ID A0A1I8D3P6_9BILA Unreviewed; 628 AA.
AC A0A1I8D3P6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=SERPIN domain-containing protein {ECO:0000313|WBParaSite:RSKR_0001077500.1};
OS Rhabditophanes sp. KR3021.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC Rhabditophanes.
OX NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0001077500.1};
RN [1] {ECO:0000313|WBParaSite:RSKR_0001077500.1}
RP IDENTIFICATION.
RC STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0001077500.1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC {ECO:0000256|ARBA:ARBA00007965}.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
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DR AlphaFoldDB; A0A1I8D3P6; -.
DR WBParaSite; RSKR_0001077500.1; RSKR_0001077500.1; RSKR_0001077500.
DR Proteomes; UP000095286; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00172; serpin; 1.
DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
DR InterPro; IPR002259; Eqnu_transpt.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461:SF211; ACCESSORY GLAND PROTEIN ACP76A-RELATED; 1.
DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR Pfam; PF01733; Nucleoside_tran; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; Serpins; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 256..627
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
SQ SEQUENCE 628 AA; 70433 MW; 7D3B679947C1246F CRC64;
MSVGPPKDNW NLTYCILFLH GIGVLLPWNM LTTIAQDYYV DLKLSDHDAS GNITTQSTYA
LNFFSYLGIF AQAPNFILNV VNLVLRIKGD LLNRVMAMII VLFVSVVFTM IWIWIDTDAW
KTLFFWMTMV SFIIFNGAGG VYQNSMFGVA AVLPSKFTNA IIFGNNVCGT FIAIINIITI
AALSDKPKIA ATVYFAVSLA IVLVCFLSVP VLKKLPFYQY YENLSKFPQK DEEDQEEVVL
NMATYCVYKM SGDLNQDLSN HLADISIKYV NELYDGKKAV VFSPISLQIA LAMAYAGAGG
KTEEELGQFL GNGAAVEKIH NKFHVILTEL AAPPANEWIK CSLKSANKIY IKDDYEVLDS
YKNSLSKFYD GQFESINFND SENAAKVMNK FVSDATNEKI KDLIAADAIN NLTRIILINC
LYFKGDWVKK FKPHNTEKDQ FYGKENVSRE MEFMKRNDFM LYNENDSFQC LTLPFDNQSI
KMVIVLPKKR FGLGEVFESV NGSDFLKLVK GSENQGVDIS IPKFKIESKF GLNDSLKKMG
INDAFVGNVA DFSGITMQDR LSISSVVQKV VIDVNEDGCE AAAATGLMME LCCMPMVPED
PIIFKADQPF AFFLIHDDST VLFNGIYQ
//
