ID ZG16_HUMAN Reviewed; 167 AA. AC O60844; B2R4Z3; B9EK72; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2014, sequence version 2. DT 16-JAN-2019, entry version 130. DE RecName: Full=Zymogen granule membrane protein 16; DE Short=Zymogen granule protein 16; DE Short=hZG16; DE AltName: Full=Secretory lectin ZG16; DE Flags: Precursor; GN Name=ZG16; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-109. RC TISSUE=Colon adenocarcinoma; RA Hosokawa S., Kojima-Aikawa K.; RT "Carbohydrate-binding activity of ZG16p."; RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-109. RC TISSUE=Colon, and Rectum; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-109. RX PubMed=10493829; DOI=10.1006/geno.1999.5927; RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., RA Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., RA Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., RA Harris P.C., Venter J.C., Adams M.D.; RT "Genome duplications and other features in 12 Mb of DNA sequence from RT human chromosome 16p and 16q."; RL Genomics 60:295-308(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-109. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-32 AND RP VAL-109. RC 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 17-31. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally RT verified cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=17307141; DOI=10.1016/j.bbrc.2007.02.020; RA Zhou Y.B., Cao J.B., Yang H.M., Zhu H., Xu Z.G., Wang K.S., Zhang X., RA Wang Z.Q., Han Z.G.; RT "hZG16, a novel human secreted protein expressed in liver, was down- RT regulated in hepatocellular carcinoma."; RL Biochem. Biophys. Res. Commun. 355:679-686(2007). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 21-159. RX PubMed=21110947; DOI=10.1016/j.bbrc.2010.11.093; RA Kanagawa M., Satoh T., Ikeda A., Nakano Y., Yagi H., Kato K., RA Kojima-Aikawa K., Yamaguchi Y.; RT "Crystal structures of human secretory proteins ZG16p and ZG16b reveal RT a Jacalin-related beta-prism fold."; RL Biochem. Biophys. Res. Commun. 404:201-205(2011). CC -!- FUNCTION: May play a role in protein trafficking. May act as a CC linker molecule between the submembranous matrix on the luminal CC side of zymogen granule membrane (ZGM) and aggregated secretory CC proteins during granule formation in the TGN. CC {ECO:0000269|PubMed:17307141}. CC -!- INTERACTION: CC Q9UHX1:PUF60; NbExp=3; IntAct=EBI-746479, EBI-1053259; CC O43765:SGTA; NbExp=8; IntAct=EBI-746479, EBI-347996; CC Q96EQ0:SGTB; NbExp=4; IntAct=EBI-746479, EBI-744081; CC Q9UMX0:UBQLN1; NbExp=8; IntAct=EBI-746479, EBI-741480; CC Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-746479, EBI-10173939; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000269|PubMed:17307141}. Cytoplasmic vesicle lumen CC {ECO:0000305|PubMed:17307141}. Golgi apparatus lumen CC {ECO:0000269|PubMed:17307141}. Note=Stored in zymogen granules. CC {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Highly expressed in liver. Detected at lower CC levels in colon, ileum and jejunum. {ECO:0000269|PubMed:17307141}. CC -!- SIMILARITY: Belongs to the jacalin lectin family. CC {ECO:0000255|PROSITE-ProRule:PRU01088, 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; AB092813; BAC20361.1; -; mRNA. DR EMBL; AK312002; BAG34940.1; -; mRNA. DR EMBL; AK125559; BAG54214.1; -; mRNA. DR EMBL; AC009133; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC002301; AAC08708.1; -; Genomic_DNA. DR EMBL; CH471238; EAW80011.1; -; Genomic_DNA. DR EMBL; BC029149; AAH29149.1; -; mRNA. DR EMBL; BC150656; AAI50657.1; -; mRNA. DR CCDS; CCDS54000.1; -. DR RefSeq; NP_689551.2; NM_152338.3. DR