ATL4_RAT
ID ATL4_RAT Reviewed; 1030 AA.
AC Q4FZU4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=ADAMTS-like protein 4;
DE Short=ADAMTSL-4;
DE Flags: Precursor;
GN Name=Adamtsl4 {ECO:0000312|EMBL:AAH99119.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH99119.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta {ECO:0000312|EMBL:AAH99119.1};
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 -!- 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; BC099119; AAH99119.1; -; mRNA.
DR RefSeq; NP_001029184.1; NM_001034012.1.
DR RefSeq; XP_008759529.2; XM_008761307.2.
DR RefSeq; XP_017446392.1; XM_017590903.1.
DR RefSeq; XP_017446393.1; XM_017590904.1.
DR RefSeq; XP_017446394.1; XM_017590905.1.
DR RefSeq; XP_017446395.1; XM_017590906.1.
DR RefSeq; XP_017446396.1; XM_017590907.1.
DR AlphaFoldDB; Q4FZU4; -.
DR SMR; Q4FZU4; -.
DR STRING; 10116.ENSRNOP00000063998; -.
DR GlyGen; Q4FZU4; 2 sites.
DR PaxDb; Q4FZU4; -.
DR Ensembl; ENSRNOT00000074156; ENSRNOP00000063998; ENSRNOG00000049385.
DR GeneID; 310670; -.
DR KEGG; rno:310670; -.
DR CTD; 54507; -.
DR RGD; 1561012; Adamtsl4.
DR eggNOG; KOG3538; Eukaryota.
DR eggNOG; KOG4597; Eukaryota.
DR GeneTree; ENSGT00940000161136; -.
DR HOGENOM; CLU_000660_6_0_1; -.
DR InParanoid; Q4FZU4; -.
DR OMA; VWSVWGE; -.
DR OrthoDB; 414258at2759; -.
DR PhylomeDB; Q4FZU4; -.
DR Reactome; R-RNO-5173214; O-glycosylation of TSR domain-containing proteins.
DR PRO; PR:Q4FZU4; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000049385; Expressed in esophagus and 18 other tissues.
DR Genevisible; Q4FZU4; RN.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005614; C:interstitial matrix; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0070285; P:pigment cell development; IEA:Ensembl.
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..1030
FT /note="ADAMTS-like protein 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000257968"
FT DOMAIN 47..91
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 681..740
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 741..800
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 803..865
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 866..925
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 926..982
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 985..1022
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 73..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 731
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1030 AA; 112785 MW; E38CC6486E08546B CRC64;
MELWLGRLWL YVMLLLLLLQ LCQDQELLGP SLQTPSEEDQ VPEGLWGPWG RWASCSQPCG
VGVQRRSRTC ELHPALSLPP RPPRHPEAPQ PRGQGSRPQT PRDPQSLYRP QPRGRGGPLR
GPASQVGREE TQEPRGAQRF RVRDPIKPGM FGYGRVPFAL PLHRSRRLAH KPGQPKDSST
AEETLPSQPP STEPASEKHS PHMQPPELRA QSRSPSAETP RSGTAQTEVP SRTSSAPSDM
GIPAPTSSFR DSRSFQGSPE PRMPTSQGAE RQPHPFSPVT RSQLSRRHWR PPGSPHRSPD
GWLPLTRDSS PHWSLFAPSS PTPECSGESE QMRACSQEPC PPEQPDPRAL QCAAFDSQEF
MGQLYQWEPF TEVQGSQRCE LNCRPRGFRF YVRHTEKVQD GTLCQPGSLD ICVAGHCLSP
GCDGILGSGR RPDGCGVCGG DGSTCRLVSG NLTDRGGPLG YQKILWIPAG ASHLRISQFR
PSSNYLALRG PGGRSIINGN WAVDPPGSYA AVGTVFQYNR PPREEGKGET LSAEGPTTQP
VDVYMIFQED NPGVFYQYVT SAAPESPSTM PPALQLQPEM LRGEPLLPSA PRPVRAPGTL
QRQARIPQVP PPTHVRTAMG SSAGYWKQVG HSECSASCGK GVWRPIFLCV SRESGEELDE
QSCAVGARPP ASPESCHRPP CPPYWEAGEW TSCSRSCGPG TQHRQLLCRQ EFGGGGSSVP
PERCGHLPRP NITQSCQLRL CGHWEISSPW SQCSVRCGRG QRSRQVRCVG SNGHEVGKQE
CASGPPPPPS REACDMGPCT TAWFYSDWSS KCSAECGTGI QRRAVVCLRS GETLQGDPEA
GSTEQGCPLR SRPPDMRACS LGPCEKTWRW YTGPWSECSS ECGSGTQHRD IICVSKLGTK
FNVTSPSNCS HLPRPPALQP CQGQACEDQW FSTLWSPCSQ SCQGGVQTRE VQCLSSNHTL
SSRCPPHLRP SRKRPCNSQP CNQRPDDQCK DSSPHCPLVV QARLCVYPYY TATCCRSCAH
VLEQSQLEPA
