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Hepatitis A virus cellular receptor 1 (HAVcr-1) (Kidney injury molecule 1) (KIM-1) (T-cell immunoglobulin and mucin domain-containing protein 1) (TIMD-1) (T-cell immunoglobulin mucin receptor 1) (TIM) (TIM-1) (T-cell membrane protein 1)

 HAVR1_HUMAN             Reviewed;         359 AA.
Q96D42; O43656;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
30-AUG-2005, sequence version 2.
18-JUL-2018, entry version 136.
RecName: Full=Hepatitis A virus cellular receptor 1;
Short=HAVcr-1;
AltName: Full=Kidney injury molecule 1;
Short=KIM-1;
AltName: Full=T-cell immunoglobulin and mucin domain-containing protein 1;
Short=TIMD-1;
AltName: Full=T-cell immunoglobulin mucin receptor 1;
Short=TIM;
Short=TIM-1;
AltName: Full=T-cell membrane protein 1;
Flags: Precursor;
Name=HAVCR1; Synonyms=KIM1, TIM1, TIMD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION (MICROBIAL
INFECTION), AND INTERACTION WITH HEPATITIS A VIRUS CAPSID PROTEINS.
TISSUE=Liver;
PubMed=9658108;
Feigelstock D., Thompson P., Mattoo P., Zhang Y., Kaplan G.G.;
"The human homolog of HAVcr-1 codes for a hepatitis A virus cellular
receptor.";
J. Virol. 72:6621-6628(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT
MET-THR-THR-VAL-PRO-157 INS.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT
MET-THR-THR-VAL-PRO-157 INS.
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH IMMUNOGLUBULIN A.
PubMed=17229699; DOI=10.1128/JVI.01585-06;
Tami C., Silberstein E., Manangeeswaran M., Freeman G.J., Umetsu S.E.,
DeKruyff R.H., Umetsu D.T., Kaplan G.G.;
"Immunoglobulin A (IgA) is a natural ligand of hepatitis A virus
cellular receptor 1 (HAVCR1), and the association of IgA with HAVCR1
enhances virus-receptor interactions.";
J. Virol. 81:3437-3446(2007).
[6]
FUNCTION, AND INDUCTION.
PubMed=17471468; DOI=10.1002/path.2175;
van Timmeren M.M., van den Heuvel M.C., Bailly V., Bakker S.J.,
van Goor H., Stegeman C.A.;
"Tubular kidney injury molecule-1 (KIM-1) in human renal disease.";
J. Pathol. 212:209-217(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
FUNCTION (MICROBIAL INFECTION).
PubMed=21536871; DOI=10.1073/pnas.1019030108;
Kondratowicz A.S., Lennemann N.J., Sinn P.L., Davey R.A., Hunt C.L.,
Moller-Tank S., Meyerholz D.K., Rennert P., Mullins R.F., Brindley M.,
Sandersfeld L.M., Quinn K., Weller M., McCray P.B. Jr., Chiorini J.,
Maury W.;
"T-cell immunoglobulin and mucin domain 1 (TIM-1) is a receptor for
Zaire Ebolavirus and Lake Victoria Marburgvirus.";
Proc. Natl. Acad. Sci. U.S.A. 108:8426-8431(2011).
[9]
FUNCTION (MICROBIAL INFECTION).
PubMed=23084921; DOI=10.1016/j.chom.2012.08.009;
Meertens L., Carnec X., Lecoin M.P., Ramdasi R., Guivel-Benhassine F.,
Lew E., Lemke G., Schwartz O., Amara A.;
"The TIM and TAM families of phosphatidylserine receptors mediate
dengue virus entry.";
Cell Host Microbe 12:544-557(2012).
[10]
POLYMORPHISM, AND VARIANTS MET-THR-THR-THR-VAL-PRO-157 INS AND THR-195
DEL.
PubMed=14534576; DOI=10.1038/425576a;
McIntire J.J., Umetsu S.E., Macaubas C., Hoyte E.G., Cinnioglu C.,
Cavalli-Sforza L.L., Barsh G.S., Hallmayer J.F., Underhill P.A.,
Risch N.J., Freeman G.J., DeKruyff R.H., Umetsu D.T.;
"Hepatitis A virus link to atopic disease.";
Nature 425:576-576(2003).
