CUZD1_HUMAN
ID CUZD1_HUMAN Reviewed; 607 AA.
AC Q86UP6; A8K080; B2RN93; D3DRE5; Q7Z660; Q7Z661; Q86SG1; Q86UP5; Q9HAR7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=CUB and zona pellucida-like domain-containing protein 1 {ECO:0000305};
DE Short=CUB and ZP domain-containing protein 1;
DE AltName: Full=Transmembrane protein UO-44;
DE Flags: Precursor;
GN Name=CUZD1 {ECO:0000312|EMBL:CAH70006.1}; ORFNames=UNQ224/PRO257;
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] {ECO:0000305, ECO:0000312|EMBL:AAP15458.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15184879; DOI=10.1038/sj.onc.1207754;
RA Leong C.T.C., Ng C.Y., Ng C.P., Ma Z.S., Nguyen T.H., Tay S.K., Huynh H.;
RT "Molecular cloning, characterization and isolation of novel spliced
RT variants of the human ortholog of a rat estrogen-regulated membrane-
RT associated protein, UO-44.";
RL Oncogene 23:5707-5718(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAQ88920.1}
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Urinary bladder;
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 [4] {ECO:0000312|EMBL:CAH70006.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5] {ECO:0000305, ECO:0000312|EMBL:CAD98079.2}
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 151-607 (ISOFORM 1).
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
CC -!- FUNCTION: Localized to zymogen granules, where it functions in
CC trypsinogen activation (By similarity). May indirectly regulate cell
CC motility, cell-cell and cell/extracellular matrix interactions
CC (PubMed:15184879). {ECO:0000250|UniProtKB:P70412,
CC ECO:0000269|PubMed:15184879}.
CC -!- SUBCELLULAR LOCATION: Zymogen granule membrane
CC {ECO:0000250|UniProtKB:P70412}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P70412}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:15184879}; Synonyms=UO-44D
CC {ECO:0000269|PubMed:15184879};
CC IsoId=Q86UP6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15184879}; Synonyms=UO-44B
CC {ECO:0000269|PubMed:15184879}, UO-44C {ECO:0000269|PubMed:15184879};
CC IsoId=Q86UP6-2; Sequence=VSP_052019;
CC Name=3 {ECO:0000269|PubMed:15184879}; Synonyms=UO-44A
CC {ECO:0000269|PubMed:15184879};
CC IsoId=Q86UP6-3; Sequence=VSP_052018;
CC -!- TISSUE SPECIFICITY: Detected in pancreas and epithelium of ovary.
CC Expressed at higher levels in ovarian tumors than in normal tissue.
CC {ECO:0000269|PubMed:15184879}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23215.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY260047; AAP15458.1; -; mRNA.
DR EMBL; AY260048; AAP15459.1; -; mRNA.
DR EMBL; AY260049; AAP15460.1; -; mRNA.
DR EMBL; AY260050; AAP15461.1; -; mRNA.
DR EMBL; AF305835; AAG23215.1; ALT_FRAME; mRNA.
DR EMBL; AY358556; AAQ88920.1; -; mRNA.
DR EMBL; AK289445; BAF82134.1; -; mRNA.
DR EMBL; AL359747; CAH70003.1; -; Genomic_DNA.
DR EMBL; AL359747; CAH70004.1; -; Genomic_DNA.
DR EMBL; AL359747; CAH70006.1; -; Genomic_DNA.
DR EMBL; AC073585; CAH70006.1; JOINED; Genomic_DNA.
DR EMBL; CH471066; EAW49302.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49303.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49304.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49305.1; -; Genomic_DNA.
DR EMBL; BC136755; AAI36756.1; -; mRNA.
DR EMBL; BX538283; CAD98079.2; -; mRNA.
DR EMBL; BX538284; CAD98080.2; -; mRNA.
DR CCDS; CCDS7631.1; -. [Q86UP6-1]
DR RefSeq; NP_071317.2; NM_022034.5. [Q86UP6-1]
DR AlphaFoldDB; Q86UP6; -.
DR SMR; Q86UP6; -.
DR BioGRID; 119100; 1.
DR IntAct; Q86UP6; 1.
DR STRING; 9606.ENSP00000357900; -.
DR GlyGen; Q86UP6; 5 sites.
DR iPTMnet; Q86UP6; -.
DR PhosphoSitePlus; Q86UP6; -.
DR BioMuta; CUZD1; -.
DR DMDM; 74750426; -.
DR EPD; Q86UP6; -.
DR MassIVE; Q86UP6; -.
DR PaxDb; Q86UP6; -.
DR PeptideAtlas; Q86UP6; -.
DR PRIDE; Q86UP6; -.
