ID HAVR1_CHLAE Reviewed; 478 AA. AC O46598; O18984; O46597; Q7JJ47; Q7JJ48; Q95144; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 2. DT 24-JAN-2024, entry version 100. DE RecName: Full=Hepatitis A virus cellular receptor 1; DE Short=HAVcr-1; DE AltName: Full=T-cell immunoglobulin and mucin domain-containing protein 1; DE Short=TIMD-1; DE AltName: Full=T-cell immunoglobulin mucin receptor 1; DE Short=TIM-1; DE AltName: Full=T-cell membrane protein 1; DE AltName: CD_antigen=CD365; DE Flags: Precursor; GN Name=HAVCR1; Synonyms=TIM1, TIMD1; OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=9534; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND FUNCTION AS A HAV RECEPTOR. RX PubMed=8861957; DOI=10.1002/j.1460-2075.1996.tb00803.x; RA Kaplan G.G., Totsuka A., Thompson P., Akatsuka T., Moritsugu Y., RA Feinstone S.M.; RT "Identification of a surface glycoprotein on African green monkey kidney RT cells as a receptor for hepatitis A virus."; RL EMBO J. 15:4282-4296(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). RX PubMed=9225030; DOI=10.1099/0022-1317-78-7-1565; RA Ashida M., Hamada C.; RT "Molecular cloning of the hepatitis A virus receptor from a simian cell RT line."; RL J. Gen. Virol. 78:1565-1569(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT). RX PubMed=9621093; DOI=10.1128/jvi.72.7.6218-6222.1998; RA Feigelstock D., Thompson P., Mattoo P., Kaplan G.G.; RT "Polymorphisms of the hepatitis A virus cellular receptor 1 in African RT green monkey kidney cells result in antigenic variants that do not react RT with protective monoclonal antibody 190/4."; RL J. Virol. 72:6218-6222(1998). RN [4] RP GLYCOSYLATION AT ASN-70 AND ASN-87. RX PubMed=9557657; DOI=10.1128/jvi.72.5.3751-3761.1998; RA Thompson P., Lu J., Kaplan G.G.; RT "The Cys-rich region of hepatitis A virus cellular receptor 1 is required RT for binding of hepatitis A virus and protective monoclonal antibody RT 190/4."; RL J. Virol. 72:3751-3761(1998). CC -!- FUNCTION: Phosphatidylserine receptor that plays an important CC functional role in regulatory B-cells homeostasis including generation, CC expansion and suppressor functions (By similarity). As P- CC selectin/SELPLG ligand, plays a specialized role in activated but not CC naive T-cell trafficking during inflammatory responses. Controls CC thereby T-cell accumulation in the inflamed central nervous system CC (CNS) and the induction of autoimmune disease (By similarity). CC Regulates also expression of various anti-inflammatory cytokines and CC co-inhibitory ligands including IL10. Acts as a regulator of T-cell CC proliferation (By similarity). May play a role in kidney injury and CC repair (By similarity). {ECO:0000250|UniProtKB:Q5QNS5, CC ECO:0000250|UniProtKB:Q96D42}. CC -!- SUBUNIT: Interacts with STAM. Interacts with SELPLG. CC {ECO:0000250|UniProtKB:Q96D42}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96D42}; CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q96D42}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=long; CC IsoId=O46598-1; Sequence=Displayed; CC Name=short; CC IsoId=O46598-2; Sequence=VSP_029086; CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. TIM family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X98252; CAA66906.1; -; mRNA. DR EMBL; D88585; BAA21556.1; -; mRNA. DR EMBL; AF043446; AAC39771.1; -; mRNA. DR EMBL; AF043447; AAC39772.1; -; mRNA. DR EMBL; AF043448; AAC39773.1; -; mRNA. DR EMBL; AF043449; AAC39774.1; -; mRNA. DR PIR; S71754; S71754. DR AlphaFoldDB; O46598; -. DR SMR; O46598; -. DR GlyCosmos; O46598; 4 sites, No reported glycans. DR iPTMnet; O46598; -. DR GO; GO:0031514; C:motile cilium; IDA:CACAO. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0001618; F:virus receptor activity; IMP:CACAO. