PCHTP_TRISP
ID PCHTP_TRISP Reviewed; 424 AA.
AC D4N4Z9; E5SHY6; P86477;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Poly-cysteine and histidine-tailed protein;
DE Short=Ts-PCHTP;
DE Flags: Precursor;
GN ORFNames=Tsp_04041;
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 118-133, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Larva;
RX PubMed=20967224; DOI=10.1371/journal.pone.0013343;
RA Radoslavov G., Jordanova R., Teofanova D., Georgieva K., Hristov P.,
RA Salomone-Stagni M., Liebau E., Bankov I.;
RT "A novel secretory poly-cysteine and histidine-tailed metalloprotein (Ts-
RT PCHTP) from Trichinella spiralis (Nematoda).";
RL PLoS ONE 5:E13343-E13343(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS 195;
RX PubMed=21336279; DOI=10.1038/ng.769;
RA Mitreva M., Jasmer D.P., Zarlenga D.S., Wang Z., Abubucker S., Martin J.,
RA Taylor C.M., Yin Y., Fulton L., Minx P., Yang S.P., Warren W.C.,
RA Fulton R.S., Bhonagiri V., Zhang X., Hallsworth-Pepin K., Clifton S.W.,
RA McCarter J.P., Appleton J., Mardis E.R., Wilson R.K.;
RT "The draft genome of the parasitic nematode Trichinella spiralis.";
RL Nat. Genet. 43:228-235(2011).
CC -!- FUNCTION: Binds iron and zinc. May bind nickel.
CC {ECO:0000269|PubMed:20967224}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20967224}.
CC -!- TISSUE SPECIFICITY: Expressed in larval tissues like cuticle,
CC hypodermis and muscle (at protein level). Note=Not excreted into
CC striated muscle fibers or nurse cell. {ECO:0000269|PubMed:20967224}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:20967224}.
CC -!- MASS SPECTROMETRY: Mass=48105; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20967224};
CC -!- CAUTION: At protein level, the N-terminus was determined to be Leu-118
CC but it is uncertain whether this is the true N-terminus of the mature
CC protein or not. {ECO:0000305|PubMed:20967224}.
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DR EMBL; GQ497342; ADD82426.1; -; mRNA.
DR EMBL; ABIR02000995; EFV55596.1; -; Genomic_DNA.
DR RefSeq; XP_003374855.1; XM_003374807.1.
DR AlphaFoldDB; D4N4Z9; -.
DR SMR; D4N4Z9; -.
DR iPTMnet; D4N4Z9; -.
DR EnsemblMetazoa; EFV55596; EFV55596; EFV55596.
DR GeneID; 10904460; -.
DR KEGG; tsp:Tsp_04041; -.
DR CTD; 10904460; -.
DR HOGENOM; CLU_647847_0_0_1; -.
DR OMA; KCCCHPY; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Iron; Metal-binding; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..424
FT /note="Poly-cysteine and histidine-tailed protein"
FT /evidence="ECO:0000255"
FT /id="PRO_5000581037"
FT REGION 372..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:20967224"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:20967224"
FT CONFLICT 121
FT /note="I -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 47739 MW; 7018E80DF2DE72AE CRC64;
MAFSTIVVLF VAAVGFGNKI SSADTCPEFG EWKPWTECLW YPMQNIYDKM TASCGLPGHR
NLTNILPLPP GFTIPPPCGH CSFKTRCRTR PKKEGCYPFD GEREICHEHG DICTIAKLPG
IGCGWTVLQE VVKQCLSRPD IPEYMRAGYK KLFHMLPKGH CIEKDNQCKC CCGDYEPNED
GTECVKQQDH QCAPFNEPGD WSECLWFPLA DMFKKVQSHC GVEGKPEGLS PSSLAPAGFQ
IPEKCGFCSF RLKCQSREKK EGCFPLKVDK KSCGAEDCPT CGDVCTLDKQ NNSCAFTKAM
GMKFWNSFAH KAKESNLAHW RRDGYADLFK FLPYGHCKEV GDKCKCCCHP YEPNEDGTAC
VVKQYCKSLE EVGGKKQQKD QPESEKKAEN MPETTGNASH HQHRHHHGDS SSESHEQHHH
HHHH