ID A0A1S3G2U4_DIPOR Unreviewed; 952 AA.
AC A0A1S3G2U4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 1 {ECO:0000313|RefSeq:XP_012882985.1};
GN Name=Adamts1 {ECO:0000313|RefSeq:XP_012882985.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012882985.1};
RN [1] {ECO:0000313|RefSeq:XP_012882985.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012882985.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR RefSeq; XP_012882985.1; XM_013027531.1.
DR AlphaFoldDB; A0A1S3G2U4; -.
DR STRING; 10020.ENSDORP00000016374; -.
DR GeneID; 105994105; -.
DR KEGG; dord:105994105; -.
DR CTD; 9510; -.
DR InParanoid; A0A1S3G2U4; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR013274; Pept_M12B_ADAM-TS1.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF40; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 1; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 2.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01858; ADAMTS1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR613274-
KW 4}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..952
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010383553"
FT DOMAIN 243..452
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 158..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 387
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT CARBOHYD 705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT DISULFID 318..370
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 347..352
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 364..447
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 402..431
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 473..496
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 484..506
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 491..525
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 519..530
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 556..593
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 560..598
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 571..583
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 952 AA; 104288 MW; 2211160AD8E2C454 CRC64;
MPVSRSRSSR PAPSRVIALL PPLLLAAAAG LLSVPGAHGR PTEEDEELVL PTLERAGGRG
TTRLLLEAFG QPLHLKLHPD HGFLAPGFTL QTVGRRPEPE TQRLEPAGDL AHCFYSGTVN
GDPNSAAALS LCEGVRGAFY LRGEEFFIQP APAEATERVA PRAPGVEPPA PPPQFHLLRR
RRRGGGAKCG VVDEDPLPAR GSGPEGEESE TQWPQRDRDP EREGQPTTVT GSIRKKRFVS
SPRYVETMLV ADQSMAEFHG SGLKHYLLTL FSVAARLYKH PSIRNSISLV VVKILVIYEE
QKGPEVTSNA ALTLRNFCNW QKQHNRPSDR YAEHYDTAIL FTRQDLCGVQ TCDTLGMADV
GTVCDPSRSC SVIEDDGLQA AFTTAHELGH VFNMPHDDAK QCAGHNGVNQ NSHMMASMLS
NLDRSQPWSP CSASTITSFL DNGHGECLMD KPQNPIQLPS DLPGTLYDAN RQCQFTFGEE
SKHCPDEAST CTTLWCTGTS GGLLVCQTKH FPWADGTNCE EGKWCVNGKC VNKTDKKHFD
TPVHGSWGPW GPWGDCSRTC GGGVQYTMRE CDNPVPKNGG KYCEGKRVRY KSCNIEDCPD
NNGKTFREEQ CEEHNEFSKA SFGSGPAVEW TPKYAGVSPK DRCKLICQAK GIGYFFVLKP
EVVDGTPCSP DSTSVCVQGQ CVKAGCDRII DSKKKFDKCG ICGGNGSTCK KISGSVTSAK
PGYHDIVTIP AGATNIEVKQ RTQRGSRNNG SFLAIRAADG TYILNGDFTL STLEQDITYK
GIVLRYSGSS AALERIRSFS PLKEPLTIQV LTVGNALRPK IKYTYFVKKK KESFNAIPTF
SEWVIEEWGE CSKSCGLGWQ RRLVECRDMN GQPASECAKE VKPDSTRPCA DLPCPQWQVG
EWSPCSKTCG KGYKKRTLKC LSHDGGVLSH ESCDPLKKPK HYIDFCTIAE CS
//
