REG3G_HUMAN
ID REG3G_HUMAN Reviewed; 175 AA.
AC Q6UW15; A8K980; D6W5J6; Q3SYE4; Q3SYE6; Q6FH18;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Regenerating islet-derived protein 3-gamma;
DE Short=REG-3-gamma;
DE AltName: Full=Pancreatitis-associated protein 1B;
DE Short=PAP-1B;
DE AltName: Full=Pancreatitis-associated protein IB;
DE Short=PAP IB;
DE AltName: Full=Regenerating islet-derived protein III-gamma;
DE Short=REG III;
DE Short=Reg III-gamma;
DE Contains:
DE RecName: Full=Regenerating islet-derived protein 3-gamma 16.5 kDa form;
DE Contains:
DE RecName: Full=Regenerating islet-derived protein 3-gamma 15 kDa form;
DE Flags: Precursor;
GN Name=REG3G; Synonyms=PAP1B; ORFNames=UNQ429/PRO162;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=15556304; DOI=10.1016/j.gene.2004.06.010;
RA Nata K., Liu Y., Xu L., Ikeda T., Akiyama T., Noguchi N., Kawaguchi S.,
RA Yamauchi A., Takahashi I., Shervani N.J., Onogawa T., Takasawa S.,
RA Okamoto H.;
RT "Molecular cloning, expression and chromosomal localization of a novel
RT human REG family gene, REG III.";
RL Gene 340:161-170(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=15777617; DOI=10.1016/j.bbaexp.2005.01.011;
RA Laurine E., Manival X., Montgelard C., Bideau C., Berge-Lefranc J.-L.,
RA Erard M., Verdier J.-M.;
RT "PAP IB, a new member of the Reg gene family: cloning, expression,
RT structural properties, and evolution by gene duplication.";
RL Biochim. Biophys. Acta 1727:177-187(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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).
RN [9]
RP PROTEIN SEQUENCE OF N-TERMINUS, STRUCTURE BY NMR, FUNCTION, AND PROTEOLYTIC
RP PROCESSING.
RX PubMed=19095652; DOI=10.1074/jbc.m808077200;
RA Mukherjee S., Partch C.L., Lehotzky R.E., Whitham C.V., Chu H.,
RA Bevins C.L., Gardner K.H., Hooper L.V.;
RT "Regulation of C-type lectin antimicrobial activity by a flexible N-
RT terminal prosegment.";
RL J. Biol. Chem. 284:4881-4888(2009).
RN [10]
RP PROTEIN SEQUENCE OF 27-41.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
CC -!- FUNCTION: Bactericidal C-type lectin which acts exclusively against
CC Gram-positive bacteria and mediates bacterial killing by binding to
CC surface-exposed carbohydrate moieties of peptidoglycan. Restricts
CC bacterial colonization of the intestinal epithelial surface and
CC consequently limits activation of adaptive immune responses by the
CC microbiota. The uncleaved form has bacteriostatic activity, whereas the
CC cleaved form has bactericidal activity against L.monocytogenes and
CC methicillin-resistant S.aureus. Regulates keratinocyte proliferation
CC and differentiation after skin injury. {ECO:0000269|PubMed:19095652}.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6UW15-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UW15-2; Sequence=VSP_045169;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in pancreas, where it may
CC be restricted to exocrine pancreas. Moderate expression levels in
CC testis and weak in heart, kidney and placenta.
CC {ECO:0000269|PubMed:15556304, ECO:0000269|PubMed:15777617}.
CC -!- DOMAIN: The EPN motif is essential for recognition of the peptidoglycan
CC carbohydrate backbone and for efficient bacterial killing with Glu-114
CC playing a key role in peptidoglycan binding and bactericidal activity.
CC {ECO:0000250}.
CC -!- PTM: Proteolytic processing by trypsin removes an inhibitory N-terminal
CC propeptide and is essential for peptidoglycan binding and antibacterial
CC activity. {ECO:0000269|PubMed:19095652}.
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DR EMBL; AB161037; BAD51394.1; -; mRNA.
DR EMBL; AB161038; BAD51396.1; -; mRNA.
DR EMBL; AY428734; AAR88147.1; -; mRNA.
DR EMBL; AY359047; AAQ89406.1; -; mRNA.
DR EMBL; CR541938; CAG46736.1; -; mRNA.
DR EMBL; AB161039; BAD51395.1; -; Genomic_DNA.
DR EMBL; AK292595; BAF85284.1; -; mRNA.
DR EMBL; AC017004; AAX88840.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99580.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99581.1; -; Genomic_DNA.
DR EMBL; BC103852; AAI03853.1; -; mRNA.
DR EMBL; BC103853; AAI03854.1; -; mRNA.
DR EMBL; BC103854; AAI03855.1; -; mRNA.
