S22AH_MOUSE
ID S22AH_MOUSE Reviewed; 401 AA.
AC Q9D9E0; Q9WTM1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Solute carrier family 22 member 17;
DE AltName: Full=24p3 receptor;
DE Short=24p3R;
DE AltName: Full=Brain-type organic cation transporter;
DE AltName: Full=Lipocalin-2 receptor;
GN Name=Slc22a17; Synonyms=Boct;
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] (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Hippocampus;
RA Yaoi T., Kuwajima G., Nakayama T.;
RT "Mouse organic cation transporter BOCT complete cDNA.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16377569; DOI=10.1016/j.cell.2005.10.027;
RA Devireddy L.R., Gazin C., Zhu X., Green M.R.;
RT "A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis
RT and iron uptake.";
RL Cell 123:1293-1305(2005).
CC -!- FUNCTION: Cell surface receptor for LCN2 (24p3) that plays a key role
CC in iron homeostasis and transport. Able to bind iron-bound LCN2 (holo-
CC 24p3), followed by internalization of holo-24p3 and release of iron,
CC thereby increasing intracellular iron concentration and leading to
CC inhibition of apoptosis. Also binds iron-free LCN2 (apo-24p3), followed
CC by internalization of apo-24p3 and its association with an
CC intracellular siderophore, leading to iron chelation and iron transfer
CC to the extracellular medium, thereby reducing intracellular iron
CC concentration and resulting in apoptosis.
CC {ECO:0000269|PubMed:16377569}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Vacuole membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Upon LCN2-binding, it is
CC internalized. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D9E0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D9E0-2; Sequence=VSP_039789;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16377569}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 7 dpc and throughout development.
CC {ECO:0000269|PubMed:16377569}.
CC -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
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DR EMBL; AB012808; BAA76761.1; -; mRNA.
DR EMBL; AK007059; BAB24845.2; -; mRNA.
DR CCDS; CCDS36924.1; -. [Q9D9E0-1]
DR RefSeq; NP_067526.2; NM_021551.4. [Q9D9E0-1]
DR AlphaFoldDB; Q9D9E0; -.
DR SMR; Q9D9E0; -.
DR STRING; 10090.ENSMUSP00000049676; -.
DR iPTMnet; Q9D9E0; -.
DR PhosphoSitePlus; Q9D9E0; -.
DR MaxQB; Q9D9E0; -.
DR PaxDb; Q9D9E0; -.
DR PRIDE; Q9D9E0; -.
DR ProteomicsDB; 253358; -. [Q9D9E0-1]
DR ProteomicsDB; 253359; -. [Q9D9E0-2]
DR Antibodypedia; 111; 237 antibodies from 33 providers.
DR DNASU; 59049; -.
DR Ensembl; ENSMUST00000050772; ENSMUSP00000049676; ENSMUSG00000022199. [Q9D9E0-1]
DR GeneID; 59049; -.
DR KEGG; mmu:59049; -.
DR UCSC; uc007txk.2; mouse. [Q9D9E0-1]
DR CTD; 51310; -.
DR MGI; MGI:1926225; Slc22a17.
DR VEuPathDB; HostDB:ENSMUSG00000022199; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000160959; -.
DR HOGENOM; CLU_001265_33_6_1; -.
DR InParanoid; Q9D9E0; -.
DR PhylomeDB; Q9D9E0; -.
DR TreeFam; TF335753; -.
DR Reactome; R-MMU-917937; Iron uptake and transport.
DR BioGRID-ORCS; 59049; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q9D9E0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9D9E0; protein.
DR Bgee; ENSMUSG00000022199; Expressed in choroid plexus of fourth ventricle and 241 other tissues.
DR ExpressionAtlas; Q9D9E0; baseline and differential.
DR Genevisible; Q9D9E0; MM.
DR GO; GO:0031301; C:integral component of organelle membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0015891; P:siderophore transport; IMP:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Ion transport; Iron; Iron transport;
KW Membrane; Receptor; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT CHAIN 1..401
FT /note="Solute carrier family 22 member 17"
FT /id="PRO_0000398633"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039789"
FT CONFLICT 51
FT /note="L -> R (in Ref. 1; BAA76761)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="Q -> H (in Ref. 1; BAA76761)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> G (in Ref. 1; BAA76761)"
FT /evidence="ECO:0000305"
FT CONFLICT 362..363
FT /note="KL -> NV (in Ref. 1; BAA76761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 43195 MW; 8E203EC412817502 CRC64;
MPSARFGRRG IVLLTLGLVG PCGVGGAAAG SSTGIMALRF LLGFLLAGVD LGVYLMRLEL
CDPTQRLRVA LAGELVGVGG HFLFLGLALV SKDWRFLQRM ITAPCILFLF YGWPGLFLES
ARWLIVKRQI EEAQSVLRIL AERNRPHGQM LGEEAQEALQ ELENTCPLPA TSTFSFASLL
NYRNIWKNLL ILGFTNFIAH AIRHCYQPVG GGGSPSDFYL CSLLASGTAA LACVFLGVTV
DRFGRRGILL LSMTLTGIAS LVLLGLWDYL NDAAITTFSV LGLFSSQASA ILSTLLASEV
IPTTVRGRGL GLIMALGALG GLSCPAQRLH MGHGAFLQHV VLAACALLCI LSIMLLPETK
RKLLPEVLRD GELCRRPSLL RQPPPNRCDH VPLLATPNPA L
