ID A0A0V1ADH4_9BILA Unreviewed; 817 AA.
AC A0A0V1ADH4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Double C2-like domain-containing protein beta {ECO:0000313|EMBL:KRY22848.1};
GN Name=Doc2b {ECO:0000313|EMBL:KRY22848.1};
GN ORFNames=T12_6599 {ECO:0000313|EMBL:KRY22848.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY22848.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY22848.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY22848.1};
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:KRY22848.1}.
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DR EMBL; JYDQ01000006; KRY22848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1ADH4; -.
DR STRING; 990121.A0A0V1ADH4; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd04035; C2A_Rabphilin_Doc2; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR043566; Rabphilin/DOC2/Noc2.
DR InterPro; IPR047022; Rabphilin_Doc2_C2A.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45729; RABPHILIN, ISOFORM A; 1.
DR PANTHER; PTHR45729:SF6; RABPHILIN, ISOFORM A; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 115..235
FT /note="RabBD"
FT /evidence="ECO:0000259|PROSITE:PS50916"
FT DOMAIN 163..223
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 540..662
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 678..811
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 275..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..346
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 92740 MW; 757371A8C9FF02B7 CRC64;
MTSCLVFIIA YSYNQCLTSD QCTFCKHYLA FTISNQIQHQ QYCNVKTECF EVVLSVNNVI
FSVQTIITMR KKDYHISEST KMPGKQSSWI CPSDRFLILR SQLSAGWSVW SDTQRADKST
ISDNEMQQIK DVIARAEHIE ENEQRRIGKL VERLDRMKKM AAGNGINQCM LCGAKFGMIG
TRSFASFCHD CNKYVCQKNC GLETLDSNGQ TIYLCKLCSE TREMWKKSGA WFYKGIPNFI
KDTGLRSKSN DVSVSNSDDR SGFDTVSLTS MDSRCSKESL PSWSGKAKHA KRLLPTPPSE
SHIRPSQPRW AIISQSIQSF DKCVDSSSEE EEEDSKDEQE TEEDIDQNNE NLNRSLFLDD
SDTPYSRQSS CLSELDNSKP LSELESPELK RLSEEEKRTT DDVKGETEIY DSKSSISEVA
VHSDSPVQSC TNSSSRYTME IAEDSDASIA LSTSVHDQAT SEVNKIADQL ADCSMNKPYA
TTTLQHSDSA KSFDSSLYDS SPDNDIKRNM SLDKNALDKP VHEEYSTEQC SNGFSSPTAS
FGSLEYSLLY DETEEMLVVT IFQASNLPAM DSNGFSDPYV KLHLLPLANK STKLRTSTKW
KTLNPRWNER LIYYGMSKDD LRKKTLRLMV LDQDRIGSDF LGETRAPLKR LQSGKEKYFN
VYLEKQMPVE KCDEFTEERG KILLALCYDL QNKLLAVEVV RCAELVGMDS TGYSDPYVKL
TLKPGALKSY HVKTEVKKKT LNPEYNRVFQ FPVSYDELAK KSLDVEVWDK DVGKLDDFIG
SVTLSANAKS DRLKHWIECI QNPNKRIKKW HKLTGKV
//