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ATL4_MOUSE
ID   ATL4_MOUSE              Reviewed;        1036 AA.
AC   Q80T21; Q148X6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=ADAMTS-like protein 4;
DE            Short=ADAMTSL-4;
DE   AltName: Full=Thrombospondin repeat-containing protein 1;
DE   Flags: Precursor;
GN   Name=Adamtsl4 {ECO:0000312|MGI:MGI:2389008};
GN   Synonyms=Tsrc1 {ECO:0000312|EMBL:AAO17738.1, ECO:0000312|MGI:MGI:2389008};
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:AAO17738.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO17738.1};
RX   PubMed=12706885; DOI=10.1016/s0378-1119(03)00423-2;
RA   Buchner D.A., Meisler M.H.;
RT   "TSRC1, a widely expressed gene containing seven thrombospondin type I
RT   repeats.";
RL   Gene 307:23-30(2003).
RN   [2] {ECO:0000312|EMBL:AAI17926.1}
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).
CC   -!- FUNCTION: Positive regulation of apoptosis. May facilitate FBN1
CC       microfibril biogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CTSB. Interacts with FBN1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}. Note=Colocalizes with FMN1 microfibrils in the
CC       eye ECM. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed in a range of tissues. Especially
CC       prevalent in brain, spinal cord, muscle, lung and heart.
CC       {ECO:0000269|PubMed:12706885}.
CC   -!- PTM: Glycosylated (By similarity). Can be O-fucosylated by POFUT2 on a
CC       serine or a threonine residue found within the consensus sequence C1-
CC       X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are
CC       the first and second cysteine residue of the repeat, respectively.
CC       Fucosylated repeats can then be further glycosylated by the addition of
CC       a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL.
CC       Fucosylation mediates the efficient secretion of ADAMTS family members.
CC       Can also be C-glycosylated with one or two mannose molecules on
CC       tryptophan residues within the consensus sequence W-X-X-W of the TPRs,
CC       and N-glycosylated. These other glycosylations can also facilitate
CC       secretion (By similarity). {ECO:0000250}.
CC   -!- CAUTION: Although similar to members of the ADAMTS family, it lacks the
CC       metalloprotease and disintegrin-like domains which are typical of that
CC       family. {ECO:0000305}.
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DR   EMBL; AY158701; AAO17738.1; -; mRNA.
DR   EMBL; BC117925; AAI17926.1; -; mRNA.
DR   CCDS; CCDS17618.1; -.
DR   RefSeq; NP_001288634.1; NM_001301705.1.
DR   RefSeq; NP_659148.2; NM_144899.3.
DR   AlphaFoldDB; Q80T21; -.
DR   SMR; Q80T21; -.
DR   BioGRID; 230868; 3.
DR   STRING; 10090.ENSMUSP00000015994; -.
DR   GlyGen; Q80T21; 2 sites.
DR   iPTMnet; Q80T21; -.
DR   PhosphoSitePlus; Q80T21; -.
DR   CPTAC; non-CPTAC-3560; -.
DR   MaxQB; Q80T21; -.
DR   PaxDb; Q80T21; -.
DR   PeptideAtlas; Q80T21; -.
DR   PRIDE; Q80T21; -.
DR   ProteomicsDB; 265150; -.
DR   Antibodypedia; 1665; 98 antibodies from 20 providers.
DR   DNASU; 229595; -.
DR   Ensembl; ENSMUST00000015994; ENSMUSP00000015994; ENSMUSG00000015850.
DR   Ensembl; ENSMUST00000117782; ENSMUSP00000113424; ENSMUSG00000015850.
DR   GeneID; 229595; -.
DR   KEGG; mmu:229595; -.
DR   UCSC; uc008qkm.2; mouse.
DR   CTD; 54507; -.
DR   MGI; MGI:2389008; Adamtsl4.
DR   VEuPathDB; HostDB:ENSMUSG00000015850; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   eggNOG; KOG4597; Eukaryota.
DR   GeneTree; ENSGT00940000161136; -.
DR   HOGENOM; CLU_000660_6_0_1; -.
DR   InParanoid; Q80T21; -.
DR   OMA; SCTHVLE; -.
DR   OrthoDB; 414258at2759; -.
DR   PhylomeDB; Q80T21; -.
DR   TreeFam; TF316874; -.
DR   Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR   BioGRID-ORCS; 229595; 5 hits in 71 CRISPR screens.