[11]
VARIANT MET-THR-THR-VAL-PRO-157 INS.
Umetsu D.T.;
Submitted (SEP-2005) to UniProtKB.
-!- FUNCTION: May play a role in T-helper cell development and the
regulation of asthma and allergic diseases. Receptor for TIMD4 (By
similarity). May play a role in kidney injury and repair.
{ECO:0000250, ECO:0000269|PubMed:17471468}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for Hepatitis A
virus. {ECO:0000269|PubMed:9658108}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for Ebolavirus
and Marburg virus by binding exposed phosphatidyl-serine at the
surface of virion membrane. {ECO:0000269|PubMed:21536871}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for Dengue
virus by binding exposed phosphatidyl-serine at the surface of
virion membrane. {ECO:0000269|PubMed:23084921}.
-!- SUBUNIT: (Microbial infection) Interacts with hepatitis A virus
capsid proteins. {ECO:0000269|PubMed:9658108}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Widely expressed, with highest levels in
kidney and testis. Expressed by activated CD4+ T-cells during the
development of helper T-cells responses.
{ECO:0000269|PubMed:9658108}.
-!- INDUCTION: Up-regulated in the kidney in renal diseases (at
protein level). {ECO:0000269|PubMed:17471468}.
-!- POLYMORPHISM: Infection by hepatitis A virus (HAV) protects
individuals from atopy if they carry insertion of the variants
Met-Thr-Thr-Val-Pro-157 and Met-Thr-Thr-Thr-Val-Pro-157.
Modernisation has led to a reduction in HAV seroprevalence and
thus, may be, to an increase of expression of atopy, such as
asthma, allergic rhinitis and atopic dermatitis. Allelic variation
does not affect HAV-infection rates in Caucasians, Asians and
African Americans. {ECO:0000269|PubMed:14534576}.
-!- MISCELLANEOUS: The extracellular part of the protein can be
cleaved and detected in urine and is in correlation with the
expression in the kidney.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. TIM family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF043724; AAC39862.1; -; mRNA.
EMBL; CR457114; CAG33395.1; -; mRNA.
EMBL; AC026777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC013325; AAH13325.1; -; mRNA.
RefSeq; NP_001166864.1; NM_001173393.2.
RefSeq; NP_001295085.1; NM_001308156.1.
RefSeq; NP_036338.2; NM_012206.3.
UniGene; Hs.129711; -.
PDB; 5DZO; X-ray; 1.30 A; A=22-127.
PDB; 5F70; X-ray; 1.80 A; A=21-123.
PDBsum; 5DZO; -.
PDBsum; 5F70; -.
ProteinModelPortal; Q96D42; -.
SMR; Q96D42; -.
BioGrid; 117812; 1.
IntAct; Q96D42; 3.
STRING; 9606.ENSP00000344844; -.
iPTMnet; Q96D42; -.
PhosphoSitePlus; Q96D42; -.
BioMuta; HAVCR1; -.
DMDM; 73919877; -.
MaxQB; Q96D42; -.
PaxDb; Q96D42; -.
PeptideAtlas; Q96D42; -.
PRIDE; Q96D42; -.
ProteomicsDB; 76250; -.
DNASU; 26762; -.
Ensembl; ENST00000339252; ENSP00000344844; ENSG00000113249.
Ensembl; ENST00000523175; ENSP00000427898; ENSG00000113249.
GeneID; 26762; -.
KEGG; hsa:26762; -.
UCSC; uc003lwi.3; human.
CTD; 26762; -.
DisGeNET; 26762; -.
EuPathDB; HostDB:ENSG00000113249.12; -.
GeneCards; HAVCR1; -.
HGNC; HGNC:17866; HAVCR1.
HPA; CAB075697; -.
HPA; HPA007173; -.
MalaCards; HAVCR1; -.
MIM; 606518; gene.
neXtProt; NX_Q96D42; -.
