ATL5_HUMAN
ID ATL5_HUMAN Reviewed; 481 AA.
AC Q6ZMM2; B4DXK7; Q8IW95;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 3.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=ADAMTS-like protein 5;
DE Short=ADAMTSL-5;
DE AltName: Full=Thrombospondin type-1 domain-containing protein 6;
DE Flags: Precursor;
GN Name=ADAMTSL5; Synonyms=THSD6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-366 (ISOFORM 2).
RC 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 ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, HEPARIN-BINDING, INTERACTION
RP WITH FBN1 AND FBN2, AND GLYCOSYLATION AT ASN-218.
RX PubMed=23010571; DOI=10.1016/j.matbio.2012.09.003;
RA Bader H.L., Wang L.W., Ho J.C., Tran T., Holden P., Fitzgerald J.,
RA Atit R.P., Reinhardt D.P., Apte S.S.;
RT "A disintegrin-like and metalloprotease domain containing thrombospondin
RT type 1 motif-like 5 (ADAMTSL5) is a novel fibrillin-1-, fibrillin-2-, and
RT heparin-binding member of the ADAMTS superfamily containing a netrin-like
RT module.";
RL Matrix Biol. 31:398-411(2012).
CC -!- FUNCTION: May play a role in modulation of fibrillin microfibrils in
CC the extracellular matrix (ECM).
CC -!- SUBUNIT: Interacts with heparin, FBN1 and FBN2.
CC {ECO:0000269|PubMed:23010571}.
CC -!- INTERACTION:
CC Q6ZMM2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-9075891, EBI-3867333;
CC Q6ZMM2; Q5TD97: FHL5; NbExp=3; IntAct=EBI-9075891, EBI-750641;
CC Q6ZMM2; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-9075891, EBI-3958099;
CC Q6ZMM2-2; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-10254938, EBI-10173507;
CC Q6ZMM2-2; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-10254938, EBI-945833;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23010571}. Secreted,
CC extracellular space, extracellular matrix
CC {ECO:0000269|PubMed:23010571}. Note=Colocalized with fibrillin
CC microfibrils. Predominantly distributed in baso-lateral regions of
CC fibroblast extracellular matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZMM2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZMM2-2; Sequence=VSP_053358;
CC -!- PTM: Proteolytically cleaved to release a C-terminal fragment
CC containing the NTR domain.
CC -!- PTM: Contains at least one additional N-linked glycosylation site.
CC {ECO:0000269|PubMed:23010571}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major.
CC -!- MISCELLANEOUS: [Isoform 2]: Minor. {ECO:0000305}.
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; AK131571; BAD18703.1; -; mRNA.
DR EMBL; AK302020; BAG63419.1; -; mRNA.
DR EMBL; AC027307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040620; AAH40620.1; -; mRNA.
DR RefSeq; NP_998769.2; NM_213604.2.
DR RefSeq; XP_005259606.1; XM_005259549.3.
DR AlphaFoldDB; Q6ZMM2; -.
DR SMR; Q6ZMM2; -.
DR BioGRID; 130874; 8.
DR IntAct; Q6ZMM2; 7.
DR STRING; 9606.ENSP00000327608; -.
DR GlyGen; Q6ZMM2; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q6ZMM2; -.
DR BioMuta; ADAMTSL5; -.
DR DMDM; 557952602; -.
DR MassIVE; Q6ZMM2; -.
DR PaxDb; Q6ZMM2; -.
DR PeptideAtlas; Q6ZMM2; -.
DR PRIDE; Q6ZMM2; -.
DR ProteomicsDB; 5446; -.
DR ProteomicsDB; 67891; -. [Q6ZMM2-1]
DR TopDownProteomics; Q6ZMM2-2; -. [Q6ZMM2-2]
DR DNASU; 339366; -.
DR GeneID; 339366; -.
DR KEGG; hsa:339366; -.
DR CTD; 339366; -.
DR DisGeNET; 339366; -.
DR GeneCards; ADAMTSL5; -.
DR HGNC; HGNC:27912; ADAMTSL5.
DR neXtProt; NX_Q6ZMM2; -.
DR PharmGKB; PA134867057; -.
DR eggNOG; KOG3538; Eukaryota.
DR InParanoid; Q6ZMM2; -.
DR OrthoDB; 548127at2759; -.
DR PhylomeDB; Q6ZMM2; -.
DR TreeFam; TF351486; -.
DR PathwayCommons; Q6ZMM2; -.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q6ZMM2; -.
DR BioGRID-ORCS; 339366; 21 hits in 1069 CRISPR screens.
DR GenomeRNAi; 339366; -.
DR Pharos; Q6ZMM2; Tbio.
DR PRO; PR:Q6ZMM2; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q6ZMM2; protein.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0001527; C:microfibril; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0050436; F:microfibril binding; IDA:MGI.
DR Gene3D; 2.20.100.10; -; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR008993; TIMP-like_OB-fold.
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; PF01759; NTR; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00643; C345C; 1.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF50242; SSF50242; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS50189; NTR; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Heparin-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..481
FT /note="ADAMTS-like protein 5"
FT /id="PRO_0000249582"
FT DOMAIN 45..97
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 360..479
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 331..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23010571"
FT DISULFID 57..91
FT /evidence="ECO:0000250"
FT DISULFID 61..96
FT /evidence="ECO:0000250"
FT DISULFID 72..81
FT /evidence="ECO:0000250"
FT DISULFID 360..425
FT /evidence="ECO:0000250"
FT DISULFID 363..427
FT /evidence="ECO:0000250"
FT DISULFID 377..479
FT /evidence="ECO:0000250"
FT VAR_SEQ 11..18
FT /note="WLASGHTE -> MDSAPLFP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_053358"
FT CONFLICT 197
FT /note="N -> D (in Ref. 1; BAD18703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 53193 MW; 8E0FDBBD63993F57 CRC64;
MGKLRPGRVE WLASGHTERP HLFQNLLLFL WALLNCGLGV SAQGPGEWTP WVSWTRCSSS
CGRGVSVRSR RCLRLPGEEP CWGDSHEYRL CQLPDCPPGA VPFRDLQCAL YNGRPVLGTQ
KTYQWVPFHG APNQCDLNCL AEGHAFYHSF GRVLDGTACS PGAQGVCVAG RCLSAGCDGL
LGSGALEDRC GRCGGANDSC LFVQRVFRDA GAFAGYWNVT LIPEGARHIR VEHRSRNHLA
LMGGDGRYVL NGHWVVSPPG TYEAAGTHVV YTRDTGPQET LQAAGPTSHD LLLQVLLQEP
NPGIEFEFWL PRERYSPFQA RVQALGWPLR QPQPRGVEPQ PPAAPAVTPA QTPTLAPDPC
PPCPDTRGRA HRLLHYCGSD FVFQARVLGH HHQAQETRYE VRIQLVYKNR SPLRAREYVW
APGHCPCPML APHRDYLMAV QRLVSPDGTQ DQLLLPHAGY ARPWSPAEDS RIRLTARRCP
G
