DCBD1_MOUSE
ID DCBD1_MOUSE Reviewed; 503 AA.
AC Q9D4J3; Q8R327; Q9D696;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Discoidin, CUB and LCCL domain-containing protein 1;
DE Flags: Precursor;
GN Name=Dcbld1;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Skin, and Testis;
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] (ISOFORM 2).
RC TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D4J3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D4J3-2; Sequence=VSP_010783;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29409.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK014521; BAB29409.1; ALT_INIT; mRNA.
DR EMBL; AK016485; BAB30265.1; -; mRNA.
DR EMBL; BC026771; AAH26771.1; -; mRNA.
DR CCDS; CCDS23839.1; -. [Q9D4J3-1]
DR CCDS; CCDS83696.1; -. [Q9D4J3-2]
DR RefSeq; NP_001334373.1; NM_001347444.1. [Q9D4J3-2]
DR RefSeq; NP_079981.2; NM_025705.4. [Q9D4J3-1]
DR AlphaFoldDB; Q9D4J3; -.
DR SMR; Q9D4J3; -.
DR STRING; 10090.ENSMUSP00000068203; -.
DR GlyGen; Q9D4J3; 2 sites.
DR iPTMnet; Q9D4J3; -.
DR PhosphoSitePlus; Q9D4J3; -.
DR MaxQB; Q9D4J3; -.
DR PaxDb; Q9D4J3; -.
DR PRIDE; Q9D4J3; -.
DR ProteomicsDB; 279831; -. [Q9D4J3-1]
DR ProteomicsDB; 279832; -. [Q9D4J3-2]
DR Antibodypedia; 46584; 21 antibodies from 10 providers.
DR DNASU; 66686; -.
DR Ensembl; ENSMUST00000069004; ENSMUSP00000068203; ENSMUSG00000019891. [Q9D4J3-1]
DR Ensembl; ENSMUST00000218582; ENSMUSP00000151265; ENSMUSG00000019891. [Q9D4J3-2]
DR GeneID; 66686; -.
DR KEGG; mmu:66686; -.
DR UCSC; uc007fbd.2; mouse. [Q9D4J3-1]
DR UCSC; uc007fbe.2; mouse. [Q9D4J3-2]
DR CTD; 285761; -.
DR MGI; MGI:1913936; Dcbld1.
DR VEuPathDB; HostDB:ENSMUSG00000019891; -.
DR eggNOG; ENOG502QW5E; Eukaryota.
DR GeneTree; ENSGT00940000157334; -.
DR HOGENOM; CLU_016654_1_0_1; -.
DR InParanoid; Q9D4J3; -.
DR OMA; SEFENHY; -.
DR OrthoDB; 317808at2759; -.
DR PhylomeDB; Q9D4J3; -.
DR BioGRID-ORCS; 66686; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9D4J3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D4J3; protein.
DR Bgee; ENSMUSG00000019891; Expressed in molar tooth and 216 other tissues.
DR Genevisible; Q9D4J3; MM.
DR GO; GO:0072562; C:blood microparticle; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR CDD; cd00041; CUB; 1.
DR Gene3D; 2.170.130.20; -; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR004043; LCCL.
DR InterPro; IPR036609; LCCL_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF03815; LCCL; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00603; LCCL; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF69848; SSF69848; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS50820; LCCL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..503
FT /note="Discoidin, CUB and LCCL domain-containing protein 1"
FT /id="PRO_0000021077"
FT TOPO_DOM 26..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..141
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 143..239
FT /note="LCCL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT REGION 410..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N8Z6"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..59
FT /evidence="ECO:0000250"
FT DISULFID 85..103
FT /evidence="ECO:0000250"
FT DISULFID 149..165
FT /evidence="ECO:0000250"
FT DISULFID 169..191
FT /evidence="ECO:0000250"
FT VAR_SEQ 30..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010783"
FT CONFLICT 291
FT /note="G -> S (in Ref. 1; BAB30265)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="V -> I (in Ref. 2; AAH26771)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="N -> T (in Ref. 2; AAH26771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 54518 MW; 5FF935690B1FE125 CRC64;
MGTGAGGPSV LALLFAVCAP LRLQAEELGD GCGHIVTSQD SGTMTSKNYP GTYPNYTVCE
KIITVPKGKR LILRLGDLNI ESKTCASDYL LFSSATDQYG PYCGSWAVPK ELRLNSNEVT
VLFKSGSHIS GRGFLLTYAS SDHPDLITCL ERGSHYFEEK YSKFCPAGCR DIAGDISGNT
KDGYRDTSLL CKAAIHAGII TDELGGHINL LQSKGISHYE GLLANGVLSR HGSLSEKRFL
FTTPGMNITT VAIPSVIFIA LLLTGMGIFA ICRKRKKKGN PYVSADAQKT GCWKQIKYPF
ARHQSTEFTI SYDNEKEMTQ KLDLITSDMA DYQQPLMIGT GTVARKGSTF RPMDTDTEEV
RVNTEASGHY DCPHRPGRHE YALPLTHSEP EYATPIVERH LLRAHTFSTQ SGYRVPGPRP
THKHSHSSGG FPPATGATQV ESYQRPASPK PVGGGYDKPA ASSFLDSRDP ASQSQMTSGG
DDGYSAPRNG LAPLNQTAMT ALL
