CCBE1_MOUSE
ID CCBE1_MOUSE Reviewed; 408 AA.
AC Q3MI99; A7MCU5; Q5DTT5; Q8BFW1; Q8BMT1;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Collagen and calcium-binding EGF domain-containing protein 1;
DE AltName: Full=Full of fluid protein homolog;
DE Flags: Precursor;
GN Name=Ccbe1; Synonyms=Kiaa1983;
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=Embryo, Placenta, and Spinal cord;
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 MRNA].
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CD-1; TISSUE=Neural stem cell;
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).
CC -!- FUNCTION: Required for lymphangioblast budding and angiogenic sprouting
CC from venous endothelium during embryogenesis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CCBE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90476.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK028377; BAC25916.1; -; mRNA.
DR EMBL; AK035153; BAC28962.1; -; mRNA.
DR EMBL; AK039742; BAC30435.1; -; mRNA.
DR EMBL; AK220435; BAD90476.1; ALT_INIT; mRNA.
DR EMBL; BC103803; AAI03804.1; -; mRNA.
DR EMBL; BC152322; AAI52323.1; -; mRNA.
DR CCDS; CCDS29314.1; -.
DR RefSeq; NP_848908.1; NM_178793.4.
DR AlphaFoldDB; Q3MI99; -.
DR STRING; 10090.ENSMUSP00000117636; -.
DR GlyGen; Q3MI99; 2 sites.
DR iPTMnet; Q3MI99; -.
DR PhosphoSitePlus; Q3MI99; -.
DR MaxQB; Q3MI99; -.
DR PaxDb; Q3MI99; -.
DR PeptideAtlas; Q3MI99; -.
DR PRIDE; Q3MI99; -.
DR ProteomicsDB; 265703; -.
DR Antibodypedia; 22986; 190 antibodies from 28 providers.
DR DNASU; 320924; -.
DR Ensembl; ENSMUST00000061103; ENSMUSP00000052011; ENSMUSG00000046318.
DR Ensembl; ENSMUST00000130300; ENSMUSP00000117636; ENSMUSG00000046318.
DR GeneID; 320924; -.
DR KEGG; mmu:320924; -.
DR UCSC; uc008ffr.1; mouse.
DR CTD; 147372; -.
DR MGI; MGI:2445053; Ccbe1.
DR VEuPathDB; HostDB:ENSMUSG00000046318; -.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00390000014907; -.
DR HOGENOM; CLU_062964_0_0_1; -.
DR InParanoid; Q3MI99; -.
DR OMA; EDYDVCS; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; Q3MI99; -.
DR TreeFam; TF333138; -.
DR BioGRID-ORCS; 320924; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ccbe1; mouse.
DR PRO; PR:Q3MI99; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q3MI99; protein.
DR Bgee; ENSMUSG00000046318; Expressed in pericardium and 154 other tissues.
DR ExpressionAtlas; Q3MI99; baseline and differential.
DR Genevisible; Q3MI99; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0043542; P:endothelial cell migration; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0001945; P:lymph vessel development; IMP:MGI.
DR GO; GO:0001946; P:lymphangiogenesis; IMP:MGI.
DR GO; GO:1904977; P:lymphatic endothelial cell migration; IMP:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:BHF-UCL.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:MGI.
DR GO; GO:1901492; P:positive regulation of lymphangiogenesis; IDA:BHF-UCL.
DR GO; GO:0010954; P:positive regulation of protein processing; ISO:MGI.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:MGI.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; ISO:MGI.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IMP:MGI.
DR GO; GO:0003016; P:respiratory system process; IMP:MGI.
DR GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0048845; P:venous blood vessel morphogenesis; ISS:UniProtKB.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR Pfam; PF01391; Collagen; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Calcium; Collagen; Developmental protein; Disulfide bond;
KW EGF-like domain; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..408
FT /note="Collagen and calcium-binding EGF domain-containing
FT protein 1"
FT /id="PRO_0000279517"
FT DOMAIN 135..176
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 247..292
FT /note="Collagen-like 1"
FT DOMAIN 302..335
FT /note="Collagen-like 2"
FT REGION 246..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 139..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 147..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 162..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 77
FT /note="K -> E (in Ref. 2; BAD90476)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="P -> L (in Ref. 3; AAI03804)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="R -> Q (in Ref. 1; BAC25916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 44357 MW; E600004B6445EE88 CRC64;
MVPPPLPSRG GAAKRQLGKS LGPLLLLLAL GHTWTYREEP EDRDREVCSE NKITTTKYPC
LKSSGELTTC FRKKCCKGYK FVLGQCIPED YDICAQAPCE QQCTDNFGRV LCTCYPGYRY
DRERHQKRER PYCLDIDECA TSNTTLCAHI CINTMGSYHC ECREGYILED DGRTCTRGDK
YPNDTGHEEK SENEVKAGTC CATCKEFSQM KQTVLQLKQK MALLPNNAAE LGKYVNGDKV
LASNAYLPGP PGLPGGQGPP GSPGPKGSPG FPGMPGPPGQ PGPRGSMGPM GPSPDLSHIK
QGRRGPVGPP GAPGRHGSKG ERGAPGPPGS PGPPGSFDFL LLVLADIRND IAELQEKVFG
HRTHSSAEDF PLPQEFSSYP ETLDFGSGDD YSRRTEARDP EAPRNFYP
