ID A0A455BH52_PHYMC Unreviewed; 1537 AA.
AC A0A455BH52;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 20 isoform X8 {ECO:0000313|RefSeq:XP_028347238.1};
GN Name=ADAMTS20 {ECO:0000313|RefSeq:XP_028347238.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028347238.1};
RN [1] {ECO:0000313|RefSeq:XP_028347238.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028347238.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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_028347238.1; XM_028491437.2.
DR Proteomes; UP000248484; Chromosome 6.
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:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 11.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR012314; Pept_M12B_GON-ADAMTSs.
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:SF165; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 20; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF08685; GON; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 13.
DR SMART; SM00209; TSP1; 12.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 12.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS51046; GON; 1.
DR PROSITE; PS50092; TSP1; 12.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1537
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019834702"
FT DOMAIN 262..361
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1322..1522
FT /note="GON"
FT /evidence="ECO:0000259|PROSITE:PS51046"
SQ SEQUENCE 1537 AA; 173359 MW; 584255918B3EABC7 CRC64;
MRVAKWLTGL LYQLSLFITK SWEVHFHPRQ EALVRTLASY EVVTPARVNE FGEVFPKSHH
FSRRKRSAEA LEPTPFRTHY RIRAYGQVFQ LNLSADAAFL AAGYTEVHLG APALQAEERR
TAPPDLRHCF YRGQVNARED HTAVFSLCGG LMGTFKAHDG EYFLEPIMKA DGSEHEDDHN
KPHLIYRQEL KRNYFLQSHK PCEVSESQIK KTTLPFHNYS DMNEDLNIKG EIVLGDSSKN
ISLEDERSQL HSRKKRFLSY PRYVEVMVTA DAKMVHHHGQ NLQHYVLTLM SIVAAIYKDS
SIGNLINIVI VKLVVIHDEQ EGPVISFNAA TTLHNFCLWQ QTQNVLDDAH PSHHDTAVLI
TREDICGARE KCDTLALSDT QGNFLLNGNF VVSMSKKEIN VQGAIFEYSG SNNSIERINS
TDRLEEELLL QVLCVGNLYN PDVRYSFNIP MEEKSDLFTW DPYGPWQDCT KMCQGLHRRK
ITCVRKSDHM VASDQRCDHL PLPLLVTERC NTDCELRWHI IGKSECSSLC GRGYKSLDIH
CMKYSIHKGH TVPVDDHYCG DQLKPPTREP CHGDCVLTRW HYSEWSQCSR SCGGGERSRE
SYCINNFGHR LADRECQELP RVTTENCNEF SCPSWATSEW SECLVTCGKG TRQRQVWCQL
NEDHLSDGFC DPSNKPESLR PCELHACASW QVGPWGSCTA TCGQGYQMRA VKCVNELLSA
VLDDRLCHGA SRPSDRQDCI VTPCPIIPKI GATSLPALPM GKIAQWRYGS WTPCSVSCGR
GNQARYVSCR DAHDGIADES YCAHLPRPAE IAVCFSPCGE WQAGNWSPCS ASCGHGKTTR
QVLCISYHQP INENYCDPEV RPVIEQECNL AACPPTYSHF PSSSEQPSHF PGRNFPLTHK
PEDNQNQGVH PSIRGNQWRT GPWGSCSSSC AGGIQRRVVV CQDENGRSAS YCNAASKPPE
SKHCDSGPCP RWSYGSWGEC TQTCGGGIKS RFVICQFPNG QMSREQNCEI LNKPPSVVQC
HVHACPDDVS WHRGPWKSCS APCGKGLKYR EVICVDQFHG KLEEKYCSHL QKPRTHKACR
SVRCPSWKAK RWKECSVTCG SGVQQRDVYC RLRGVGRVAE EKCDQSTRPY FQRQCWRQDC
IQYHWVAGEW LDCSTSCKKR ETHRQVKCVG AQNMQVNESF CDPSTRPLAI RKCRNPPCKY
IVVTGDSSQC AGNCGFSYGQ RITYCIEIRS TEKYKLHELW PTDYQECPVL PSPQVYKCNF
RTCLHMATWK VGKWSKCSVT CGVGIMERRV ECIADNGWSS DLCLKSLKPD AQKKCYVHDC
KTFTSCKEIQ VKNNITKDGD YYLNIKGRII KIYCAGMHLQ NPKEYISLVK GEEDNFSEVY
GFRLQNPYEC PFNGSRRQDC ECKNDCLAAG HTVFSKIRID LNSMQIKTTD LLFAQTVFGN
AVPFATAGDC YSAARCPQGQ FSINLAGTGM KISSTAKWLA QGSYASVIIH RSQDGTKVYG
RCGGFCGKCI PHMTTGLPIQ GTHQGVTSPL NFSRPSK
//