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR PANTHER; PTHR47009:SF1; HEPATITIS A VIRUS CELLULAR RECEPTOR 1; 1. DR PANTHER; PTHR47009; HEPATITIS A VIRUS CELLULAR RECEPTOR 1 HOMOLOG; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein; KW Host cell receptor for virus entry; Host-virus interaction; KW Immunoglobulin domain; Membrane; Receptor; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..478 FT /note="Hepatitis A virus cellular receptor 1" FT /id="PRO_5000146882" FT TOPO_DOM 25..397 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 398..418 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 419..478 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 25..126 FT /note="Ig-like V-type" FT REPEAT 148..155 FT /note="1" FT REPEAT 156..161 FT /note="2" FT REPEAT 162..167 FT /note="3" FT REPEAT 168..173 FT /note="4" FT REPEAT 174..179 FT /note="5" FT REPEAT 180..185 FT /note="6" FT REPEAT 186..191 FT /note="7" FT REPEAT 192..197 FT /note="8" FT REPEAT 198..201 FT /note="9" FT REPEAT 202..207 FT /note="10" FT REPEAT 208..211 FT /note="11" FT REPEAT 212..217 FT /note="12" FT REPEAT 218..221 FT /note="13" FT REPEAT 222..227 FT /note="14" FT REPEAT 228..233 FT /note="15" FT REPEAT 234..239 FT /note="16" FT REPEAT 240..245 FT /note="17" FT REPEAT 246..251 FT /note="18" FT REPEAT 252..257 FT /note="19" FT REPEAT 258..263 FT /note="20" FT REPEAT 264..268 FT /note="21" FT REPEAT 269..273 FT /note="22" FT REPEAT 274..279 FT /note="23" FT REPEAT 280..285 FT /note="24" FT REPEAT 286..291 FT /note="25" FT REPEAT 292..297 FT /note="26" FT REPEAT 298..303 FT /note="27" FT REPEAT 304..309 FT /note="28" FT REGION 148..309 FT /note="28 X 6 AA approximate tandem repeats of L-P-[MT]-T- FT [MT]-T" FT REGION 187..303 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 320..339 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 344..370 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 70 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000305|PubMed:9557657" FT CARBOHYD 87 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000305|PubMed:9557657" FT CARBOHYD 379 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 393 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 41..110 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 51..62 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 57..109 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 1..5 FT /note="Missing (in isoform short)" FT /evidence="ECO:0000303|PubMed:8861957, FT ECO:0000303|PubMed:9225030, ECO:0000303|PubMed:9621093" FT /id="VSP_029086" FT CONFLICT 22 FT /note="S -> F (in Ref. 2; BAA21556)" FT /evidence="ECO:0000305" FT CONFLICT 53 FT /note="N -> H (in Ref. 3; AAC39771/AAC39772/AAC39773)" FT /evidence="ECO:0000305" FT CONFLICT 136 FT /note="I -> T (in Ref. 1; CAA66906)" FT /evidence="ECO:0000305" FT CONFLICT 153..154 FT /note="Missing (in Ref. 1; CAA66906)" FT /evidence="ECO:0000305" FT CONFLICT 172 FT /note="M -> T (in Ref. 1; CAA66906 and 2; BAA21556)" FT /evidence="ECO:0000305" FT CONFLICT 176 FT /note="T -> M (in Ref. 1; CAA66906)" FT /evidence="ECO:0000305" FT CONFLICT 194 FT /note="M -> T (in Ref. 2; BAA21556 and 1; CAA66906)" FT /evidence="ECO:0000305" FT CONFLICT 196..209 FT /note="Missing (in Ref. 1; CAA66906)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="Missing (in Ref. 2; BAA21556)" FT /evidence="ECO:0000305" FT CONFLICT 212..215 FT /note="Missing (in Ref. 3; AAC39771/AAC39772)" FT /evidence="ECO:0000305" FT CONFLICT 224 FT /note="T -> M (in Ref. 1; CAA66906)" FT /evidence="ECO:0000305" FT CONFLICT 232 FT /note="M -> R (in Ref. 1; CAA66906)" FT /evidence="ECO:0000305" FT CONFLICT 236 FT /note="M -> T (in Ref. 1; CAA66906)" FT /evidence="ECO:0000305" FT CONFLICT 240 FT /note="L -> I (in Ref. 3; AAC39771/AAC39772)" FT /evidence="ECO:0000305" FT CONFLICT 243 FT /note="T -> M (in Ref. 2; BAA21556)" FT /evidence="ECO:0000305" FT CONFLICT 244 FT /note="T -> M (in Ref. 1; CAA66906)" FT /evidence="ECO:0000305" FT CONFLICT 248 FT /note="T -> M (in Ref. 1; CAA66906)" FT /evidence="ECO:0000305" FT CONFLICT 257..268 FT /note="Missing (in Ref. 2; BAA21556)" FT /evidence="ECO:0000305" FT CONFLICT 283..290 FT /note="TMTLPMTT -> MM (in Ref. 1; CAA66906)" FT /evidence="ECO:0000305" FT CONFLICT 323 FT /note="D -> N (in Ref. 1; CAA66906 and 2; BAA21556)" FT /evidence="ECO:0000305" FT CONFLICT 334 FT /note="A -> P (in Ref. 1; CAA66906 and 2; BAA21556)" FT /evidence="ECO:0000305" SQ SEQUENCE 478 AA; 51490 MW; A2794438E8BAC379 CRC64; MADPIMHLQV VILSLILHLA DSVADSVNVD GVAGLSITLP CRYNGAITSM CWNRGTCSVF SCPDGIVWTN GTHVTYRKET RYKLLGNLSR RDVSLTIANT AVSDSGIYCC RVKHSGWFND MKITISLKIG PPRVTIPIVR TVRTSTTVPT TTTTTLPTTT TLPTTTTLPT TMTLPTTTTL PMTTTLPTTT TVPMTTTLPT TLPTTTTLPT TLPTTTTLPT TLPTTTTLPT TMTLPMTTTL PTTTTLPTTT TLPTTTTLPT TTTLPTTTLP TMTLPTTTTL PTTMTLPMTT TLPTTTTLPT TTTLPTTTMV STFVPPTPLP MQDHEPVATS PSSAQPAETH PVTLLGATRT QPTSSPLYSY TTDGSDTVTE SSDGLWNNNQ TQLSPEHSPQ MVNTTEGIYA GVCISVLVLL AVLGVVIAKK YFFKKEIQQL SVSFSNHQFK TLQNAVKKEV HAEDNIYIEN NLYAMNQDPV VLFESLRP //