REG4_MOUSE
ID REG4_MOUSE Reviewed; 157 AA.
AC Q9D8G5; Q3TS25; Q9D858;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Regenerating islet-derived protein 4;
DE Short=REG-4;
DE Flags: Precursor;
GN Name=Reg4;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon, and Small intestine;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
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; AK008049; BAB25429.1; -; mRNA.
DR EMBL; AK008438; BAB25669.1; -; mRNA.
DR EMBL; AK162316; BAE36851.1; -; mRNA.
DR EMBL; BC019465; AAH19465.1; -; mRNA.
DR CCDS; CCDS17661.1; -.
DR RefSeq; NP_080604.2; NM_026328.2.
DR AlphaFoldDB; Q9D8G5; -.
DR SMR; Q9D8G5; -.
DR STRING; 10090.ENSMUSP00000029469; -.
DR GlyGen; Q9D8G5; 2 sites.
DR iPTMnet; Q9D8G5; -.
DR PhosphoSitePlus; Q9D8G5; -.
DR MaxQB; Q9D8G5; -.
DR PaxDb; Q9D8G5; -.
DR PeptideAtlas; Q9D8G5; -.
DR PRIDE; Q9D8G5; -.
DR ProteomicsDB; 253202; -.
DR Antibodypedia; 46951; 208 antibodies from 27 providers.
DR Ensembl; ENSMUST00000029469; ENSMUSP00000029469; ENSMUSG00000027876.
DR GeneID; 67709; -.
DR KEGG; mmu:67709; -.
DR UCSC; uc008qpq.1; mouse.
DR CTD; 83998; -.
DR MGI; MGI:1914959; Reg4.
DR VEuPathDB; HostDB:ENSMUSG00000027876; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000161011; -.
DR HOGENOM; CLU_049894_10_1_1; -.
DR InParanoid; Q9D8G5; -.
DR OMA; WNSNECN; -.
DR OrthoDB; 1509611at2759; -.
DR PhylomeDB; Q9D8G5; -.
DR BioGRID-ORCS; 67709; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Reg4; mouse.
DR PRO; PR:Q9D8G5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D8G5; protein.
DR Bgee; ENSMUSG00000027876; Expressed in crypt of Lieberkuhn of small intestine and 42 other tissues.
DR Genevisible; Q9D8G5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:2001065; F:mannan binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
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_0000017438"
FT DOMAIN 36..154
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 97..102
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 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"
FT CONFLICT 3
FT /note="S -> Y (in Ref. 1; BAB25669)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 157 AA; 18398 MW; F3981722BBD83968 CRC64;
MASKGVRLLL LLSWVAGPEV LSDILRPSCA PGWFYYRSHC YGYFRKLRNW SHAELECQSY
GNGSHLASVL NQKEASVISK YITGYQRNLP VWIGLHDPQK KQLWQWTDGS TNLYRRWNPR
TKSEARHCAE MNPKDKFLTW NKNGCANRQH FLCKYKT
