DR   PANTHER; PTHR48071; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48071:SF27; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   Pfam; PF00530; SRCR; 1.
DR   PRINTS; PR00258; SPERACTRCPTR.
DR   SMART; SM00202; SR; 1.
DR   SUPFAM; SSF56487; SRCR-like; 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
//