ATL2_MOUSE
ID ATL2_MOUSE Reviewed; 957 AA.
AC Q7TSK7; Q3U0C8;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=ADAMTS-like protein 2;
DE Short=ADAMTSL-2;
DE AltName: Full=TSP1-repeat-containing protein 1;
DE Short=TCP-1;
DE Flags: Precursor;
GN Name=Adamtsl2; Synonyms=Kiaa0605, Tcp1;
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=C57BL/6J; TISSUE=Spleen;
RA Kishi Y., Toji S., Tanaka M., Miyajima A., Yahara I.;
RT "Cloning of TSP1-repeats-containing protein expressed in splenic CD11c+
RT cells.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
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).
CC -!- SUBUNIT: Interacts with LTBP1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q7TSK7; P28301: Lox; NbExp=3; IntAct=EBI-25406979, EBI-642911;
CC Q7TSK7; P58215: LOXL3; Xeno; NbExp=2; IntAct=EBI-25406979, EBI-723960;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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 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; AB096928; BAC76875.1; -; mRNA.
DR EMBL; AK156991; BAE33926.1; -; mRNA.
DR CCDS; CCDS15824.1; -.
DR RefSeq; NP_084257.1; NM_029981.1.
DR AlphaFoldDB; Q7TSK7; -.
DR SMR; Q7TSK7; -.
DR BioGRID; 218926; 1.
DR IntAct; Q7TSK7; 3.
DR STRING; 10090.ENSMUSP00000088774; -.
DR GlyGen; Q7TSK7; 10 sites.
DR iPTMnet; Q7TSK7; -.
DR PhosphoSitePlus; Q7TSK7; -.
DR SwissPalm; Q7TSK7; -.
DR MaxQB; Q7TSK7; -.
DR PaxDb; Q7TSK7; -.
DR PRIDE; Q7TSK7; -.
DR ProteomicsDB; 265149; -.
DR Antibodypedia; 45302; 87 antibodies from 24 providers.
DR DNASU; 77794; -.
DR Ensembl; ENSMUST00000091233; ENSMUSP00000088774; ENSMUSG00000036040.
DR GeneID; 77794; -.
DR KEGG; mmu:77794; -.
DR UCSC; uc008ixa.1; mouse.
DR CTD; 9719; -.
DR MGI; MGI:1925044; Adamtsl2.
DR VEuPathDB; HostDB:ENSMUSG00000036040; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000159447; -.
DR HOGENOM; CLU_000660_6_1_1; -.
DR InParanoid; Q7TSK7; -.
DR OMA; QPVYYSF; -.
DR OrthoDB; 84598at2759; -.
DR PhylomeDB; Q7TSK7; -.
DR TreeFam; TF316874; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 77794; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q7TSK7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q7TSK7; protein.
DR Bgee; ENSMUSG00000036040; Expressed in left lung lobe and 137 other tissues.
DR ExpressionAtlas; Q7TSK7; baseline and differential.
DR Genevisible; Q7TSK7; MM.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0050436; F:microfibril binding; IPI:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0060481; P:lobar bronchus epithelium development; IMP:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR Gene3D; 2.20.100.10; -; 5.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 7.
DR SUPFAM; SSF82895; SSF82895; 7.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 4.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..957
FT /note="ADAMTS-like protein 2"
FT /id="PRO_0000249683"
FT DOMAIN 47..106
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 570..624
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 628..692
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 694..742
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 743..801
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 803..857
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 859..914
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 918..956
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 532..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 63..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 74..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT CONFLICT 441
FT /note="F -> L (in Ref. 2; BAE33926)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="V -> A (in Ref. 2; BAE33926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 957 AA; 105647 MW; D92FB05E0CF7FEC0 CRC64;
MDGRRQHPHW AWSLLAVAVV AGGAAPTEAS DNSPTSNSLE GGADTTAYWW GEWTKWTACS
RSCGGGVTSQ ERHCLQQRRK SVPGTGNRTC VGTSKRYQLC RVQECPPDGR SFREEQCVSF
NSRVYDGRAY QWKPLYPDDY VHISSKPCDL HCSTVDGQRQ LTVPARDGTS CKLTDLRGVC
VSGKCEPIGC DGVLFSTHTL DKCGVCQGDG SSCTHVTGNY RKGNNHLGYS LVTHIPAGAR
DIQIVERKKS ADVLALADEA GFYFFNGNYK VDSPKNFNIA GTVVKYRRPM DVYETGIEYI
VAQGPTNQGL NVMVWNQNGK SPSITFEYTL LQSPHMHHLP PVYYSFSEAA SQSTESTERQ
ELDSARLLGF MQHNGSLYRQ TSSERLGLNS QLFQPPAPEV ELGPSRGQES NEVCKQASGG
VCEGPPRGKG FQDHNATGRA FSADKDDREI SAHFTSHELL SANTISDQLL GTGSESEEFS
LNETMNSIFA QGAPRSSPAE SLYVDYEENE GPAAYLINGS YLELSSDRIN TSSEAPFPNT
SASPPNLAGN RTHKARTRPK ARKQGVSPAD MYRWKLSSHE PCSATCTTGV MSTYAMCVRY
DGVEVDDSYC DALTRPEPVH EFCAGRECQP RWETSSWSEC SRTCGEGHQF RIVRCWKMLS
PGFDSSVYSD LCEATEAVRP EERKTCRNPA CGPQWEMSEW SECTAKCGER SVVTRDIRCS
EDEKLCDPST KPVGEKNCTG PPCDRQWTVS DWGPCSGSCG QGRTIRHVYC KTSDGRVVPE
SQCQTETKPL AIHPCGDKNC PAHWLAQDWE RCNTTCGRGV KKRLVLCMEL ANGKPQIRSG
PECGLARKPP EESTCFERPC FKWYTSPWSE CTKTCGVGVR MRDVKCYQGT DIVRGCDPLV
KPVGRQACDL QPCPTEPPDD SCQDQPGTNC ALAIKVNLCG HWYYSKACCR SCRPPHS
