ID A0A8S4AX00_9TELE Unreviewed; 1339 AA.
AC A0A8S4AX00;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 08-OCT-2025, entry version 12.
DE SubName: Full=(Atlantic silverside) hypothetical protein {ECO:0000313|EMBL:CAG5897181.1};
GN ORFNames=MMEN_LOCUS8223 {ECO:0000313|EMBL:CAG5897181.1};
OS Menidia menidia (Atlantic silverside).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Atheriniformes; Atherinopsidae; Menidiinae;
OC Menidia.
OX NCBI_TaxID=238744 {ECO:0000313|EMBL:CAG5897181.1, ECO:0000313|Proteomes:UP000677803};
RN [1] {ECO:0000313|EMBL:CAG5897181.1}
RP NUCLEOTIDE SEQUENCE.
RA Tigano A.;
RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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:CAG5897181.1}.
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DR EMBL; CAJRST010007779; CAG5897181.1; -; Genomic_DNA.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000677803; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF910; COLLECTIN-12; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000677803};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1339
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035875751"
FT DOMAIN 127..316
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 35..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..49
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..347
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..439
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..485
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..517
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..559
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..659
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..697
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..764
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..811
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..903
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1339 AA; 139265 MW; B628466C3B6E2081 CRC64;
MGVFRLSFAF FFLVWSPVRG QWWSLFWANP KTTSLPPVTS PPAMSPEPPG AQGTALGGVE
EGTETALEGI QTKGPELGPT GSTGLPIQST VKPGMLHPEE RAEGGSKTKS QYKPLKHWKS
ERGSGSHLDL MELVGVPLPP SVSFTPGYEG FPAFNFGPNA NIGRLTKTFV PGSFYRDFAI
IATVRPTSPR GGVLFAITDS QQKVVELGLA LTPVRGGLQS LLLYYTDRAQ AAHSHKAAAF
SVPDMTDQWT RFTVAVEHDE VRLYMDCGEA ERTTFHRRPE KLTFSRNSGI FVANAGGTGL
HKFVGYIQQL VIKDDPRAAE EQCEDDDPYA SGFTSGDDAL DDRESEEDTM RRKEGKKMDT
LLEEDSVPVR APPTEAPEVE LDEYSGHMTP TASNDKLLMT GPQGTEERRK GLVRTGLKGE
HGDPGPSGPP GPPGPPGPPG VVEERLGPQG PPGTPGFPGQ PGREGQKGSK GEAGQPGQRG
PQGYPGLNGE TGIKGEKGEP GVGLPGAPGL PGPPGPPRSR SVPYGPDALG SGFGDLDTDT
ELIRGPPGPP GPPGPPGPSS PRLSSELTPG HVGPPGEPGR TGLPGTSGIT GPAGADGSPG
PQGPGGEKGD RGLPGPPGPK GECGSVGVTG SPGPLGPMGP PGKRGPAGPS GPPGPPGPPG
TKYLIEDMEG SGKTDMIIGA RVKGPQGPPG LPGPQGPPGK DGAPGLSVKG EPGDPGPEGR
QGPAGLPGVR GAKGEKGSPG PKGDRGADGL SISGPPGPPG PPGPAANLQE LLLNATEGVV
NITDIRGPPG PMGPRGPKGD KGPQGGEGPT GLKGEKGEPG VTIAADGSIL SAPRGPQGPR
GPKGDRGFPG PAGHMGPLGP PGQKGEYGFP GRPGRPGMAG KKGDRGESVG VPGPPGPPGP
PGLPGRIIGL NGTVFPVRPR PHCKMGRESP TRGDSFALKG DKGDEGLPGE PGTPGFLMEL
WDLKVTWVLK ARRERRVTPV CLVLRVNQGG LDLWVQRGIP SSVLQVQSVL RGSLEFLVMD
VQEPEAPLVL QVPPERPLHM DQPSVSRAPP VLPAPQGLLV TPYKTVQALT RETHRAAEGA
LAYVSERGGE LYVRTHNGWR RIPLGELIQN GPGSPEASQA LSRGGDRGKP HRVHSQELQD
GSRGYQPSYN IPPQAVSSEP GLRLVALNAP LRGDMRGIRG ADFQCYQQAR AMGLTSTYRA
FLSSHLQDLA TIVRKADRND LPVVNLRGEV LFSSWMSIFS GNGGLFDPST PIYSFDGRNV
LTDSAWPEKL VWHGSSPVGI RLTSTYCEAW RTADAAVSGQ AALLQTGRLL GQHARPCSGQ
HIVLCVENTY VGGARQRRT
//
