ID T2M5G7_HYDVU Unreviewed; 847 AA.
AC T2M5G7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=SPARC-related modular calcium-binding protein 1 {ECO:0000313|EMBL:CDG67374.1};
GN Name=SMOC1 {ECO:0000313|EMBL:CDG67374.1};
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG67374.1};
RN [1] {ECO:0000313|EMBL:CDG67374.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole animals {ECO:0000313|EMBL:CDG67374.1};
RX PubMed=24065732; DOI=10.1093/gbe/evt142;
RA Wenger Y., Galliot B.;
RT "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT bilaterian, euteleostome, and hominidae ancestors.";
RL Genome Biol. Evol. 5:1949-1968(2013).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
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DR EMBL; HAAD01001142; CDG67374.1; -; mRNA.
DR AlphaFoldDB; T2M5G7; -.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; Kunitz-type; 2.
DR CDD; cd00191; TY; 3.
DR CDD; cd01450; vWFA_subfamily_ECM; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 2.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 5.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR12352:SF3; NIDOGEN-2; 1.
DR PANTHER; PTHR12352; SECRETED MODULAR CALCIUM-BINDING PROTEIN; 1.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR Pfam; PF00086; Thyroglobulin_1; 5.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 2.
DR SMART; SM00211; TY; 5.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF57362; BPTI-like; 2.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 5.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 2.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 3.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 5.
DR PROSITE; PS50234; VWFA; 1.
PE 2: Evidence at transcript level;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..847
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004603615"
FT DOMAIN 43..225
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 326..400
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 411..480
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 489..539
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 542..602
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 614..676
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 676..736
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 729..802
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
SQ SEQUENCE 847 AA; 93363 MW; 51898C32E72B5A23 CRC64;
MEMFVKLFVF AIYTLQVFNF PLATITESSS SFVTTPLCPN PLDIVIVIDS SGSVQKEWND
IIDHAQYFAS TFNVSEQHTR IGIVDFSAVA NVYKTVDNEN TEEQVYNALE SLRARPQNGE
TWLNLALQRT IELFGSATPQ RENVRKIMVL YTDGKMTNKD EESLRDLIKS HRLVSVESYI
VQVNNDSHES TLHEVASSKL HIFKLSGEPV ESGKSFLNDA VCFNIDNEND CTTPSPINPG
CVKTTKPPCV TTTPSSQGGD CSTNAFTTTS TTTSTTTSTT ISTTTKNVDH NDCTTTTPAA
TGVNCGIATT ISTTPQGLSY STVTVQSKCL LEKMHATWLV ESKVPTAVPV FIPDCNSDGK
YNKIQHHEGT GYYWCVDPNT GDIIEGTTKD EGNSSDLPNC DIKEDTQSLN LTSCLKDRAS
KLKLSEKIPD INIPECNPED GLYESLQIGN GGRFKWCVNR LTGKLIEGTI TDGAEKQPHC
SDILVNSKCL AQKEVGPCKG AVSAFYFNKE TLKCEPFMYG GCNGNENNFQ TLVDCQKACG
SLSKCLIERE VARLKNNPYI PECTNDGLYN QVQNYAGNYW CVDIVKGTLL KGSMLQGKVP
SCDQGKSVSE NEFPVNCLKE LTSKKLLPGT FVPQCDENGY YREVQVHGST GNSWCVHKYE
GTEIEGTRVD ASNPDCLLPR NSGLNEQPDS ERPDCFGLSQ RIYYDWQQGK CLSFNYGGCG
GNKNNFKNLE ECQLICNADF ARQVANSNRQ LLGNYIPQCD QSGNYNPLQY HNSTGMRWCV
NVTTGVEING TRVYPGQNDP KCETSYSDNS VVSTAMPPPE FVVIPVLNPP PTPKPTSGFT
FYLLLVK
//
