ID A0A1I7XIT9_HETBA Unreviewed; 595 AA.
AC A0A1I7XIT9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Cysteine-rich motor neuron 1 protein {ECO:0000313|WBParaSite:Hba_17231};
OS Heterorhabditis bacteriophora (Entomopathogenic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heterorhabditidae;
OC Heterorhabditis.
OX NCBI_TaxID=37862 {ECO:0000313|Proteomes:UP000095283, ECO:0000313|WBParaSite:Hba_17231};
RN [1] {ECO:0000313|WBParaSite:Hba_17231}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the beta-microseminoprotein family.
CC {ECO:0000256|ARBA:ARBA00010352}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A1I7XIT9; -.
DR WBParaSite; Hba_17231; Hba_17231; Hba_17231.
DR Proteomes; UP000095283; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR Gene3D; 6.20.200.20; -; 2.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR InterPro; IPR004094; Antistasin-like.
DR InterPro; IPR008735; PSP94.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR46439; CYSTEINE-RICH MOTOR NEURON 1 PROTEIN; 1.
DR PANTHER; PTHR46439:SF1; CYSTEINE-RICH MOTOR NEURON 1 PROTEIN; 1.
DR Pfam; PF02822; Antistasin; 1.
DR Pfam; PF05825; PSP94; 1.
DR Pfam; PF00093; VWC; 2.
DR SMART; SM00214; VWC; 4.
DR SUPFAM; SSF57603; FnI-like domain; 4.
DR PROSITE; PS51252; ANTISTASIN; 1.
DR PROSITE; PS01208; VWFC_1; 2.
DR PROSITE; PS50184; VWFC_2; 4.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 478..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..126
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 137..163
FT /note="Antistasin-like"
FT /evidence="ECO:0000259|PROSITE:PS51252"
FT DOMAIN 252..312
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 327..388
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 395..451
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT REGION 533..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 65394 MW; CD963DBFC7D4A2ED CRC64;
MDRCRCRAAV CRPAVCPEGK KLKIIRKGNG NPGKCCDEWE CEDDPQSLTP GRCTWIVIPD
GECCPICVGC QTERLEKKKK HEIWQKDDCT TCTCSEEGTH VCEKHMCRTE CENSRKVNGQ
CCPVCDEPVV LTLPATCPSL EHCPLRCENG LRRDDRGCFE CECLPVEHPS GSDCPQISKQ
NCDKLVISSF YNIILDYFEL HFLKEFCSLI SCPTRPKDCN ENDWQQKEGS CCPTCVTSVL
DTTLPTSKHE HTVCQSPGTG RLFTDGETWQ LAPCVSCTCR VGHVLCRTVE CPPIACKDPV
MAPDDQCCPK CLSNTVHNDK FNSETTSICT DEAGIAHVLG SPWRTDDCTS CTCTNVGKIE
CYRESCEPSE ECVGSPLIIK GRCCPVCSDV LSSADVCSYK SSVYSVNEEW MDGYCTNCSC
VTGGHTVCRE MVCPQCADPV PIEGHCCPLC KDIGWTAFSE SNGSVLVPPR GGWAPLPIIG
FLLMSFAIFG LLVVLFILYK RSRNNSKVSR KSFDKASSSV RLSASKQIGS MPQLVDWPGR
RDSHSDGQSE SLLSTASDTS TAISSVSSGN SPHNDTQPLT GRRNLPHNKL FQCNV
//
