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DCBD2_MOUSE
ID   DCBD2_MOUSE             Reviewed;         769 AA.
AC   Q91ZV3; A6X950; Q8BKI4;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Discoidin, CUB and LCCL domain-containing protein 2;
DE   AltName: Full=Endothelial and smooth muscle cell-derived neuropilin-like protein;
DE   Flags: Precursor;
GN   Name=Dcbld2; Synonyms=Esdn;
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 [MRNA].
RC   STRAIN=ICR;
RX   PubMed=11447234; DOI=10.1074/jbc.m105293200;
RA   Kobuke K., Furukawa Y., Sugai M., Tanigaki K., Ohashi N., Matsumori A.,
RA   Sasayama S., Honjo T., Tashiro K.;
RT   "ESDN, a novel neuropilin-like membrane protein cloned from vascular cells
RT   with the longest secretory signal sequence among eukaryotes, is up-
RT   regulated after vascular injury.";
RL   J. Biol. Chem. 276:34105-34114(2001).
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   STRAIN=C57BL/6J; 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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 168-769.
RC   STRAIN=C57BL/6J; TISSUE=Eye;
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]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
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:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
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DR   EMBL; AF387548; AAL30179.1; -; mRNA.
DR   EMBL; CT027564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC066097; AAH66097.1; -; mRNA.
DR   EMBL; AK051889; BAC34801.1; -; mRNA.
DR   CCDS; CCDS28229.1; -.
DR   RefSeq; NP_082799.2; NM_028523.3.
DR   RefSeq; XP_006522685.1; XM_006522622.1.
DR   AlphaFoldDB; Q91ZV3; -.
DR   SMR; Q91ZV3; -.
DR   BioGRID; 215971; 3.
DR   STRING; 10090.ENSMUSP00000039915; -.
DR   GlyGen; Q91ZV3; 5 sites.
DR   iPTMnet; Q91ZV3; -.
DR   PhosphoSitePlus; Q91ZV3; -.
DR   MaxQB; Q91ZV3; -.
DR   PaxDb; Q91ZV3; -.
DR   PeptideAtlas; Q91ZV3; -.
DR   PRIDE; Q91ZV3; -.
DR   ProteomicsDB; 279884; -.
DR   Antibodypedia; 8135; 211 antibodies from 29 providers.
DR   DNASU; 73379; -.
DR   Ensembl; ENSMUST00000046663; ENSMUSP00000039915; ENSMUSG00000035107.
DR   GeneID; 73379; -.
DR   KEGG; mmu:73379; -.
DR   UCSC; uc007zno.1; mouse.
DR   CTD; 131566; -.
DR   MGI; MGI:1920629; Dcbld2.
DR   VEuPathDB; HostDB:ENSMUSG00000035107; -.
DR   eggNOG; ENOG502QRMB; Eukaryota.
DR   GeneTree; ENSGT00940000158147; -.
DR   HOGENOM; CLU_016654_2_0_1; -.
DR   InParanoid; Q91ZV3; -.
DR   OMA; GVGRTEI; -.
DR   OrthoDB; 317808at2759; -.
DR   PhylomeDB; Q91ZV3; -.
DR   TreeFam; TF352191; -.
DR   BioGRID-ORCS; 73379; 1 hit in 74 CRISPR screens.
DR   ChiTaRS; Dcbld2; mouse.
DR   PRO; PR:Q91ZV3; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q91ZV3; protein.
DR   Bgee; ENSMUSG00000035107; Expressed in decidua and 218 other tissues.
DR   Genevisible; Q91ZV3; MM.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0042060; P:wound healing; ISS:UniProtKB.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00057; FA58C; 1.
DR   Gene3D; 2.170.130.20; -; 1.
DR   Gene3D; 2.60.120.290; -; 1.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR004043; LCCL.
DR   InterPro; IPR036609; LCCL_sf.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF03815; LCCL; 1.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00603; LCCL; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF49854; SSF49854; 1.
DR   SUPFAM; SSF69848; SSF69848; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS50820; LCCL; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..63
FT                   /evidence="ECO:0000255"
FT   CHAIN           64..769
FT                   /note="Discoidin, CUB and LCCL domain-containing protein 2"
FT                   /id="PRO_0000021079"
FT   TOPO_DOM        64..523
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        524..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        545..769
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          69..184
FT                   /note="CUB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DOMAIN          184..282
FT                   /note="LCCL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT   DOMAIN          289..446
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         601
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PD2"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        511
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        69..96
FT                   /evidence="ECO:0000250"
FT   DISULFID        123..145
FT                   /evidence="ECO:0000250"
FT   DISULFID        212..234
FT                   /evidence="ECO:0000250"
FT   DISULFID        289..446
FT                   /evidence="ECO:0000250"
FT   CONFLICT        478..479
FT                   /note="Missing (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   769 AA;  83774 MW;  73C1F1646FA3F017 CRC64;
     MASRAPLRAA RSPQGPGGPA APAATGRAAL PSAGCCPLPP GRNSSSRPRL LLLLLLLLQD
     AGGQQGDGCG HTVLGPESGT LTSINYPHTY PNSTVCEWEI RVRTGERIRI KFGDFDIEDS
     DYCHLNYLKI FNGIGVSRTE IGKYCGLGLQ MNQSIESKGS EVTVLFMSGT HAAGRGFLAS
     YSVIDKEDLI TCLDTVSNFL EPEFSKYCPA GCLLPFAEIS GTIPHGYRDS SPLCMAGIHA
     GVVSNVLGGQ ISIVISKGTP YYESSLANNV TSTVGYLSAS LFTFKTSGCY GTLGMESGVI
     ADPQITASSA LEWTDHMGQE NSWTAEKARL RKPGPPWAAF ATDEHQWLQI DLNKEKKITG
     IVTTGSTMIE HSYYVSAYRV LYSDDGQRWT VYREPGVDQD KIFQGNKDYH KDVRNNFLPP
     IIARFIRVNP VQWQQKIAMK VELLGCQFTL KGRLPKLTPP PRNGNNLRNT TARPKLGKGR
     APKFTQVLQP RSRNELPVQP AETTTTPDIK NTTVTPSVTK DVALAAVLVP VLVMALTTLI
     LILVCAWHWR NRKKKTEGAY DLPHWDRAGW WKGMKQLLPA KSVDHEETPV RYSTSEVSHL
     SAREVTTVLQ ADSAEYAQPL VGGIVGTLHQ RSTFKPEEGK EAGYADLDPY NSPMQEVYHA
     YAEPLPVTGP EYATPIVMDM SGHPTASVGL PSTSTFKTAG TQPHALVGTY NTLLSRTDSC
     SSGQAQYDTP KGGKSAATPE ELVYQVPQST QELSGAGRDE KFDAFKEIL
 
 
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