DR CCDS; CCDS1962.1; -. [Q6UW15-1]
DR CCDS; CCDS58714.1; -. [Q6UW15-2]
DR RefSeq; NP_001008388.1; NM_001008387.2. [Q6UW15-1]
DR RefSeq; NP_001256969.1; NM_001270040.1. [Q6UW15-2]
DR RefSeq; NP_940850.1; NM_198448.3. [Q6UW15-1]
DR RefSeq; XP_005264192.1; XM_005264135.2. [Q6UW15-1]
DR AlphaFoldDB; Q6UW15; -.
DR SMR; Q6UW15; -.
DR BioGRID; 126224; 2.
DR STRING; 9606.ENSP00000272324; -.
DR BioMuta; REG3G; -.
DR DMDM; 68565895; -.
DR MassIVE; Q6UW15; -.
DR PaxDb; Q6UW15; -.
DR PeptideAtlas; Q6UW15; -.
DR PRIDE; Q6UW15; -.
DR ProteomicsDB; 61859; -.
DR ProteomicsDB; 67443; -. [Q6UW15-1]
DR Antibodypedia; 52910; 253 antibodies from 20 providers.
DR DNASU; 130120; -.
DR Ensembl; ENST00000272324.10; ENSP00000272324.5; ENSG00000143954.13. [Q6UW15-1]
DR Ensembl; ENST00000393897.6; ENSP00000377475.2; ENSG00000143954.13. [Q6UW15-1]
DR Ensembl; ENST00000409471.1; ENSP00000387105.1; ENSG00000143954.13. [Q6UW15-2]
DR GeneID; 130120; -.
DR KEGG; hsa:130120; -.
DR MANE-Select; ENST00000272324.10; ENSP00000272324.5; NM_001008387.3; NP_001008388.1.
DR UCSC; uc002snw.5; human. [Q6UW15-1]
DR CTD; 130120; -.
DR DisGeNET; 130120; -.
DR GeneCards; REG3G; -.
DR HGNC; HGNC:29595; REG3G.
DR HPA; ENSG00000143954; Tissue enriched (pancreas).
DR MIM; 609933; gene.
DR neXtProt; NX_Q6UW15; -.
DR OpenTargets; ENSG00000143954; -.
DR PharmGKB; PA142671087; -.
DR VEuPathDB; HostDB:ENSG00000143954; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162300; -.
DR HOGENOM; CLU_049894_18_0_1; -.
DR InParanoid; Q6UW15; -.
DR OMA; WEWSNAD; -.
DR OrthoDB; 1509611at2759; -.
DR PhylomeDB; Q6UW15; -.
DR PathwayCommons; Q6UW15; -.
DR Reactome; R-HSA-6803157; Antimicrobial peptides.
DR BioGRID-ORCS; 130120; 10 hits in 1028 CRISPR screens.
DR GeneWiki; REG3G; -.
DR GenomeRNAi; 130120; -.
DR Pharos; Q6UW15; Tbio.
DR PRO; PR:Q6UW15; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6UW15; protein.
DR Bgee; ENSG00000143954; Expressed in body of pancreas and 111 other tissues.
DR Genevisible; Q6UW15; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0070492; F:oligosaccharide binding; IDA:UniProtKB.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0044278; P:cell wall disruption in another organism; IDA:UniProtKB.
DR GO; GO:0051838; P:cytolysis by host of symbiont cells; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045617; P:negative regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
DR GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central.
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; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Acute phase; Alternative splicing; Antimicrobial; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Inflammatory response; Lectin;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:15340161,
FT ECO:0000269|PubMed:19095652"
FT CHAIN 27..175
FT /note="Regenerating islet-derived protein 3-gamma 16.5 kDa
FT form"
FT /id="PRO_0000017434"
FT PROPEP 27..37
FT /evidence="ECO:0000269|PubMed:19095652"
FT /id="PRO_0000422751"
FT CHAIN 38..175
FT /note="Regenerating islet-derived protein 3-gamma 15 kDa
FT form"
FT /id="PRO_0000422752"
FT DOMAIN 47..172
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 114..116
FT /note="EPN"
FT /evidence="ECO:0000250"
FT DISULFID 40..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 68..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 146..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 66..111
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045169"
FT CONFLICT 174
FT /note="K -> T (in Ref. 4; CAG46736)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 175 AA; 19330 MW; AF0F5FC59ACB90F5 CRC64;
MLPPMALPSV SWMLLSCLIL LCQVQGEETQ KELPSPRISC PKGSKAYGSP CYALFLSPKS
WMDADLACQK RPSGKLVSVL SGAEGSFVSS LVRSISNSYS YIWIGLHDPT QGSEPDGDGW
EWSSTDVMNY FAWEKNPSTI LNPGHCGSLS RSTGFLKWKD YNCDAKLPYV CKFKD
