KAZD1_MOUSE
ID KAZD1_MOUSE Reviewed; 313 AA.
AC Q8BJ66; Q14BR9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Kazal-type serine protease inhibitor domain-containing protein 1;
DE AltName: Full=Bone and odontoblast-expressed protein 1;
DE AltName: Full=Insulin-like growth factor-binding-related protein 10;
DE Short=IGFBP-rP10;
DE Short=IGFBP-related protein 10;
DE AltName: Full=Insulin-like growth factor-binding-related protein 4;
DE Flags: Precursor;
GN Name=Kazald1; Synonyms=Bono1, Igfbprp10;
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=Head;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15261838; DOI=10.1016/j.modgep.2004.01.013;
RA James M.J., Jaervinen E., Thesleff I.;
RT "Bono1: a gene associated with regions of deposition of bone and dentine.";
RL Gene Expr. Patterns 4:595-599(2004).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15555553; DOI=10.1016/j.bbrc.2004.10.157;
RA Shibata Y., Tsukazaki T., Hirata K., Xin C., Yamaguchi A.;
RT "Role of a new member of IGFBP superfamily, IGFBP-rP10, in proliferation
RT and differentiation of osteoblastic cells.";
RL Biochem. Biophys. Res. Commun. 325:1194-1200(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18757743; DOI=10.1073/pnas.0803640105;
RA Manabe R., Tsutsui K., Yamada T., Kimura M., Nakano I., Shimono C.,
RA Sanzen N., Furutani Y., Fukuda T., Oguri Y., Shimamoto K., Kiyozumi D.,
RA Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S., Kawai J., Sugiura N.,
RA Kimata K., Hayashizaki Y., Sekiguchi K.;
RT "Transcriptome-based systematic identification of extracellular matrix
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12849-12854(2008).
CC -!- FUNCTION: Involved in the proliferation of osteoblasts during bone
CC formation and bone regeneration. Promotes matrix assembly.
CC {ECO:0000269|PubMed:15555553, ECO:0000269|PubMed:18757743}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:18757743}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the spleen. Moderately
CC expressed in the skin, lung and urinary bladder. Weakly expressed in
CC the brain, tongue, esophagus, stomach, large intestine, liver and bone.
CC Expressed in osteoblastic cells during bone regeneration. Expressed in
CC secretory osteoblasts in the tooth. {ECO:0000269|PubMed:15261838,
CC ECO:0000269|PubMed:15555553}.
CC -!- DEVELOPMENTAL STAGE: At 15 dpc embryos, weakly expressed in osteoblasts
CC within the distal area of the ossification center of the mid-shaft
CC region of the ulna and the radius. At 16 dpc embryos highly expressed
CC in mandible, maxilla, frontal bone and ossification regions of the
CC nasal septum. At 17 dpc embryos expression is localized to developing
CC mandibular and maxillar bones, the frontal bones and in the nasal
CC capsule surrounding the nasopharynx. Expression throughout the
CC developing mandibular bone is found in 15 dpc-17 dpc embryos. Present
CC in periosteum of the humerus at 16.5 dpc (at protein level).
CC {ECO:0000269|PubMed:15261838, ECO:0000269|PubMed:18757743}.
CC -!- INDUCTION: Up-regulated during the early phase of the bone
CC regeneration. Up-regulated by BMP2 during osteoblast differentiation.
CC {ECO:0000269|PubMed:15555553}.
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DR EMBL; AK030678; BAC27075.1; -; mRNA.
DR EMBL; CH466534; EDL41948.1; -; Genomic_DNA.
DR EMBL; BC115642; AAI15643.1; -; mRNA.
DR CCDS; CCDS29857.1; -.
DR RefSeq; NP_849260.2; NM_178929.4.
DR RefSeq; XP_006526629.1; XM_006526566.2.
DR RefSeq; XP_006526630.1; XM_006526567.2.
DR RefSeq; XP_006526631.1; XM_006526568.2.
DR RefSeq; XP_017173531.1; XM_017318042.1.
DR AlphaFoldDB; Q8BJ66; -.
DR SMR; Q8BJ66; -.
DR STRING; 10090.ENSMUSP00000107579; -.
DR GlyGen; Q8BJ66; 3 sites.
DR PaxDb; Q8BJ66; -.
DR PRIDE; Q8BJ66; -.
DR ProteomicsDB; 269181; -.
DR Antibodypedia; 1720; 61 antibodies from 17 providers.
DR DNASU; 107250; -.
DR Ensembl; ENSMUST00000026234; ENSMUSP00000026234; ENSMUSG00000025213.
DR Ensembl; ENSMUST00000111948; ENSMUSP00000107579; ENSMUSG00000025213.
DR GeneID; 107250; -.
DR KEGG; mmu:107250; -.
DR UCSC; uc008hqs.2; mouse.
DR CTD; 81621; -.
DR MGI; MGI:2147606; Kazald1.
DR VEuPathDB; HostDB:ENSMUSG00000025213; -.
DR eggNOG; ENOG502R5QG; Eukaryota.
DR GeneTree; ENSGT00530000063555; -.
DR HOGENOM; CLU_075590_1_0_1; -.
DR InParanoid; Q8BJ66; -.
DR OMA; SPPYDTW; -.
DR OrthoDB; 994901at2759; -.
DR PhylomeDB; Q8BJ66; -.
DR TreeFam; TF331645; -.
DR BioGRID-ORCS; 107250; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q8BJ66; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8BJ66; protein.
DR Bgee; ENSMUSG00000025213; Expressed in epithelium of cochlear duct and 153 other tissues.
DR Genevisible; Q8BJ66; MM.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005614; C:interstitial matrix; IDA:MGI.
DR GO; GO:0005520; F:insulin-like growth factor binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR011390; IGFBP_rP_mac25.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR PANTHER; PTHR14186; PTHR14186; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR PIRSF; PIRSF018239; IGFBP_rP_mac25; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51323; IGFBP_N_2; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Immunoglobulin domain; Osteogenesis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..313
FT /note="Kazal-type serine protease inhibitor domain-
FT containing protein 1"
FT /id="PRO_0000015077"
FT DOMAIN 56..131
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 127..177
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 179..276
FT /note="Ig-like C2-type"
FT REGION 290..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 200..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 66..67
FT /note="EE -> KK (in Ref. 1; BAC27075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 34272 MW; DD1C117EBED4A0FC CRC64;
MPRVFTGLPA NYAAPTLALS LLLPLLLVVW TQLPVSARPS TGPDYLRRGW LRLLAEGEGC
APCRPEECAA PRGCLAGRVR DACGCCWECA NLEGQLCDLD PSANFYGRCG EQLECRLDAG
GDLSRGEVPE PLCVCRSQRP LCGSDGRTYA QICRLQEAAR ARLDANLTVV HPGPCESEPQ
ILSQPHNIWN VTGQDVIFGC EVFAYPMASI EWRKDGLDIQ LPGDDPHISV QFRGGPQKFE
VTGWLQIQAL RPSDEGTYRC LARNALGQAE ASATLTVLTP EQLNATGFSQ LQSRSLFPEE
EEEAESEELG DYY
