CUZD1_MOUSE
ID CUZD1_MOUSE Reviewed; 607 AA.
AC P70412; B2RU69; Q9CTZ7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 120.
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=Integral membrane-associated protein 1;
DE Flags: Precursor;
GN Name=Cuzd1 {ECO:0000312|MGI:MGI:1202881};
GN Synonyms=Itmap1 {ECO:0000312|EMBL:AAC24898.2};
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] {ECO:0000305, ECO:0000312|EMBL:AAC24898.2}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=CF-1 {ECO:0000312|EMBL:AAC24898.2};
RC TISSUE=Uterus {ECO:0000312|EMBL:AAC24898.2};
RX PubMed=9480914; DOI=10.1042/bj3300947;
RA Kasik J.W.;
RT "A cDNA cloned from pregnant mouse uterus exhibits temporo-spatial
RT expression and predicts a novel protein.";
RL Biochem. J. 330:947-950(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAB31520.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-607.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB31520.1};
RC TISSUE=Pancreas {ECO:0000312|EMBL:BAB31520.1};
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 [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=12401800; DOI=10.1074/jbc.m204159200;
RA Imamura T., Asada M., Vogt S.K., Rudnick D.A., Lowe M.E., Muglia L.J.;
RT "Protection from pancreatitis by the zymogen granule membrane protein
RT integral membrane-associated protein-1.";
RL J. Biol. Chem. 277:50725-50733(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Localized to zymogen granules, where it functions in
CC trypsinogen activation (PubMed:12401800). May indirectly regulate cell
CC motility, cell-cell and cell/extracellular matrix interactions (By
CC similarity). {ECO:0000250|UniProtKB:Q86UP6,
CC ECO:0000269|PubMed:12401800}.
CC -!- SUBCELLULAR LOCATION: Zymogen granule membrane
CC {ECO:0000269|PubMed:12401800}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12401800}.
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreatic acinar cells. Also
CC expressed in epithelium of the uterus during late pregnancy but not
CC detected in non-pregnant uterus or in a variety of other adult and
CC fetal tissues. {ECO:0000269|PubMed:12401800,
CC ECO:0000269|PubMed:9480914}.
CC -!- DEVELOPMENTAL STAGE: First detected in uterus 6 days prior to birth,
CC increases daily to reach maximum levels 3 days before birth, abruptly
CC decreases during the last 3 days of pregnancy and is almost
CC undetectable by the first day after birth.
CC {ECO:0000269|PubMed:9480914}.
CC -!- DISRUPTION PHENOTYPE: Mice display increased severity of
CC secretagogue- and diet-induced pancreatitis which seems to be due to
CC impaired activation of trypsin. {ECO:0000269|PubMed:12401800}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24898.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U69699; AAC24898.2; ALT_FRAME; mRNA.
DR EMBL; AC110885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140992; AAI40993.1; -; mRNA.
DR EMBL; AK019038; BAB31520.1; -; mRNA.
DR CCDS; CCDS40157.1; -.
DR RefSeq; NP_032437.3; NM_008411.3.
DR AlphaFoldDB; P70412; -.
DR SMR; P70412; -.
DR STRING; 10090.ENSMUSP00000037168; -.
DR GlyGen; P70412; 4 sites.
DR PhosphoSitePlus; P70412; -.
DR MaxQB; P70412; -.
DR PaxDb; P70412; -.
DR PRIDE; P70412; -.
DR ProteomicsDB; 279303; -.
DR ProteomicsDB; 339066; -.
DR DNASU; 16433; -.
DR Ensembl; ENSMUST00000046611; ENSMUSP00000037168; ENSMUSG00000040205.
DR GeneID; 16433; -.
DR KEGG; mmu:16433; -.
DR UCSC; uc009kbc.1; mouse.
DR CTD; 50624; -.
DR MGI; MGI:1202881; Cuzd1.
DR VEuPathDB; HostDB:ENSMUSG00000040205; -.
DR eggNOG; KOG4292; Eukaryota.
DR GeneTree; ENSGT00940000154525; -.
DR HOGENOM; CLU_024908_1_0_1; -.
DR InParanoid; P70412; -.
DR OMA; CEMEYNS; -.
DR OrthoDB; 776870at2759; -.
DR TreeFam; TF351216; -.
DR BioGRID-ORCS; 16433; 2 hits in 72 CRISPR screens.
DR PRO; PR:P70412; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P70412; protein.
DR Bgee; ENSMUSG00000040205; Expressed in pyloric antrum and 46 other tissues.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0042588; C:zymogen granule; IDA:MGI.
DR GO; GO:0042589; C:zymogen granule membrane; IDA:MGI.
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:0007565; P:female pregnancy; NAS:UniProtKB.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISO:MGI.
DR GO; GO:0032023; P:trypsinogen activation; IMP: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 1: Evidence at protein level;
KW Cell adhesion; Cell cycle; Cell division; Cytoplasmic vesicle;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..607
FT /note="CUB and zona pellucida-like domain-containing
FT protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000233332"
FT TOPO_DOM 20..568
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:12401800"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12401800"
FT DOMAIN 20..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 22
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 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"
SQ SEQUENCE 607 AA; 68195 MW; 466A2AEFB7A070F1 CRC64;
MEVTGRLFIW AILAVSCGAQ LNSTEAEGKS RCTASLGGAN LGETHKALVL QLSANENCTW
TIERPENRSI RIIFSYIKLD PGSRCETENI KVFDGSSTSG PLLGKACSRN DFVPVFESSS
NSMTFQIVTG LTKFPRSVFI FYYFFSAATV IPNCGGDLRA LEGSFSSPNY PKPHPELAYC
VWHIQVGKGY KIQLKFTDLL LEMDENCKFD FIAVYDGPST TAGLLKQLCG RGKPTLESSS
DAMTVVLSTD YANSYKGFSA SYTSIYIHDV NTTSLSCVSD KMRVIISKSY LPALNYNESN
LQLNDPTCRP NVSNVIEFSI PLHECGTVKK IEDHAISYTN RITFIESPVS AVITRQKLLQ
IVVTCEMEYN STVEIMYITE DDIIQNQSVL GKYNTSLALY ESDSFENLVQ ESPYYVDLNQ
TLFVQATLHT SDPSLVVFLD TCRASPTSDF ASPTYDLISS GCCQDETCKV YPLFGHYGRF
QFNAFKFLKH LNSVYLKCKI LICDNNDQTS RCNQGCVPRR KRDIPSYKWK TDSVIGPIRL
KRDRSASRDS GLLPQIHEAE ISNQPLSRLY LFSFMVLALN VVIVAITTVK HFLNRWMDHR
YQKLQVY
