ID A0A016WLH4_9BILA Unreviewed; 1245 AA.
AC A0A016WLH4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Nematode cuticle collagen N-terminal domain-containing protein {ECO:0000259|SMART:SM01088};
GN Name=Acey_s0603.g538 {ECO:0000313|EMBL:EYC40659.1};
GN ORFNames=Y032_0603g538 {ECO:0000313|EMBL:EYC40659.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC40659.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYC40659.1}.
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DR EMBL; JARK01000203; EYC40659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016WLH4; -.
DR STRING; 53326.A0A016WLH4; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR InterPro; IPR002486; Col_cuticle_N.
DR InterPro; IPR008160; Collagen.
DR PANTHER; PTHR24637:SF236; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR Pfam; PF01391; Collagen; 1.
DR SMART; SM01088; Col_cuticle_N; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1245
FT /note="Nematode cuticle collagen N-terminal domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001491471"
FT TRANSMEM 929..952
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 928..980
FT /note="Nematode cuticle collagen N-terminal"
FT /evidence="ECO:0000259|SMART:SM01088"
FT REGION 21..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1034
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1085
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1245 AA; 132336 MW; 0E99BC60EACE6B00 CRC64;
MGWKLGLAMV FLAASCCADE SPESTLTTQD NQSEDYESSD ADENVLKNRS TITNQSKVTQ
TVGSMLPPNP DLIVNLTPND DNGAVKESER KRAELELLKK SSKFRNAALG APITKTKLDE
VEIQNIDGAN PHLPPFAFSG DDADTKAKSA REIKQPDESP PKTTPATPTT TGFEQAKLIE
TLEDINSGGF VEEERAKRVG TGSPDGEPTA HVQESVDTVV ESDTTIAPSA VVTNTEVVDP
IAEYNRKIVE LAKRRRMIKE EGYKKYKQIM FKSGRNIVPV RLFFDTDPAL PLQPEDSFKR
SIKTPSETAK GSPVQGDKHN LVDAAVGGEK RQEVQKVEIS KPNPQLETRK ALLVDSASFT
PSAVNIVETT TLLNADQVLL NGQTESAPED LAGSGLPPPT TSESTIEVQE ELLSQQAHHA
AEVVSVQRQT STPFALDLSS TTTEDITRFD KMVKVEPAVM ASTPSPTEPL SEVSSQRSEE
STTERSVSEI TSEILDMLGE STTPILPTSS QQLLEPSSSI PVFSEAASST ALTANLSQTL
PPLLSMPPLS ALSSFSSLNT PVKIATQPRK PKKTSSERVG DDRKKSSGIL GLKTPLPTKK
PRRKLTKLRT STVPFDVVDS EGRTGITSTG TRAVTPAERH RFIKQKPGAS PVFSKPDRFG
VIRKGIRVNR PIRHRAVLVG QTSSPALISR THPGQRIFER TVKVDKPRRR RVRTKLQRRN
PNILTIRQRG SATDLRSSFA TTEAKSSVPL VITSPIPPRS PPVLSRLSIR PHAVNRHPTF
GASHQQAPAV QLSLRPSGVS MARGPQSLIQ PQPSLARTLA SPLNPVGELK VVKPKKNNIF
RLSEWDRIRE EFLRIKRQHK KLRQKHRQAR ARAASGGKTL SSERPNTAAA RENTRYVPHN
GEIARGVVYL AGHCVPIADF RLRMYATKVV TAVAGITAVT TVCSLVVVLY LVNDINNFYD
EAIEELTEFK DLANSAWHEM RPSYQDMREK RAVLAGAVRQ RRQWPAHCAC GTPPASCAPG
PPGPPGPPGL PGERGVPGLP GKRGNDGIKI SSGGGAGGCI KCPPGPPGSP GNDGPPGPPG
PGGAPGAPAI GGGQGPPGPI GPAGDAGAPG MPGNAGAPGQ PGAPGQRSIG LPGPPGPPGP
LGPPGAPGMP GAAGGPAPPG PPGLPGRPGN PGAPGPDGQP GGAGQPGMPG TDAQYCPCPP
RTVLYSQRKV LAQRRNRDAP PASKPVKSTD IKVTATAARK AVRKH
//
