ID U4TWS4_DENPD Unreviewed; 1915 AA.
AC U4TWS4;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Contactin-associated protein-like 5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=D910_01851 {ECO:0000313|EMBL:ERL84418.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL84418.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL84418.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KB631579; ERL84418.1; -; Genomic_DNA.
DR STRING; 77166.U4TWS4; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00109; Kunitz-type; 1.
DR CDD; cd00110; LamG; 4.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 2.60.120.200; -; 6.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR15036:SF49; AXOTACTIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF02210; Laminin_G_2; 6.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00131; KU; 1.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 6.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1915
FT /note="Contactin-associated protein-like 5"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004655756"
FT TRANSMEM 1634..1655
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..77
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 112..292
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 293..331
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 467..640
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 642..680
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 888..1061
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1062..1099
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1134..1343
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1344..1382
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1384..1580
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1711..1805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1831..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1714..1730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1794
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1831..1852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1352..1369
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1915 AA; 216400 MW; 1E13553A5592B933 CRC64;
MLRCVLTIAL LALVTARPEQ NRIEPCPGTP EKGPCNRNIF KWAFDHEKRE CITFIWGGCA
GNDKNRFESE KHCIEKCFPS LEKNETAVQN VSVIPKEKRG PKLTFQETGT ENTFMFAQSN
TFIQIDGDII QTFQLRLCRQ ISFQFRTRLP HGLLVYHNVK VPNGVSLQPY ALYIIVQQGQ
LKVVHVYGKH STALTVGRGL NNDQWHTVTV RIDVHAAKLL AIVDELRDET DLKGLDTERL
SSEERLHGVK YIIESFVGCI KDVVLSTGKS ASDLLQISPL IATKHENVQE GCKNKCLTSD
NLCFKGSRCM NHYYTYTCDC FGTRYEGEYC DIYREQGVDH YIAASVFNGS VHIVMDFGEN
SPVTIVLGQT PDFKLHEWNN LTIFHEHEKI HLILNDEIKS LNITGKPLLY IDPEIYIGGG
PELQKKTGLK SKNNFVGSLK YVFYNDISII YELNKNNPKV HYIGILRPEF YESDVQIIPI
TFPFSASHIW WHNAHVDSLS LSFHFKASSN LSVIASSEAQ TGLYWEVRVV NDEVRFELLN
SVQNTTHLIS VKKTPGQWHF LNVTYIGGEI TVSIDRKGKT EKIGDLKFAI GDKIKIAAGS
RSNAGLVGCM RNIEVNGVSL EPRSVLQTER VVGEVTLDDC RFVDACQRPN TCEHGGKCSV
KENRLTCDCT NTGYIGTNCH FALYRKTCEE LALLGYTKPD VYLIDIDGNG RFPPAHVRCE
FQSIEESTKT IVEHNLPSQM DVRSPSEQDF SFSIKYREFN AEMLQELVSH SLNCSQYIKY
DCFMAPLELH STTWFISSAN QTVDFIGDVK RGTCPCSIGR QCENPTQWCN CDDVSDDKWD
TDDGYYTTGD SLGITEMYFL QQPDLPQNAL GRITLGPLEC VETNTQRFVV TFTTSQSYIE
VPGWRKGDLA FSFRTTGKKA ILLYQPPIRP NYPSFMIALT SDFQLTFNFT LNTGVSKELV
IDSVRRLNGG EWHKLWIDYN KYHVRFMINE DYQMVDLKSE EEFGPFEGSM FIGGAPFDLL
DPRSSVHQGL IGCFRGLVVN EEILDIYSYM SVHLSEIIKD CKPSCVPNPC KNGAQCKELW
STFECVCPNP WAYKGQYCET KKPYNFHKSF ENALSLPPLG YPGLNCGFSD INTNAVTFTH
SESYIHKNYF NNDTEEEKTI LSDIFKKRIL VNLRTYDNYS LVFYANDHLN NFVHLHIVEG
TKVEYLFNHD NQIYNITVPY KELNISMSVQ IAIVREENLT TMFVNDQNNS IPIGVKLLDV
YANKPWSNPD KEVLAPQRPP ASPTEYFQLN IGGYDPETLL RVNDDFPLLP GYVGCFRGFQ
IHDTLIDLPP KINSTIKGVI PNCNMKCDEE PCKNGGICIE EFRNLEHTCN CEHTSYYGEF
CNEEKGADFN GEAILSRVFV LNDTVDDVKI KVAFSSQDVR QKNTILLLLQ TENNRSYYLL
VGLSTEGFLI VQEDREGAVF SATVSKKSFI NGARHSIYYK RTFNDSELYV DKELTQMEQI
PAQTFTNIPE LGANEVHIGG QETNDPRFAI FKKFSGCLSN ILIAVNGHVM KPLEEYMLFT
KNGAEKVNVS NSHGVRSAQC SADFDVVHEK SPGTPNLNIS QGKDKTWVQD APQRVLYTHS
YAADSVEENN LEHLIIIVLA AFFLLILICI IYDVYRTNKK YKQKKEFETD ASILLSKKQA
AIMLQENNKP VQPLQLRPKA SDLEIIKPPQ LNGNMLTEKP NGNSNGTKPV EQAAPVPEEQ
VLLPLKRADS KREKQKRISF RDSASELAWD TPDESAEMLS PMLEEDEDSA SDENDDLPSA
VSSTGNLLSM APISSISEVT LADRRSMILK NDALNSSTPP LGKKALETDQ SPGPQSPQPP
KVPPRKFPRR KPSINPAPLI GGDHLRTYDN PISYLGGPKL PSRNRWSIES VLSLD
//
