ID   A0A158QP53_HAEPC        Unreviewed;      1250 AA.
AC   A0A158QP53;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Attractin {ECO:0000313|WBParaSite:HPLM_0001187401-mRNA-1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001187401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0001187401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR   AlphaFoldDB; A0A158QP53; -.
DR   WBParaSite; HPLM_0001187401-mRNA-1; HPLM_0001187401-mRNA-1; HPLM_0001187401.
DR   OMA; MNGCPSD; -.
DR   Proteomes; UP000038042; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00055; EGF_Lam; 2.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR46376:SF2; DISTRACTED, ISOFORM B; 1.
DR   PANTHER; PTHR46376; LEUCINE-ZIPPER-LIKE TRANSCRIPTIONAL REGULATOR 1; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF01344; Kelch_1; 1.
DR   Pfam; PF13418; Kelch_4; 1.
DR   Pfam; PF00053; Laminin_EGF; 2.
DR   Pfam; PF01437; PSI; 1.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00180; EGF_Lam; 2.
DR   SMART; SM00423; PSI; 4.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00460};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1094..1118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..144
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          869..922
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          923..970
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DISULFID        894..903
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        906..920
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        954..968
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1250 AA;  139287 MW;  19889D768C65EF7B CRC64;
     LSLSTSCDRH CYNGVCLNGS CVCSKGWVGS QCDHCYGRIK VTENHSHLID GPLDYSPSSK
     CTWLIESEKV GAPLNIRLEN FQTECGWDFV YIYDGDGVYG EQLAAFCGEQ EVQELSAPSG
     KALIYFFSDL AMNLSGFNIT YEFERCPYNC NSHGSCQNSQ CVCDHGDYCE VRVCTKEDED
     KQGPCLHGGV CKDSRCSCAT SYHGDTCQMR NDRSVWDRIT TPKAPAGRAS HASVLIDDVI
     WSIGGEHFSG VVFEDPVLFN ITSRSWKSVV VGGKVKPGPR FDHTLVRYKS KLFMYGGVID
     RRNITSELWS FDLHTKEWNQ ENGENRNLTI PPLAVSGHTA HVIGSEMYVI FGYHPEIGFV
     HNIQIYNFET GRWRFGNTKD QVYGRFRHTS VHYKMDSGDA ILVYGGTMWS NTQNNLTDSL
     MRYDIKHEKW ANLPPSGVQL FLHTATILNG LMIVVGGNGY NISESRTKQE CFSSMVQAYD
     IACKQWFNIS SDAVQLRRYG HTAVATNYEL YVIGGFNGKM LNDVWRFSAA ECSSATRPEE
     CRSLIDGVKC IFTERACVRF DPFVSYKQSF LSFVKNEVPK SMSECRNTAL RQALQTCEDY
     TDCMSCISEP ACGWCPSGDQ CLPNEGECVD GQMMHTTWEK CSSSRGPPPP RPCGMANDCR
     SCKLLSHCNW YTADGKPACI PLEDESKCTS AIMVKRCRQL TFTLTVLLRK EQLDRELDRV
     ASSSLPLRLP TTPPPIPPGQ NLSYCPLPCS SLYTCSECLQ EQKCMWCPST SRCINMEAYA
     LSFAYGQCPS WVAGHAHGFA FSKSCRIESS NCSTHKTCAE CHLSPECGWL DDGSRTGLGT
     CTRGSARGPL ERSPDFQQHQ WYFIDCPACQ CNGHSMCNET RQTFGGVQEV CGECQNNTMG
     KHCEICAPGY HGDPRNGDNC SPCQCNGQAD TCDHITGTCH CRTKGVSGAS CDRCDQKYYG
     QPKNGTPCYY ELSVDFIFTF KLKNEDKDKH ATEIYLFSIP HKKDTDVTFQ ISCDGGSQAN
     VALNITSSLF ESTPRRMMLN TTCDAKGFRR VYVASDPDYA YGTDANTTFF VRVFNFTTPI
     TIQVSFAQSP PINWVLFFVI FAACFIVLLV VAGLLWMIKL RIEVYRRNQR RIDEIEHMAS
     RPFSSVKLEL TSPNAFQASG PVQGPTPLSV EPCSNYKSGI FTLAVRLPTG GRATTPNGTS
     GLAVASALCL LTPAQLGVLQ APDNSENRNN RKTTLRSYIP FLRARMNDTT
//