ID A0A3B3YCG7_9TELE Unreviewed; 1104 AA.
AC A0A3B3YCG7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Tenascin N {ECO:0008006|Google:ProtNLM};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000025046.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000025046.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR AlphaFoldDB; A0A3B3YCG7; -.
DR Ensembl; ENSPMET00000006046.1; ENSPMEP00000025046.1; ENSPMEG00000007794.1.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00063; FN3; 7.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR InterPro; IPR000742; EGF-like_dom.
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; IPR020837; Fibrinogen_CS.
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:SF5; TENASCIN N; 1.
DR Pfam; PF18720; EGF_Tenascin; 3.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 7.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 7.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 4.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 6.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1104
FT /note="Tenascin N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017185880"
FT DOMAIN 258..350
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 438..525
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 526..614
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 615..700
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 701..790
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 791..879
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 877..1061
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT REGION 518..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1104 AA; 121933 MW; 305B1AAA148A3BC7 CRC64;
MSAGLLWRAL CLLIILCTVS HHVRCTDNQP DSSGTEQGLT FSHIYKLDIP GSSSCTVERL
PTHKTALQQD TITNGENDII FKHNIRLQTP KCNCEESESF KDLLYRINGL EEEVTYLKTQ
CTQGCCGRGG VADTSCSDHG TYQQDTCSCL CNPGWEGPDC SVSSCPDECN DNGRCVDGKC
VCYEGYTGED CSQLTCPGDC NDKGECRDGK CVCFPHFTGE DCSTPTCPND CGGNGQCVDG
QCVCEEGFYG EDCSLVLTPQ GLRLVQVTDV SLLVEWESVQ GAEYYMLTYH PKFDEGAKEE
VRISNSENSY LITGLAPGVT YVVQVYAVIK TIQSEADMIE GTTDVSTVDD MQVIGQTEVS
IQVDWKNPQA EVDYFRLTHT DPSGQEEELN VQRSQEARTK YTIVGLYPGT EYQISVQPIK
GNTKGKASFA TGVTDIDAPT NFVTTEVTED TATVSWDKAQ AEIEGYMLSY TSAEGSSSDI
FVGRDSTSYR LVGLRPGVLH TVYIWAFKGD KVSGKSSTEA ETELDAPTNL SVEDETDSSF
RVSWDPTEAQ IDGYMLAYSS ADGSREETQV GSGSSYALTG LRPGVVYTVY VWAVRGSKAS
RKTSTQAETE LDAPANLVAY DETESSFSLS WDPVQAEIDG YILTYTFLDG SSKEIPLGPD
STSYLLTGLR PGVLYTVYIK ASRGDKTSRT ISTQAETELD APANLIARGE TESSFILSWD
PVRAEIDGYI LTYTFHDGSS KEILVGPDSA SYVLTGLRPA FIYTVYIKAV RGDKASRTIS
IQAETEIDSP KDLKASDVTQ DSVSLTWVPP LADINGYVLT IRDEEGKLQT IENTLASSKR
RFAASKLERG KRYIVTIYAF RGSKRSKVVE TFFKTVALLY PFPMDCGQIM KNGNKNNGVY
TVYINNNQSK PIQVYCDMTT DGGGWLVLQR RNTGNLDFMR RWRQYIAGFG NLTEEFWIGL
DKIHELTNTP TQYEIRFDLG LGSDRAYAVY DNFKIAPVRQ RFKLTIGKYR GTAGDAMTYH
QGRPWTTMDS DNDLALTNCA RTHQGAWWYA NCHLANLNGK WGDNTHSVVS EQGGHFAFIT
WLAECFSKRV WPTSQVSVQC ASVK
//
