ID A0A1S3JTY4_LINAN Unreviewed; 3118 AA.
AC A0A1S3JTY4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 35.
DE SubName: Full=FRAS1-related extracellular matrix protein 2-like {ECO:0000313|RefSeq:XP_013413797.1};
GN Name=LOC106176111 {ECO:0000313|RefSeq:XP_013413797.1};
OS Lingula anatina (Brachiopod) (Lingula unguis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013413797.1};
RN [1] {ECO:0000313|RefSeq:XP_013413797.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013413797.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SIMILARITY: Belongs to the FRAS1 family.
CC {ECO:0000256|ARBA:ARBA00005529}.
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DR RefSeq; XP_013413797.1; XM_013558343.1.
DR STRING; 7574.A0A1S3JTY4; -.
DR GeneID; 106176111; -.
DR KEGG; lak:106176111; -.
DR InParanoid; A0A1S3JTY4; -.
DR OrthoDB; 430044at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR Gene3D; 2.60.40.2030; -; 5.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR039005; CSPG_rpt.
DR InterPro; IPR045658; FRAS1-rel_N.
DR InterPro; IPR051561; FRAS1_ECM.
DR PANTHER; PTHR45739:SF8; FRAS1-RELATED EXTRACELLULAR MATRIX PROTEIN 1; 1.
DR PANTHER; PTHR45739; MATRIX PROTEIN, PUTATIVE-RELATED; 1.
DR Pfam; PF16184; Cadherin_3; 11.
DR Pfam; PF03160; Calx-beta; 3.
DR Pfam; PF19309; Frem_N; 1.
DR SMART; SM00237; Calx_beta; 5.
DR SUPFAM; SSF141072; CalX-like; 5.
DR PROSITE; PS51854; CSPG; 12.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..3118
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010380312"
FT TRANSMEM 3054..3078
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 270..368
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 391..479
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 500..610
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 635..741
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 763..856
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 886..978
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 1007..1109
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 1130..1223
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 1244..1340
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 1361..1453
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 1473..1562
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 1596..1693
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT DOMAIN 1695..1799
FT /note="Calx-beta"
FT /evidence="ECO:0000259|SMART:SM00237"
FT DOMAIN 1812..1923
FT /note="Calx-beta"
FT /evidence="ECO:0000259|SMART:SM00237"
FT DOMAIN 1939..2043
FT /note="Calx-beta"
FT /evidence="ECO:0000259|SMART:SM00237"
FT DOMAIN 2058..2161
FT /note="Calx-beta"
FT /evidence="ECO:0000259|SMART:SM00237"
FT DOMAIN 2179..2285
FT /note="Calx-beta"
FT /evidence="ECO:0000259|SMART:SM00237"
FT REGION 3089..3118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3109..3118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3118 AA; 348487 MW; E90FE52DD737BF57 CRC64;
MDPLESKSPG RGKFLWLAVV FVLACMFCMG HGQLTSAGRI LRVNRGIQVP FGRSVYLDPE
RDLKIDQQPG DRCIVSVLET DVLAQRPGML MPHAFPCRFR PGEVEYTHFG SRNPLFDRVR
LQIRYDSQTE TIIIPFTIEV EVLSVQLEIV TRNMPITVDR LLGYSTPINN KALQFTYDRG
SESCKVSVLS AASGLPRYGE MANTSAAMTM IDCEAFLESG IRYKHTSPLD SPNRDYIPMV
