ID A0A2K5I6B5_COLAP Unreviewed; 1691 AA.
AC A0A2K5I6B5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=ADAMTS like 3 {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000012173.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000012173.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_011809250.1; XM_011953860.1.
DR STRING; 336983.ENSCANP00000012173; -.
DR Ensembl; ENSCANT00000035076.1; ENSCANP00000012173.1; ENSCANG00000029466.1.
DR GeneID; 105520257; -.
DR CTD; 57188; -.
DR OMA; YRQITCQ; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 12.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR045371; ADAMTS_CR_3.
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:SF169; ADAMTS-LIKE PROTEIN 3; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 11.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00209; TSP1; 12.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 12.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 10.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1691
FT /note="ADAMTS like 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014363654"
FT DOMAIN 896..992
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1185..1279
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1296..1378
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1655..1691
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 1152..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 87..118
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 91..123
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 102..108
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1691 AA; 188962 MW; 40A3DEA1B8F4AA1A CRC64;
MASWTSPWWL LVGMVFMHST LQETTAEKSP GAYFLPEFAL SPQGSFLEDT TGEQFLTYRY
DDQTSRNTRS DEDKDGNWDA WGDWSDCSRT CGGGASYSLR RCLTGRNCEG QNIRYKTCSN
HDCPPDAEDF RAQQCSAYND VQYQGRYYEW LPQYDDPAAP CALRCHARGQ NLVVELAPKV
LDGTRCNTDS LDMCISGICQ AVGCDRQLGS SAKEDNCGVC AGDGSTCRLV RGQSKSHVSP
EKREENVIAV PLGSRTVRIT VKGPAHLFIE SKTLQGSKGE HSFNSPGVFV VENTTVEFQR
GSERQTFKIP GPLMADFIFK TRYTAAKDSM VQFFFYQPIS HQWRQTDFFP CTVTCGGGYQ
LNSAECVDIR LKRVVPDHYC HYYPENVKPK PKLKECSMDP CPSSDGFKEI MPYDHFQPLP
RWEHNPWTAC SVSCGGGIQR RSFVCVEESM HGEILQVEEW KCMYAPKPKV MQTCNLFDCP
KWIAMEWSQC TVTCGRGLRY RVVLCINHRG EHVGGCNPQL KLHIKEECVI PIPCYKPKEK
SPVEAKLPWL KQAQELEETR IATEEPTFIP EPWSACSTTC GPGVQVREVK CRVLLTFTQT
ETELPEEECE GPKLPTERPC LLEACDESLA SRELDIPLPE DSEMTYDWEY AGFTPCTATC
LGGHQEAIAV CLHIQTQQTV NDSLCDMVHR PPAMSQACNT EPCPPRWHMG SWGPCSATCG
VGIQTRDVYC LHPGETPAPP EECRDEKPHA LQACSQFDCP PGWHIEEWQQ CSRTCGGGTQ
NRRVTCRQLL TDGSFLNLSD ELCQGPKASS HKSCARTDCP PHLAVGDWSK CSVSCGVGIQ
RRKQVCQRLT AKGRRVPLSE MMCRDLPGLP LVRSCQMPEC SKIKSEMKTK LGEQGPQILS
VQRVYIQTRE EKRINLTIGS RAYLLPNTSV IIKCPVRRFQ KSLIQWEKDG HCLQNSKRLG
ITKSGSLKIH SLATPDIGVY RCIAGSAQET VVLKLIGTDN RLIARPTLRE PMREYPGMDH
NEANSLGVTW HKMRQMWNNK NDLYLDDDYI SNQPFLRALL GHCSSSAGNT NSWELKNKQF
EAAVKQGAYS MDTAQFDELI RNMSQLMETG EVSDDLASQL IYQLVAELAK AQPTHMQWWG
IQEETPPAAQ LRGETGSVSQ SSNAKNSGKL TFKPKRPVLM RQSQPPSISF NKTINSRIGN
TVYITKRTEV INILCDLITP GEATYTWTKD GTLLQPSVKI ILDGTGKIQI QNPTRKEQGI
YECSVANHLG SDVESSSVLY AEAPVILSVE RNITKPEHNH LSVMVGGIVE AALGANVTIR
CPVKGVPQPN ITWLKRGGSL SGNVSLLFNG SLLLQNVSLE NEGTYVCTAT NALGKAVATS
VLHLLERRWP ESKIVFPQGH KKYVLQATNT RTNSNDPTGE PLPQEPFWEP GNWSHCSATC
GHLGARIQRP QCVMANGQEV SEALCDHLQK PLAGFQPCNI WDCPARWFTS MWSQCSVSCG
EGYHSRQVMC KQTKANGTVQ VVSARACAPK DRPLGRKPCF GHPCVQWEPG NQCPGRCMGH
AVRMHQHHTA CQHNGSDSNC DDRRRPTFRR NCTSGACDVC WHTGPWKPCT AACGRGLQSR
KVDCIHTRSC KPVAERHCVQ KKKPVSWRHC LGPSCDRDCT DTTHYCMFVK HLNLCSLDLY
KQRCCQSCQE G
//
