ID Q5CXK9_CRYPI Unreviewed; 1607 AA.
AC Q5CXK9;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 22-FEB-2023, entry version 90.
DE SubName: Full=Extacellular protein with a signal peptide, clostripain like caspase/hemoglobinase domain, notch domain and 2 EGF domains {ECO:0000313|EMBL:EAK89763.1};
GN ORFNames=cgd6_670 {ECO:0000313|EMBL:EAK89763.1};
OS Cryptosporidium parvum (strain Iowa II).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK89763.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK89763.1, ECO:0000313|Proteomes:UP000006726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX PubMed=15044751; DOI=10.1126/science.1094786;
RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA Anantharaman V., Aravind L., Kapur V.;
RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL Science 304:441-445(2004).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:EAK89763.1}.
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DR EMBL; AAEE01000002; EAK89763.1; -; Genomic_DNA.
DR RefSeq; XP_627445.1; XM_627445.1.
DR STRING; 353152.Q5CXK9; -.
DR EnsemblProtists; EAK89763; EAK89763; cgd6_670.
DR GeneID; 3376053; -.
DR KEGG; cpv:cgd6_670; -.
DR VEuPathDB; CryptoDB:cgd6_670; -.
DR InParanoid; Q5CXK9; -.
DR OMA; FRHINIT; -.
DR OrthoDB; 207261at2759; -.
DR Proteomes; UP000006726; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00053; EGF; 1.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 3.40.50.11970; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR005077; Peptidase_C11.
DR PANTHER; PTHR37835; ALPHA-CLOSTRIPAIN; 1.
DR PANTHER; PTHR37835:SF1; ALPHA-CLOSTRIPAIN; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF03415; Peptidase_C11; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006726};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1528..1555
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1154..1194
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1308..1353
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 70..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1607 AA; 185586 MW; 58C66D5316FB8260 CRC64;
MKREITFVFL VTIKFIFDIQ PISSFLYLPE NYVNVDKYQN LQSSKVNSTI TDIEEVNHND
NYNVDKTNNI RSEKKSHNNS KEEVVLSSIK KEEEPPKNKN DQLEFQYSKV CSTINKERIH
EKRYWTHLIF IHADNNLESM SLVDLGEMTS PLQTQTADHL HLVVYIDRCK DFTNKDVSAP
IISCPESGLT NPMIKQEQIS QNFTGAYILY RWRLTQELRV QFRKKFVWII LEDLGEVDSN
SPEILSNFIS KGLDSFPSIY SALTLWNHGS AWSGFGDDHD NADGNGMFLG EMYRGIKEGI
MNSKIGGKTG ENFSFEFKFD ILGFDACLMM QFDVLEVMNS LANYILASED NEPGHGWNFR
SLNPVTKKGS AEDEVQIFGP NKVQEYRIAT PLEYASRIVY GYTLHSQSYP LTLSLINTEF
YRIFRFNLYN LFTILYKCGG ENISDLLKRT ILNSKKIENC DISNLCSCYD MGDMLELLRS
YLSQEFFLDN SIQELLALTL DSYYNMQIAS VNIQECTDPD SELYGNCQGE LFNNRDLNKK
YALSNVYNKN SNILESRFTG VSIYYPDPDQ QVLCRNEAVA KSLAKKYTKQ TNYKWVQIIS
DILINKPGQL CNLELKYKGN HHFEEINSNF NSDSSYSDSI IKMNTTLLNI IPCKENSTNQ
ILFTSRMDNQ VISSQTLITY PINQSINNMV PILLIFPTRI KSNGIITTTY EHIGYEIYQI
AKNNDNNKEE KIIHSNLTLI TDMEKNHFTG HFLYYNNKYE IENDKNGAII AYLVFNKTIN
GSKLLISTSE GMTEKKKEDG GYLVPIIYYL KVDTRRNKYF DEIYQQICDL YSKFSGYLNG
LSYPLIGINI LPKYDEISIK SRRIQLITLV QKEMIFEWNN KIELRERKYQ SSKSLDNIGN
KRVLIGRYSI TSNGYDELSI LGVNMDFGTK LKDYHLNEEF NQIYTGKECN TDWLEDGICD
IFCINDSKDC DKVLDIGMKN KTMIDENKVQ KKKMVPNFLE SHSIHVECDN MDGRICWKNS
KCLKSKMTIN MNSSSHIMRN IFSDINNSQE NGNNQPNQLI NKVNNYCICD EGFQHQVIRL
IDSKTGNIFF RHSCEDINEC EEHNRQFQIE EKEQRQGDIY MGYNTNNAIY PTIERTREIT
SILNSPFSSI RRHIVTPSGL KRPCHPLALC INKEGSYSCV CKPGYYGDGK KSCIQENVCF
DKSFQELVIG PETQIDFSRG IDEEQSEKSL FCPKGLQCII QNTNIENNSE SYGNIIDEKR
KSINDYQEKS LLSLISNDLE DDKSYNHYCG CKKGYRISSL NQDLRCIDIN ECDEKNNGEL
INNCGEDSLC TNTIGSYICS CPIGWYGNGY ICIPKGEKRD IALKVELSGF YERIMPMGYD
NFINSFKQSI IQVLGINENG IEIVDMVLDH SLGVIRVITH FKSEMKINNS TNRILILKDE
ENTIEDLHLN LKKADEFITK LKNNTSDWYR KTYIGTSFGD MVNPNKIEMR KVKEREIKVW
QGSISKLMNR IMSDKIYIFI NSSPFGRIIV TLILITTVIW SIIGLLGIIL IFKVYKDNKK
EKMNKLILKS EEYGLEMEDY NINSSNVNIV NTIQQEKKEN KELSEKK
//
