ID A0A0V0W8M9_9BILA Unreviewed; 2307 AA.
AC A0A0V0W8M9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 28.
DE RecName: Full=Hepatocyte growth factor-regulated tyrosine kinase substrate {ECO:0000256|ARBA:ARBA00015450};
DE Flags: Fragment;
GN Name=nas-8 {ECO:0000313|EMBL:KRX72188.1};
GN ORFNames=T06_1779 {ECO:0000313|EMBL:KRX72188.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX72188.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX72188.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX72188.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX72188.1}.
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DR EMBL; JYDK01000214; KRX72188.1; -; Genomic_DNA.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd11304; Cadherin_repeat; 8.
DR CDD; cd15720; FYVE_Hrs; 1.
DR CDD; cd21387; GAT_Hrs; 1.
DR CDD; cd03569; VHS_Hrs; 1.
DR Gene3D; 1.20.5.1940; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 8.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR017073; HGS/VPS27.
DR InterPro; IPR024641; HRS_helical.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46275; HEPATOCYTE GROWTH FACTOR-REGULATED TYROSINE KINASE SUBSTRATE; 1.
DR PANTHER; PTHR46275:SF1; HEPATOCYTE GROWTH FACTOR-REGULATED TYROSINE KINASE SUBSTRATE; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF12210; Hrs_helical; 1.
DR Pfam; PF00790; VHS; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 8.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF49313; Cadherin-like; 8.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50179; VHS; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:KRX72188.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KRX72188.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT TRANSMEM 1313..1337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1503..1521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 278..399
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 417..512
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 530..628
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 630..736
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 736..837
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 838..955
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 965..1077
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1093..1196
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1532..1659
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 1676..1736
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1754..1845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2061..2081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1979..2054
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1758..1782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2307
FT /evidence="ECO:0000313|EMBL:KRX72188.1"
SQ SEQUENCE 2307 AA; 258995 MW; CC1C96BCE482A411 CRC64;
MHAQEERKKF YRFERAEKLF SHGAAELPSN QSCENPQTRP RACRGKNVQF EDGCCKSWLF
TCAMRYGRDN NLLRRPTAEQ GQFVLVWANI RADRDVVTIK RPFGEHENKT QSYFEQQPLT
DPLNDNVPQS WNMLWPAMRS DHFYVTQPLS FIHPTCGPAV SICSGVQYTA SVVTGIPPEK
KALKIHPLPI KAKNIYNPNV PVTYAFFNGT PETFSKYFAI NAQNAEIVQL KIIPNKEAGP
FLIYVIARTA YTGSKVSFAQ LNIQALNPTE SRFEPEVQVT NTQAYIDENA SIGTLIRTER
RQNGPPLQIS VTDKDLKPGM PPAIYQYILS GSGANHFAID QRGYVFLNAL ALKVDKNGDN
VHELIIRARE VDTTPIRTSE PVKVRIEIIA LDSHSPPVFG SKVYYATAYS GLPQQSLIRV
KATVKDSKTL AILKYRILSV SKGAEDLFHY NEDTNTLIAL GFLNPNAQYR VVLEVMDKFS
RTATTTIMVR VVDAATIGHL YQYSTQSVQP IAWTTTTTTT ATIPATQPVI AATFNITVSE
EVSPDTLVMT LTAEGAAPDQ TSYRITDATE KGKFRIDKND GRIFTAGVLD REHIPSHRLV
IEVKSGTMTT YAEILVNISD VNDNPPKIVN ETPIKFTVNS NSPNSIIGKI TATDNDIGDN
GIVRYRLKFP NKFFSIDPMK GIIKSRADLS TTGHSVHKLT IIAEDGGEPS LQSSVDATVE
ILNDNIDTGP LSVPVFTGNY SVGIDENLGP TNLVQIKAKY LDGRQGPVTY ILRRGDMSLF
SIDQRTGMLS TLVSLDAEKQ KKYTLIVGTE ENLSEEPPAW ARVTVIVHEL NDNSPIFQEK
SYSTTISEAL PPGSSILQVS ASDRDDSSPN NLIKYRLIGD EEAAKFFAVD EDSGLITIAK
SLLGAGKNKF TLSVEAKDKG NPPRSSFTTV AVHVEISTTT PLHFGSLSTW MPPSRNAVHL
QNNFVSSVFN TTVYELVPSP HFVMTLPMKS SNPTWQPVVQ CKILDGDSEE AFIIKTGSGG
LCELETRLKL DREEVSMYKL NISAATVLPS GNDGAQYFDY ATVFIEVLDQ NDNRPEFQFD
EDSALLGTFI GIVDEKASEF TPILRIKAVD KDVGRNKQIA YSLLENDPDS SLFMIDQETG
ELKTKAKLKE QRGKSAAVYR FRVQAKDNPS YGIPLSAEAN VVVNTVRNTN RFMITVDKWH
AGQQDQYVKK LKNEIRQIIE RSRNKCQMII LERIEDADYL GIVNNFGVNL IFVAVNIQTK
RVCRSSDLGE IFAKENIRRL KERLAPALLV QNVQEMVSPS TLLFGRRLQM SEIVLISVGC
FIGLACLVGV LVLCYYWNRY GFEVNFLIGK FHTVNEADID KSQAKRASSE KAMLYAGIPP
FNPILMSPSE KEYETQMLEL SVPDEPYDKR FNLTTVGIDD GIYTIRPGDR SALYGTRSSS
LSHVYIPPPD YPRNEDIYPR RPKQLYKFDL QKGRKAIFHK EINFFYTLLI ILSCMMIEND
ININYITTFV LLFTALGMFA MSKKFEKLLD RATDATLLEA DWESIMNCVD AVRSGETAPK
SAILSVRKRY HSDNPHVAHH ALLVLEALVK NGGPKIHREI ATKEFMEDLK HVTSESADKV
KDKVLELIQC WAHAFRDNPE YKIVKDTHTL MKLEGHVFPV LRESDAMFMA ESAPDWVDAD
HCFRCKVQFS LITRKHHCRN CGQIFCDKCS NKNIPLPHLG IERDVRVCEG CFDRIKNPIG
DLIKKLGEFT PSSVESSKAA LEKERQKEKE KKEAELREEE ELQLALALSQ SEKEEKDRLK
NRNSYQWKTS PPTMMNSNYG TSSASVANNP PNHNEGKKDK GLSSAKDMEN ELARYLNRQY
WEKVRLEQKQ ANTRKSPTPS APFEPTSVIK QPLESVESEN NNNSGVEMDA LQDFVNSLNE
SISVFVNRIK SNQTRGRSVT ADDTIQNNFI ALTSMHSRLL KNMQERIDRR GIILNWKYYE
NLQDKVNQIR EAREALESLR EEYRDKKKVE LAEMQRQQQL VMLAKLQSMR LKKYEMLGLQ
RMEALRQIEE KQRELFMRNK TAMQQPPPPP SQQPQQQQQQ PVIPVGLPPQ QQQQQHHHHH
QQQQPSLLTG AMGSNTFVQP SAAFNHSCTT ALQSGHVQAE FSQTPQVVSV PHVALMYPYT
VPTNENCAPS SQVLMPNSYS VNQPSMVPQQ AAYHSPYCPV DPSYGPSYMH APSAYHHSPS
YAVAGQMDMQ SYVYPPAGAG HFPAPHAYTV SQGIPGMVMH SQPTQQVMPT AGQPNVSTPV
TLASASTQSE PLSILCRVAQ MIKTVRD
//
