REG4_RAT
ID REG4_RAT Reviewed; 157 AA.
AC Q68AX7;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Regenerating islet-derived protein 4;
DE Short=REG-4;
DE Flags: Precursor;
GN Name=Reg4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Ileum;
RA Namikawa K., Murakami K., Fukushima M., Kiyama H.;
RT "Differential regulation of Reg family member expression after peripheral
RT nerve injury.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-independent lectin displaying mannose-binding
CC specificity and able to maintain carbohydrate recognition activity in
CC an acidic environment. May be involved in inflammatory and metaplastic
CC responses of the gastrointestinal epithelium (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR EMBL; AB164049; BAD38673.1; -; mRNA.
DR RefSeq; NP_001004096.1; NM_001004096.1.
DR RefSeq; XP_006233071.1; XM_006233009.3.
DR RefSeq; XP_008759543.1; XM_008761321.2.
DR RefSeq; XP_017446498.1; XM_017591009.1.
DR AlphaFoldDB; Q68AX7; -.
DR SMR; Q68AX7; -.
DR STRING; 10116.ENSRNOP00000025821; -.
DR GlyGen; Q68AX7; 3 sites.
DR PaxDb; Q68AX7; -.
DR Ensembl; ENSRNOT00000025821; ENSRNOP00000025821; ENSRNOG00000019046.
DR GeneID; 445583; -.
DR KEGG; rno:445583; -.
DR UCSC; RGD:1303341; rat.
DR CTD; 83998; -.
DR RGD; 1303341; Reg4.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000161011; -.
DR HOGENOM; CLU_049894_10_1_1; -.
DR InParanoid; Q68AX7; -.
DR OMA; WNSNECN; -.
DR OrthoDB; 1509611at2759; -.
DR PhylomeDB; Q68AX7; -.
DR PRO; PR:Q68AX7; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000019046; Expressed in jejunum and 11 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; ISO:RGD.
DR GO; GO:2001065; F:mannan binding; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Lectin; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..157
FT /note="Regenerating islet-derived protein 4"
FT /id="PRO_0000017439"
FT DOMAIN 36..154
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 97..101
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 134..136
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 57..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 128..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 157 AA; 18269 MW; 55B129FB10BA4D1D CRC64;
MASKCVRLLL LLSWVAGPEV LSDILRPSCA SGWFNYRSHC YGYFRKLRNW SHAELECQSY
GNGSHLASVL NPKEASVISK YITGYQRSLP VWIGLHDPQK NASWQWIDGS TNQYRPWSPR
TKSEARHCTE MNPKDKFLTW NKNGCTKRQH FLCKYRP