PharmGKB; PA134924567; -.
eggNOG; ENOG410IZDR; Eukaryota.
eggNOG; ENOG410YSF7; LUCA.
InParanoid; Q96D42; -.
KO; K20413; -.
PhylomeDB; Q96D42; -.
TreeFam; TF336163; -.
ChiTaRS; HAVCR1; human.
GeneWiki; HAVCR1; -.
GenomeRNAi; 26762; -.
PRO; PR:Q96D42; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113249; -.
CleanEx; HS_HAVCR1; -.
ExpressionAtlas; Q96D42; baseline and differential.
Genevisible; Q96D42; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031514; C:motile cilium; IDA:CACAO.
GO; GO:0001618; F:virus receptor activity; IDA:CACAO.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction;
Immunoglobulin domain; Membrane; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 359 Hepatitis A virus cellular receptor 1.
/FTId=PRO_0000014981.
TOPO_DOM 21 290 Extracellular. {ECO:0000255}.
TRANSMEM 291 311 Helical. {ECO:0000255}.
TOPO_DOM 312 359 Cytoplasmic. {ECO:0000255}.
DOMAIN 21 121 Ig-like V-type.
REPEAT 138 143 1.
REPEAT 144 149 2.
REPEAT 150 155 3.
REPEAT 156 160 4.
REPEAT 161 166 5.
REPEAT 167 172 6.
REPEAT 173 178 7.
REPEAT 179 184 8.
REPEAT 185 190 9.
REPEAT 191 196 10.
REPEAT 197 202 11.
REGION 138 202 11 X 6 AA approximate tandem repeats of
V-P-T-T-T-T].
COMPBIAS 130 205 Thr-rich.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 286 286 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 105 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 46 57 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 52 104 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VARIANT 51 51 S -> L (in dbSNP:rs2270922).
/FTId=VAR_056080.
VARIANT 157 157 P -> PMTTTVP.
/FTId=VAR_023321.
VARIANT 157 157 P -> PMTTVP.
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.11, ECO:0000269|Ref.2}.
/FTId=VAR_023322.
VARIANT 195 195 Missing. {ECO:0000269|PubMed:14534576}.
/FTId=VAR_023323.
CONFLICT 174 174 L -> P (in Ref. 1; AAC39862).
{ECO:0000305}.
STRAND 22 30 {ECO:0000244|PDB:5DZO}.
STRAND 32 34 {ECO:0000244|PDB:5DZO}.
STRAND 45 50 {ECO:0000244|PDB:5DZO}.
TURN 56 59 {ECO:0000244|PDB:5DZO}.
STRAND 60 64 {ECO:0000244|PDB:5DZO}.
STRAND 66 74 {ECO:0000244|PDB:5DZO}.
HELIX 83 85 {ECO:0000244|PDB:5DZO}.
STRAND 90 94 {ECO:0000244|PDB:5DZO}.
HELIX 97 99 {ECO:0000244|PDB:5DZO}.
STRAND 101 107 {ECO:0000244|PDB:5DZO}.
STRAND 110 113 {ECO:0000244|PDB:5DZO}.
STRAND 116 125 {ECO:0000244|PDB:5DZO}.
SEQUENCE 359 AA; 38720 MW; D24BA2C932903ECA CRC64;
MHPQVVILSL ILHLADSVAG SVKVGGEAGP SVTLPCHYSG AVTSMCWNRG SCSLFTCQNG
IVWTNGTHVT YRKDTRYKLL GDLSRRDVSL TIENTAVSDS GVYCCRVEHR GWFNDMKITV
SLEIVPPKVT TTPIVTTVPT VTTVRTSTTV PTTTTVPTTT VPTTMSIPTT TTVLTTMTVS
TTTSVPTTTS IPTTTSVPVT TTVSTFVPPM PLPRQNHEPV ATSPSSPQPA ETHPTTLQGA
IRREPTSSPL YSYTTDGNDT VTESSDGLWN NNQTQLFLEH SLLTANTTKG IYAGVCISVL
VLLALLGVII AKKYFFKKEV QQLSVSFSSL QIKALQNAVE KEVQAEDNIY IENSLYATD


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