DR   ChiTaRS; Adamtsl4; mouse.
DR   PRO; PR:Q80T21; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q80T21; protein.
DR   Bgee; ENSMUSG00000015850; Expressed in interventricular septum and 150 other tissues.
DR   ExpressionAtlas; Q80T21; baseline and differential.
DR   Genevisible; Q80T21; 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:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0002020; F:protease binding; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0002064; P:epithelial cell development; IMP:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR   GO; GO:0070285; P:pigment cell development; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   Gene3D; 2.20.100.10; -; 6.
DR   InterPro; IPR045371; ADAMTS_CR_3.
DR   InterPro; IPR010294; ADAMTS_spacer1.
DR   InterPro; IPR010909; PLAC.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   Pfam; PF19236; ADAM_CR_3; 1.
DR   Pfam; PF05986; ADAM_spacer1; 1.
DR   Pfam; PF08686; PLAC; 1.
DR   Pfam; PF00090; TSP_1; 1.
DR   SMART; SM00209; TSP1; 7.
DR   SUPFAM; SSF82895; SSF82895; 6.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS50092; TSP1; 6.
PE   2: Evidence at transcript level;
KW   Apoptosis; Extracellular matrix; Glycoprotein; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1036
FT                   /note="ADAMTS-like protein 4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000257967"
FT   DOMAIN          47..91
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          687..748
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          750..804
FT                   /note="TSP type-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          805..871
FT                   /note="TSP type-1 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          872..931
FT                   /note="TSP type-1 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          932..988
FT                   /note="TSP type-1 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          991..1028
FT                   /note="PLAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT   REGION          73..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        737
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        93
FT                   /note="G -> R (in Ref. 2; AAI17926)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1036 AA;  113225 MW;  F018D59E71018714 CRC64;
     MESWLGRLWL CMMLLLPLPQ PCQDQELFGP SHQLPSEEGQ VPEGLWGPWG RWASCSQPCG
     VGVQRRSRTC ELHPALPLPP RPPRHPEAHR PRGQGSRPQT PRDPQSLYRP QPRGRGGPLR
     APASQVGREE TQEPQGAQRF RVRDPIKPGM FGYGRVPFAL PLHRSRRHPH RPGQPKNSST
     GEGMVPSQPP STELASEKHG PHMQPPEPRS HSAETPRSGT AQTEVLPRTS SAPSYTGTPA
     PTSSFGDSRS FQGSLGPRMP PSPGSWSSPQ GAERRHPPPF SPVPRSQQSR RHWRPPGPHR
     SPDGWLPLTR DSSPLWSIFA PSIPAPNCSG ESEQMRACSQ EPCPPEQPDP RALQCAAFDS
     QEFMGQLYQW EPFTEVQGSQ RCELNCRPRG FRFYVRHTEK VQDGTLCQPG SLDICVAGRC
     LSPGCDGVLG SGRRPDGCGV CGGDGSTCRL VSGNLTDRGG PLGYQKILWI PAGASHLHIS
     QLRPSSNYLA LRGPGGRSII NGNWAVDPPG SYTAIGTVFQ YNRPPREEGK GESLSAEGPT
     TQPVDVYMIF QEDNPGVFYQ YVISSPPAVL ESPSTKPPAL QPQPEMLRGE PLLPSAPRPV
     RAPGTLQRQV RIPQVPPPTR VRTAMGSSAG YWKQVGHSEC SASCGKGVWH PIFLCISRES
     GEELDEQSCA VGARPPASPE PCHGPPCPPY WEAGEWTSCS RSCGPGTQHR QLLCRQEFGG
     GGSSVPPERC GHLPRPNITQ PCQLHLCGHW EISSPWSQCS VRCGRGQRSR QVRCVGSNGD
     EVDKQECASG PPPPPSREAC DMGPCTTAWF YSDWSSKCSA ECGTGIQRRA VVCLRSGETL
     QGDPEAGSTE QGCPLRSRPP DMRACSLGPC ERTWRWFTGP WSECSSECGS GTQHRDIICV
     SKLGAEFNVT SPSNCSHLPR PPALQPCQGQ ACEDKWFSTL WSPCSRSCQG GMQTREVQCL
     SGNQTLSSRC PPHLRPSRKR PCNSQPCNQR PDDQCKDSSP HCPLVVQARL CVYPYYTTTC
     CRSCAHVLEQ SQLEPA
 
 
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