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Database: UniProt
Entry: A0A3Q2C9S8_CYPVA
LinkDB: A0A3Q2C9S8_CYPVA
Original site: A0A3Q2C9S8_CYPVA 
ID   A0A3Q2C9S8_CYPVA        Unreviewed;      1861 AA.
AC   A0A3Q2C9S8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Tenascin-like {ECO:0000313|Ensembl:ENSCVAP00000001561.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000001561.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000001561.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498}.
CC   -!- SIMILARITY: Belongs to the tenascin family.
CC       {ECO:0000256|ARBA:ARBA00008673}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   RefSeq; XP_015243026.1; XM_015387540.1.
DR   Ensembl; ENSCVAT00000013206.1; ENSCVAP00000001561.1; ENSCVAG00000002557.1.
DR   GeneID; 107092858; -.
DR   CTD; 100149028; -.
DR   GeneTree; ENSGT00940000155188; -.
DR   OrthoDB; 5489847at2759; -.
DR   Proteomes; UP000265020; Unplaced.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd00063; FN3; 11.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 11.
DR   Gene3D; 2.10.25.10; Laminin; 13.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR041161; EGF_Tenascin.
DR   InterPro; IPR036056; Fibrinogen-like_C.
DR   InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   NCBIfam; NF040941; GGGWT_bact; 1.
DR   PANTHER; PTHR46708; TENASCIN; 1.
DR   PANTHER; PTHR46708:SF1; TENASCIN; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF18720; EGF_Tenascin; 10.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   Pfam; PF00041; fn3; 11.
DR   SMART; SM00181; EGF; 14.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM00060; FN3; 11.
DR   SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 8.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 9.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1861
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018528694"
FT   DOMAIN          374..405
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          595..685
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          774..865
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          866..951
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          956..1044
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1096..1185
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1189..1280
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1370..1459
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1460..1546
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1547..1635
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1635..1850
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
FT   REGION          903..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1056..1091
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1061..1075
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        378..388
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        395..404
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1861 AA;  203068 MW;  4C879AF4FAF77B04 CRC64;
     MGTHSLLGFL LLITLISLTN AGFVKKILRH KRQTLSPPSE HNVTFPSADH PVVFSHVYNI
     NVPESSLCSV DLESPEGAHV HSKDIAAVPQ GHHVTEHTFN GENQILFTHR INIPRQACGC
     KDDFPGLKEL MSRLEMLEGE VSALRDQCSS EQLTGELGTK PYCNGHGKYS TETCACICDP
     GWRGPNCTEG ECPTSCQDRG RCVDGKCECY KGFTGEDCAL KTCPMDCGAH GICEREVCVC
     SDGFFGEDCS ESRCLNNCLG RGRCDEGDCI CDEPWTGLDC SELICPNDCY DRGRCVNGTC
     YCDEGFSGED CADFSCPNNC RGNGFCVDGK CICTVGYSGQ DCSQLTCLND CNDRGRCFNG
     VCICDSGYQG EDCSQVACVN NCHNRGQCIN GRCSCDAGFH GDDCSELSCP NNCQLKGRCV
     NGQCVCDEGF AGEDCSIHTC PSNCYGRGEC IEGRCACHVG YVGEDCSQLS CPNNCNNRGR
     CIDGQCVCDE GFSGEDCSQK ACLNDCLARG YCIDGKCFCH EGYTGESCSI LACPENCNNR
     GRCVNGRCTC DSGYEGESCA DLSCINNCQD KGRCVNGQCF CDEGYIGEDC SEVSPPKDLT
     VGEVSTETVD LSWNNEMLVT EYLITYVPTS PGGLLMEFTV PGDKNAATVK ELEPGIEYLI
     SVYAVLSNKR SIPVSARVAT DLPQPEGVRF KSVRETSVEV VWDQLDISFD SWEIYFRNTK
     EENGKVVSTL PPSQNEFLQS GLGPGQEYEV SINVVKNNTR GPQTSRTVTT KIDGPRQVEV
     KDVTDSSALI SWYLPVAPAD GVTIFYMPSS NHSDETTVDV SPSDKQYSID NLKPDTEYAV
     SIISRHKEAT SDPVTTIFTT ELDAPTAAQA VSQTDDSITL EWTNSQADVS SYRVKYTPIS
     GSSHGERVFP RGSGRTTQAT ITGLKPGTEY GVGVTAVKHE RESLPATTNA ATELDPPRDF
     KQIRSTETSL SVSWQKPQAK LSGYRLEYMS RDGQAEQVDI PASANTFVLS DLIPGMSYTM
     TLTAERGHKR SRPVSLTAST APPDVLALSI KEAPTTAISA QDEENHKHGY DISSEAPSDN
     EEMISGAEPE SSGMELLSNL TPVNVTATSM SLVWSAPDEA FDSFLVELVA PSAAAAQPRV
     TTIPGGLRKA KIEGLLPSTL YEITLHGLME GTPSLPLRVF TTTAGLEPTL GNLIISDITW
     DSFVASWNPT GEDFNSFVIE VTNMDDLAEA QNLTLSGDAT SLLISGLNPN TSYMVGLYGT
     HQGSFLEPLY SEATTEAEPE VEHLFISDIT SHSFRLSWAA DEDQFDRFVI KIRDSKRLAH
     PREYKARGSE RTKVITGLMS GTEYEIELYG LTLDQRSQPI TAVAQTGLSA PKGLHFTEVT
     DSSAVVHWSN PRSQVDSYRI TYVPFEGGSP LILNADGSMS EMLLINMFPG KTYQVTVSSL
     KGLEESEPST GTVTTALDSP RGVTAVNVTD TSALLSWQPS VATVDGYVIT YSTDTVSPVV
     EHVSGNIVEF QINTLVPGSH YTAAVYGVKE AQRSESTLTA FTTDLDPPRD LMANNVQTDT
     ATLTWKPPTA AVTGYMLSFS SPGGVIREVM LSPTASSYSM SQLTGSTKYD VRLQAISGAQ
     RSRYVTTTFS TNKVGQLYAR PWDCAQILLN GETTSGLYTI YIGGEESQPI QVYCDMTTDG
     GGWMVFLRRQ NGKLEFFRNW KNYTAGFGNM NDEFWLGLSS LHKITSLGHY ELRVDLRDNE
     ESAYAQYDKF TIAEPRTRYK VYLGAYSGTA GDSMSYHQGR PFSTYDNDND IAVTNCALSY
     KGAFWYKNCH RVNLMGKYGD SSHSKGINWF HWKGHEHSIE FAEMKIRPAN FKNPESRKKS
     S
//
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