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
//
