CIH1_COLLN
ID CIH1_COLLN Reviewed; 230 AA.
AC Q9P403; O13445;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Intracellular hyphae protein 1;
DE Flags: Precursor;
GN Name=CIH1;
OS Colletotrichum lindemuthianum (Bean anthracnose fungus) (Glomerella
OS lindemuthiana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=290576;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=LARS 137 / race kappa {ECO:0000269|PubMed:9721685};
RX PubMed=9721685; DOI=10.1046/j.1365-313x.1998.00196.x;
RA Perfect S.E., O'Connell R.J., Green E.F., Doering-Saad C., Green J.R.;
RT "Expression cloning of a fungal proline-rich glycoprotein specific to the
RT biotrophic interface formed in the Colletotrichum-bean interaction.";
RL Plant J. 15:273-279(1998).
RN [2] {ECO:0000312|EMBL:CAC00481.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 56987 / race gamma {ECO:0000312|EMBL:CAC00481.1};
RA Perfect S.E., O'Connell R.J., Green J.R.;
RT "Functional studies of CIH1, a biotrophy-related gene from Colletotrichum
RT lindemuthianum.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP GLYCOSYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=ATCC 56987 / race gamma {ECO:0000269|Ref.3};
RX AGRICOLA=IND20502939; DOI=10.1111/j.1469-8137.1994.tb04275.x;
RA Pain N.A., O'Connell R.J., Mendgen K., Green J.R.;
RT "Identification of glycoproteins specific to biotrophic intracellular
RT hyphae formed in the Colletotrichum lindemuthianum-bean interaction.";
RL New Phytol. 127:233-242(1994).
CC -!- FUNCTION: May have roles in host-pathogen interaction, including
CC establishment and maintenance of biotrophy, prevention of host
CC recognition of the fungus and a barrier to host defense molecules.
CC {ECO:0000303|PubMed:9721685}.
CC -!- SUBUNIT: Forms a multimeric structure. {ECO:0000303|Ref.3,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|Ref.3}.
CC Note=Cell wall and surrounding interfacial matrix.
CC -!- TISSUE SPECIFICITY: Expressed in penetration hyphae, infection vesicles
CC and primary hyphae (intracellular hyphae). {ECO:0000269|PubMed:9721685,
CC ECO:0000269|Ref.3}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the biotrophic phase of host-
CC pathogen interaction. {ECO:0000269|PubMed:9721685, ECO:0000269|Ref.3}.
CC -!- PTM: N-glycosylated and may be O-glycosylated. {ECO:0000269|Ref.3,
CC ECO:0000303|PubMed:9721685}.
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DR EMBL; AJ001441; CAA04765.1; -; mRNA.
DR EMBL; AJ271296; CAC00481.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9P403; -.
DR SMR; Q9P403; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030446; C:hyphal cell wall; IDA:UniProtKB.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 3.10.350.10; -; 2.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR Pfam; PF01476; LysM; 2.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF54106; SSF54106; 2.
DR PROSITE; PS51782; LYSM; 2.
PE 1: Evidence at protein level;
KW Cell wall; Glycoprotein; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..230
FT /note="Intracellular hyphae protein 1"
FT /id="PRO_0000020931"
FT REPEAT 30..33
FT /note="1-1"
FT /evidence="ECO:0000269|PubMed:9721685"
FT REPEAT 36..39
FT /note="1-2"
FT /evidence="ECO:0000269|PubMed:9721685"
FT REPEAT 42..45
FT /note="1-3"
FT /evidence="ECO:0000269|PubMed:9721685"
FT REPEAT 46..49
FT /note="2-1"
FT /evidence="ECO:0000269|PubMed:9721685"
FT REPEAT 50..53
FT /note="3-1"
FT /evidence="ECO:0000269|PubMed:9721685"
FT REPEAT 57..60
FT /note="1-4"
FT /evidence="ECO:0000269|PubMed:9721685"
FT REPEAT 65..68
FT /note="3-2"
FT /evidence="ECO:0000269|PubMed:9721685"
FT REPEAT 76..79
FT /note="2-2"
FT /evidence="ECO:0000269|PubMed:9721685"
FT REPEAT 80..83
FT /note="3-3"
FT /evidence="ECO:0000269|PubMed:9721685"
FT REPEAT 84..87
FT /note="1-5"
FT /evidence="ECO:0000269|PubMed:9721685"
FT DOMAIN 108..152
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 183..227
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 20..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..87
FT /note="5 X 4 AA repeats of L-P-E-P"
FT REGION 46..87
FT /note="2 X 4 AA repeats of V-E-G-P"
FT REGION 50..83
FT /note="3 X 4 AA repeats of Y-K-P-K"
FT COMPBIAS 36..61
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 93
FT /note="K -> Q (in Ref. 1; CAA04765)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="V -> I (in Ref. 1; CAA04765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 230 AA; 24518 MW; 66C1CA10EF78B3AB CRC64;
MQTSFVALLA VAASLASALP HGGNSYEASL PEPTNLPEPT KLPEPVEGPY KPKPPILPEP
IKDNYKPKTP ILPEHVEGPY KPKLPEPTTG DPKNNTLPVP TCVDGKIKTH KVKSGESLTT
IAEKYDTGIC NIAKLNNLAD PNFVDLNQDL QIPTDACEKD NTSCIKPDGT ATCVKDGKKD
GKDIYSVVSG DTLTSIAQAL QITLQSLKDA NPGVVPEHLN VGQKLNVPVC