DR ProteomicsDB; 69848; -. [Q86UP6-1]
DR ProteomicsDB; 69849; -. [Q86UP6-2]
DR ProteomicsDB; 69850; -. [Q86UP6-3]
DR Antibodypedia; 62632; 148 antibodies from 16 providers.
DR DNASU; 50624; -.
DR Ensembl; ENST00000392790.6; ENSP00000376540.1; ENSG00000138161.14. [Q86UP6-1]
DR GeneID; 50624; -.
DR KEGG; hsa:50624; -.
DR MANE-Select; ENST00000392790.6; ENSP00000376540.1; NM_022034.6; NP_071317.2.
DR UCSC; uc001lgs.4; human. [Q86UP6-1]
DR CTD; 50624; -.
DR DisGeNET; 50624; -.
DR GeneCards; CUZD1; -.
DR HGNC; HGNC:17937; CUZD1.
DR HPA; ENSG00000138161; Tissue enriched (pancreas).
DR MIM; 616644; gene.
DR neXtProt; NX_Q86UP6; -.
DR OpenTargets; ENSG00000138161; -.
DR PharmGKB; PA134903546; -.
DR VEuPathDB; HostDB:ENSG00000138161; -.
DR eggNOG; ENOG502RSDM; Eukaryota.
DR GeneTree; ENSGT00940000154525; -.
DR HOGENOM; CLU_024908_1_0_1; -.
DR InParanoid; Q86UP6; -.
DR OMA; CEMEYNS; -.
DR OrthoDB; 776870at2759; -.
DR PhylomeDB; Q86UP6; -.
DR TreeFam; TF351216; -.
DR PathwayCommons; Q86UP6; -.
DR SignaLink; Q86UP6; -.
DR BioGRID-ORCS; 50624; 7 hits in 1072 CRISPR screens.
DR GeneWiki; CUZD1; -.
DR GenomeRNAi; 50624; -.
DR Pharos; Q86UP6; Tbio.
DR PRO; PR:Q86UP6; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q86UP6; protein.
DR Bgee; ENSG00000138161; Expressed in body of pancreas and 95 other tissues.
DR ExpressionAtlas; Q86UP6; baseline and differential.
DR Genevisible; Q86UP6; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0042589; C:zymogen granule membrane; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032023; P:trypsinogen activation; ISS:UniProtKB.
DR CDD; cd00041; CUB; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS51034; ZP_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell cycle; Cell division;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..607
FT /note="CUB and zona pellucida-like domain-containing
FT protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000233331"
FT TOPO_DOM 25..568
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P70412"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P70412"
FT DOMAIN 25..146
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 154..265
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 276..519
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 17..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 85..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 154..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 207..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 442..498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT VAR_SEQ 1..366
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15184879"
FT /id="VSP_052018"
FT VAR_SEQ 1..281
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15184879"
FT /id="VSP_052019"
FT VARIANT 156
FT /note="G -> S (in dbSNP:rs35120257)"
FT /id="VAR_061992"
FT CONFLICT 235
FT /note="T -> P (in Ref. 7; CAD98079)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="V -> A (in Ref. 7; CAD98079)"
FT /evidence="ECO:0000305"
FT CONFLICT 494..495
FT /note="VY -> AC (in Ref. 1; AAG23215)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="E -> G (in Ref. 7; CAD98080)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="T -> I (in Ref. 7; CAD98080)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 68153 MW; 098A365612251C5E CRC64;
MELVRRLMPL TLLILSCLAE LTMAEAEGNA SCTVSLGGAN MAETHKAMIL QLNPSENCTW
TIERPENKSI RIIFSYVQLD PDGSCESENI KVFDGTSSNG PLLGQVCSKN DYVPVFESSS
STLTFQIVTD SARIQRTVFV FYYFFSPNIS IPNCGGYLDT LEGSFTSPNY PKPHPELAYC
VWHIQVEKDY KIKLNFKEIF LEIDKQCKFD FLAIYDGPST NSGLIGQVCG RVTPTFESSS
NSLTVVLSTD YANSYRGFSA SYTSIYAENI NTTSLTCSSD RMRVIISKSY LEAFNSNGNN
LQLKDPTCRP KLSNVVEFSV PLNGCGTIRK VEDQSITYTN IITFSASSTS EVITRQKQLQ
IIVKCEMGHN STVEIIYITE DDVIQSQNAL GKYNTSMALF ESNSFEKTIL ESPYYVDLNQ
TLFVQVSLHT SDPNLVVFLD TCRASPTSDF ASPTYDLIKS GCSRDETCKV YPLFGHYGRF
QFNAFKFLRS MSSVYLQCKV LICDSSDHQS RCNQGCVSRS KRDISSYKWK TDSIIGPIRL
KRDRSASGNS GFQHETHAEE TPNQPFNSVH LFSFMVLALN VVTVATITVR HFVNQRADYK
YQKLQNY