VELMSSEGTV KKQEYFQVMV RIKEGLENTP PSPSYDAILV LEVDQFVMTA ITPDILAAID
QETPAGQLIF NITRPLTFDE GVIVSTDDRN LPVKSFYQSD VQDLKIAYKP PSIDSAVRRI
FQVEFQVVDA EGLTSDPFTL MIIVKPMNTL APVVTRNTGI QLFEGQSRPL LSAQNLEISD
EDNLDDVRIQ VIDGLRHGEL HMNGIKRKFF SPADLDAGMV VYQHDGSDTY SDNIIFRMTD
GEHEVEFLFP VTVYPEDDEP PIINVNTGLQ IQKNDVVSIS PFVLSATDID SDDASIKFTL
LEPHSTEGMV MMRQIEPPSD PDNWRFVNGH YERPVTMWTQ QDIVEGKLFY HHVGPHNTEV
VMDRLKFTVQ DNHTPPNVSP IQDFVVKIMP VDDQPPYLCP RTPLLMTVNE FQLTHFRKKV
MCYTDLDSID RELQYTITAP PYDTDTNNPL PAGSIVLFEY PEIIISEFTQ AQVNHRKVGY
QPPSTELGIT PRLIQFEFDV KDTAGNVLPQ QKFTIKLQPV DNKPPVITNP GFSVFENNYL
QITPQNLDAV DPDTDGNMIN FTVVEIPVHG QLTYLGNPMA EGEVFKRGDI SSGRIAYLNQ
GQVGEMDSDK FKLDVTDGIH HIPVVVKVAV RGVDDEMPSL ALTDEASSGN LGFRIEVKEG
QSAPITSNMI KATDTDTDDL MLTFLVESAP RKGVILLGNQ VTDKFTQSDI INNNVVYMHT
SGEIGPEETK DHFTLTLSDM SDDLLIGGNR IQGIKVNVTI LPVDNNTPVV VVGGPLVVPE
GNKSAITLSH ISASDVDSEV DDIQCTIIVQ PTQGYLENSA PGDGSEKSRA GMPISTFTMK
DIRLMNINYV QSIHQGVEST EDRFTFRCSD GVNFSPNFFL DVVIIPDNDE VPELYMREFV
VLEGNSLVID TPILNAIDKD IPEQELIFHI LEAPGHGKIL QQRPTGSVQV DRFSVSDISD
GSTIVYEHDD SETTEDKFKV KLTDGKHEVE KEILIMVIPV DDETPRLTIN NGLEVDIGET
KVINDQVLKA EDLDSDDLNI QFIVRKQPIH GYLQRVVNGV SSNITRGMNF SQWEIDDGSR
IQYVHTGAEG VRDLIKFDVT DGFNPLIDRY FYVSVEGIDM TYPEVINKGV ELPEGGSVIL
TTDLLSTYDL NSPDENLQFT ITRAPSRGHL ESTDQPGVPI TTFTQLQLAG NKIRYVHMSE
DEMKMDSFEF EVTDGYNPVV RTFRVSLSDI DNKKPVLMLE PLRVKEGGTK LITPFELKAV
DRDTDDTKIR FTVTQIPIHG TIRYNNTRSV TTFTMEDLNE NLITYAHDGT ETLEDSFALV
VTDGTHTDFF VFPDTTTTTR RPQEVLVEII PVDNGVPQIA VNRGGASLDQ LGDGRLGFRF
TNKVLKAEDR DSTGDVLKYK IITPPEHGYI INRAHGNKSV GNWSQEDVDR MRIHYILKNN
TNATGDVFYF KITDKGGNVL DNQPFYLNWA WISFATEYYI VNETDRRVNV TLNRRGFLGE
TSFITITAKN GTAKVGEDVR KKYAHQVQFN PGQMKKNWHI RLIDDDKYED FETFTLELSE
PVMGALEHPK VATVRILDKE DESTVFFPES QYTVEEDIGI IKVPIKRTGD ISDELMVICS
TVQDSATGTV PSTVTSYSDY ITRPEDHNSM VRFDKNEDTK FCNIQIIDDS LFEEEERFQV
VLTMPMGGKV GQHNMTEVVI APDKDDEPAI YLGASEYEVD ESDGFVEVKI WRTGTDLSKT
SSVTIRSKKT KPVSADAGLD YSAINRVVNF APGMTMQTVK VTILDDLGQP RLEGPESFQL
VLRMPTGGMM GEPSKALVVI NDSVTDLPKF HFEEDMYMGF ENDGVVRTMI RRTGDTSHLA
TVRCYTRQDT ARVMMDYSER PDTDASIVTF LPGEVKKPCV VELMGDSEFE EEEEQFRLVL
GSPSSPSAGG ALIGSPNFTT IVVKDAGDKP IIKFERTKYS VNEPMFSGEI ATVEIPVVRL
GDLSQTSIVR VHTKDGSAKS GPGNDYHGFS KELEFGLNVS RHVIKVEVLY DGEREMREAF
TVHIKPDRNM VADVQMNKAI VYIEEMNKMA DVTFPSPPMV VSLRNYDDAK NAPPNPVQGY
PVICITPCNP KHPEYYKTGS LCTSEGINDT QTIFRWRVSA PSYLDGVTSE LNDVSSNTFF
TNTHKITLDS IYFSGGSRVQ CAARAVNEDG DPGLELLSPV VTVSSDEGIC MPRVMGSVGA
EPFTAKLRYT GPGDPTHPNM VRLSVTIPHR DGMLPVISTN ILSNFELALS PDAFRIGQHK
CSNLLDYDEV RTKYGYITNE TKNPNIVGSM EPYQYNADIR SEPSLRFYKN LDLEACLWEF
VTYYTMSELV TDCGGTIGTD GQVLNLKQSY VSVRVPLYVS YVFHSPVATG GWQNYDLSSQ
LRLTFVYDTA ILWQNGIGAE DGSSELQGFL YPTSMRIRKD GRLAVNFRTE ARFRGQYVLS
HPGTSLTSMV MSAVNPDLTF TLELLRSEPT FEQPEQTWEF VSDYAVRDYS GKYTIKLIPC
TTPLDQEYAL PVVCNPRQPM NFDLDIRFQQ ISDPVPAEFS LNTNFHLLRK KALWLSDGSM
GFGEDSDAAF GQGDKIYGRI MVDSVQNLGD SFNLNIEKVF ICTGKDGYIP KYDPANEEYG
CVADSPNLQQ TFRILDKGAP NTISPTFRDI PFNARLAVDD PSAVNLVLQP GSDGFSLDAK
PLFKVDSGRQ WFVHAIYTVR SMENSRNGIG KRSITYHSIS GIQSSLETMV EEVLHTRRKR
AIEDTKNIGQ SNNRGTNMVR ISLNFTAKAE DNNLQGNTEV GTSVLNTEPA STPIIPIIIA
VVLFLVLCII IIVIVIVVGR KKKEKKKSLS NGVTVPIGNG KSRVYDPKYQ NNNDSSEV
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