ID ATL1_MOUSE Reviewed; 1745 AA.
AC Q8BLI0; A2AM52;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 24-JAN-2024, entry version 148.
DE RecName: Full=ADAMTS-like protein 1;
DE Short=ADAMTSL-1;
DE AltName: Full=Punctin-1;
DE Flags: Precursor;
GN Name=Adamtsl1;
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 {ECO:0000312|EMBL:BAC32213.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
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 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).
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q96RW4}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BLI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BLI0-2; Sequence=VSP_039332, VSP_039333;
CC -!- PTM: Glycosylated (By similarity). O-fucosylated by POFUT2 on a serine
CC or a threonine residue found within the consensus sequence C1-X(2)-
CC (S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the
CC 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 -!- PTM: Disulfide bonds are present. {ECO:0000250|UniProtKB:Q96RW4}.
CC -!- CAUTION: Although strongly similar to members of the ADAMTS family it
CC lacks the metalloprotease and disintegrin-like domains which are
CC typical of that family. {ECO:0000305}.
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DR EMBL; AK045085; BAC32213.1; -; mRNA.
DR EMBL; AL772130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL824705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_084243.3; NM_029967.3.
DR AlphaFoldDB; Q8BLI0; -.
DR STRING; 10090.ENSMUSP00000102796; -.
DR GlyCosmos; Q8BLI0; 4 sites, No reported glycans.
DR GlyGen; Q8BLI0; 4 sites.
DR iPTMnet; Q8BLI0; -.
DR PhosphoSitePlus; Q8BLI0; -.
DR MaxQB; Q8BLI0; -.
DR PaxDb; 10090-ENSMUSP00000102796; -.
DR ProteomicsDB; 277066; -. [Q8BLI0-1]
DR ProteomicsDB; 277067; -. [Q8BLI0-2]
DR Antibodypedia; 24655; 192 antibodies from 24 providers.
DR DNASU; 77739; -.
DR Ensembl; ENSMUST00000141889.8; ENSMUSP00000119278.2; ENSMUSG00000066113.17. [Q8BLI0-1]
DR GeneID; 77739; -.
DR KEGG; mmu:77739; -.
DR UCSC; uc008tlr.2; mouse. [Q8BLI0-2]
DR AGR; MGI:1924989; -.
DR CTD; 92949; -.
DR MGI; MGI:1924989; Adamtsl1.
DR VEuPathDB; HostDB:ENSMUSG00000066113; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000156243; -.
DR InParanoid; Q8BLI0; -.
DR OrthoDB; 2910701at2759; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 77739; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Adamtsl1; mouse.
DR PRO; PR:Q8BLI0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BLI0; Protein.
DR Bgee; ENSMUSG00000066113; Expressed in animal zygote and 149 other cell types or tissues.
DR ExpressionAtlas; Q8BLI0; baseline and differential.
DR Genevisible; Q8BLI0; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR CDD; cd00096; Ig; 2.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 10.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR PANTHER; PTHR13723:SF157; ADAMTS-LIKE PROTEIN 1; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 2.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 10.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00209; TSP1; 12.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 10.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 9.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Immunoglobulin domain; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..1745
FT /note="ADAMTS-like protein 1"
FT /id="PRO_0000035861"
FT DOMAIN 33..82
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 376..424
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 436..493
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 522..584