UniGene; Hs.632195; -. DR PDB; 3APA; X-ray; 1.65 A; A=21-159. DR PDB; 3VY6; X-ray; 2.00 A; A=21-159. DR PDB; 3VY7; X-ray; 2.14 A; A=21-159. DR PDB; 3VZE; X-ray; 1.90 A; A=21-159. DR PDB; 3VZF; X-ray; 2.80 A; A=21-159. DR PDB; 3VZG; X-ray; 2.70 A; A=21-159. DR PDBsum; 3APA; -. DR PDBsum; 3VY6; -. DR PDBsum; 3VY7; -. DR PDBsum; 3VZE; -. DR PDBsum; 3VZF; -. DR PDBsum; 3VZG; -. DR ProteinModelPortal; O60844; -. DR SMR; O60844; -. DR BioGrid; 576089; 4. DR IntAct; O60844; 12. DR STRING; 9606.ENSP00000383563; -. DR UniLectin; O60844; -. DR iPTMnet; O60844; -. DR PhosphoSitePlus; O60844; -. DR BioMuta; ZG16; -. DR jPOST; O60844; -. DR PaxDb; O60844; -. DR PeptideAtlas; O60844; -. DR PRIDE; O60844; -. DR ProteomicsDB; 49629; -. DR Ensembl; ENST00000400752; ENSP00000383563; ENSG00000174992. DR GeneID; 653808; -. DR KEGG; hsa:653808; -. DR UCSC; uc002dtr.5; human. DR CTD; 653808; -. DR EuPathDB; HostDB:ENSG00000174992.7; -. DR GeneCards; ZG16; -. DR H-InvDB; HIX0012923; -. DR HGNC; HGNC:30961; ZG16. DR HPA; HPA052066; -. DR HPA; HPA052512; -. DR neXtProt; NX_O60844; -. DR PharmGKB; PA164727719; -. DR eggNOG; ENOG410IE5W; Eukaryota. DR eggNOG; ENOG41122DQ; LUCA. DR HOGENOM; HOG000015245; -. DR HOVERGEN; HBG079379; -. DR InParanoid; O60844; -. DR OrthoDB; 1305607at2759; -. DR PhylomeDB; O60844; -. DR TreeFam; TF333440; -. DR EvolutionaryTrace; O60844; -. DR GeneWiki; ZG16; -. DR GenomeRNAi; 653808; -. DR PRO; PR:O60844; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000174992; Expressed in 46 organ(s), highest expression level in sigmoid colon. DR Genevisible; O60844; HS. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB. DR GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005796; C:Golgi lumen; IDA:UniProtKB. DR GO; GO:0042589; C:zymogen granule membrane; IEA:Ensembl. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; TAS:UniProtKB. DR Gene3D; 2.100.10.30; -; 1. DR InterPro; IPR001229; Jacalin-like_lectin_dom. DR InterPro; IPR036404; Jacalin-like_lectin_dom_sf. DR InterPro; IPR033563; ZG16. DR PANTHER; PTHR33589:SF4; PTHR33589:SF4; 1. DR Pfam; PF01419; Jacalin; 1. DR SMART; SM00915; Jacalin; 1. DR SUPFAM; SSF51101; SSF51101; 1. DR PROSITE; PS51752; JACALIN_LECTIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasmic vesicle; KW Direct protein sequencing; Extracellular matrix; Golgi apparatus; KW Lectin; Polymorphism; Protein transport; Reference proteome; Secreted; KW Signal; Transport. FT SIGNAL 1 16 {ECO:0000269|PubMed:15340161}. FT CHAIN 17 167 Zymogen granule membrane protein 16. FT /FTId=PRO_0000017570. FT DOMAIN 24 159 Jacalin-type lectin. FT {ECO:0000255|PROSITE-ProRule:PRU01088}. FT VARIANT 32 32 G -> S (in dbSNP:rs235636). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_034587. FT VARIANT 109 109 L -> V. {ECO:0000269|PubMed:10493829, FT ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.1, ECO:0000269|Ref.5}. FT /FTId=VAR_070695. FT VARIANT 162 162 S -> T (in dbSNP:rs235638). FT /FTId=VAR_034588. FT STRAND 25 31 {ECO:0000244|PDB:3APA}. FT STRAND 35 39 {ECO:0000244|PDB:3APA}. FT HELIX 41 46 {ECO:0000244|PDB:3APA}. FT STRAND 48 56 {ECO:0000244|PDB:3APA}. FT STRAND 58 68 {ECO:0000244|PDB:3APA}. FT STRAND 79 87 {ECO:0000244|PDB:3APA}. FT STRAND 94 112 {ECO:0000244|PDB:3APA}. FT STRAND 117 121 {ECO:0000244|PDB:3APA}. FT STRAND 125 130 {ECO:0000244|PDB:3APA}. FT STRAND 138 158 {ECO:0000244|PDB:3APA}. SQ SEQUENCE 167 AA; 18147 MW; 247AE2FB4FC180A3 CRC64; MLTVALLALL CASASGNAIQ ARSSSYSGEY GGGGGKRFSH SGNQLDGPIT ALRVRVNTYY IVGLQVRYGK VWSDYVGGRN GDLEEIFLHP GESVIQVSGK YKWYLKKLLF VTDKGRYLSF GKDSGTSFNA VPLHPNTVLR FISGRSGSLI DAIGLHWDVY PSSCSRC //