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 607..667
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 703..762
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 763..825
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 836..938
FT /note="Ig-like C2-type 1"
FT DOMAIN 1139..1241
FT /note="Ig-like C2-type 2"
FT DOMAIN 1261..1352
FT /note="Ig-like C2-type 3"
FT DOMAIN 1378..1468
FT /note="Ig-like C2-type 4"
FT DOMAIN 1528..1591
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1649..1709
FT /note="TSP type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1709..1745
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 966..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 391
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 451
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000250"
FT DISULFID 45..76
FT /evidence="ECO:0000250"
FT DISULFID 49..81
FT /evidence="ECO:0000250"
FT DISULFID 60..66
FT /evidence="ECO:0000250"
FT DISULFID 534..578
FT /evidence="ECO:0000250"
FT DISULFID 538..583
FT /evidence="ECO:0000250"
FT DISULFID 549..567
FT /evidence="ECO:0000250"
FT DISULFID 775..819
FT /evidence="ECO:0000250"
FT DISULFID 779..824
FT /evidence="ECO:0000250"
FT DISULFID 790..807
FT /evidence="ECO:0000250"
FT DISULFID 874..922
FT /evidence="ECO:0000250"
FT DISULFID 1177..1225
FT /evidence="ECO:0000250"
FT DISULFID 1283..1336
FT /evidence="ECO:0000250"
FT DISULFID 1401..1452
FT /evidence="ECO:0000250"
FT VAR_SEQ 362..377
FT /note="SDGYKQIMPYDLYHPL -> RSVQFTCLCMINQVPS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039332"
FT VAR_SEQ 378..1745
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039333"
SQ SEQUENCE 1745 AA; 192008 MW; 5A9E6EBC3C220ABB CRC64;
MECCRRAAPG TPLLVLAFLL LSSRTARSEE DREGLWDAWG PWSECSRTCG GGASYSLRRC
LSSKSCEGRN IRYRTCSNVD CPPEAGDFRA QQCSAHNDVK YHGQLYEWLP VSNDPDNPCS
LKCQAKGTSL VVELAPKVLD GTRCYTESLD MCISGLCQIV GCDHQLGSTV KEDNCGVCNG
DGSTCRLVRG QYKSQLSASK SDDTVVAIPY GSRHIRLVLK GPDHLYLETK TLQGTKGENS
LSSTGIFLVD NSTVDFQKLP DKEILRMTGP LTADFIIKIH DLGPADSTVQ FIFYQPIIHR
WRETDFFPCS ATCGGGYQLT SAECYDLRSN RVVADQYCHY YPENVKPKPK LQECNLDPCP
ASDGYKQIMP YDLYHPLPRW EATPWTACSS SCGGGIQSRA VSCVEEDIQG HVTSVEEWKC
MYTPKMPVVQ PCNIFDCPKW LAQEWSPCTV TCGQGLRYRV VLCIDHRGMH TGGCSAKTKP
HIKEECIIPT PCYKPREKLP IEAKLPWFKQ AQELEEGAAV SEEPSFIPEA WSACTVTCGV
GTQVRIIRCQ VLLPFSQSVA DLPADECEGP KPASQRACYA GPCNGETPEF NPDNGDGLLG
GLQDLDELYD WEYEGFTKCS ESCGGGVQEA VVSCLNKQTR ELADENLCVT SRRPPQLLKS
CNLDPCPASH LLSREMNEVV VLADELCHHP KPSTVQACNR FNCPPAWYPA QWQLCSRTCG
GGIQKRDVLC KQRMADGSFL ELPETFCSAS KPTSHQGCKK DDCPSEWLLS EWSECSVSCG
EGTQTRSAIC QRVLKTGVST VVNSTLCPPL PFSSSIRPCM LATCARPGRP STKHSPHIAA
ARNIYIQTRR QRKLHFVVGG FAYLLPKTTV VLRCPTRRFR KPLITWEKDG QHSISSAHVT
VAPFGYLKIH RLKPSDAGIY TCSAGPAREQ FVIKLIGGNR KLVARPLSLW SEEEEALQVR
KTNPKEALQT HKHQNGIFSN GSKAEKRGLT ADPGNRYDDI VSRLLEQGGW PGELLASWEV
QDSAERNASS EEDPNAEQAL LHLPFTMVAE QKRLDDILRN LSQQPEELRD LYSKHLVAQL
AQDIFRSHLE NQDLLPKPSE QRFPPMAVPA HKHVSGFSSS LRSSSGEAGG GSRRPHRKPA
ILRKISAAQQ LSASEVVTHL GQTVALASGT LSVLLHCEAV GNPRPTIHWT RNGEAVQFSD
RILLQPDDSL QILAPVEADV GFYTCNATNA LGYDSVSIAV TLAGKPLVKT SRMTVLNTEK
PTVTVDIGGT VRTVRGVNVT INCQVAGVPE AEVTWFRNKS KLGSSHHLHE GSSHHLHEGS
LLLTDVSFSD QGLYSCRAAN LHGEQTESTQ LLILDPPQVP TQLEDIRALL LATGPNLPSV
LMSPLGTQLV LDPGNSALLG CPIKGHPTPN ITWFQNGQPI ATAPGLTHHI WGAGQILRVA
NLSGGPQGEF SCLAQNEAGT LLQKASLVIQ DYWWSVDRLA TCSASCGNRG IHQPRLRCLL
NTTEVDPEHC TGKPRPAVQP VACNRRDCPS RWMVTSWSAC TRSCGGGVQT RRVTCQKLKA
SGISTPVSND MCSQLAKRPV DTQACNQQLC VEWAFSSWGQ CNGPCIGPRL AVQHRQVFCQ
TRDGITLPSE QCSALPRPVS TQNCWSEACS VHWRVSLWTL CTATCGNYGF QSRRVECVHV
RTNKAVPEHL CSWGPRPANW QRCNVTPCEN TECRDTTRYC EKVRQLKLCQ LGQFRSRCCG
TCGKA
//
