ID   A0A1S3H3U7_LINUN        Unreviewed;      1114 AA.
AC   A0A1S3H3U7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Titin homolog isoform X2 {ECO:0000313|RefSeq:XP_013380632.1};
GN   Name=LOC106151773 {ECO:0000313|RefSeq:XP_013380632.1};
OS   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_013380632.1};
RN   [1] {ECO:0000313|RefSeq:XP_013380632.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013380632.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_013380632.1; XM_013525178.1.
DR   AlphaFoldDB; A0A1S3H3U7; -.
DR   EnsemblMetazoa; XM_013525178.1; XP_013380632.1; LOC106151773.
DR   GeneID; 106151773; -.
DR   OrthoDB; 2906101at2759; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR045072; MKRN-like.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR   PANTHER; PTHR11224:SF10; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00367; LRR_CC; 2.
DR   SMART; SM00356; ZnF_C3H1; 2.
DR   SUPFAM; SSF90229; CCCH zinc finger; 2.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS50103; ZF_C3H1; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          23..50
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          54..77
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         23..50
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         54..77
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          287..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          77..182
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        380..412
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..496
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..534
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..660
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1114 AA;  128567 MW;  F8D384499C706B23 CRC64;
     MFCDDDEFFF YHAFRKSSYS SPDTSHIFCK YFARGSCKFG NDCYFSHDIT DKKPCKNYLR
     DGSCSFGDNC WYRHIGAEQV SKEKEEKEEK RKRELEELKE HNARLLKEQI AERERLRSIQ
     PFEFREPKPK SKLTLEEALS KLEVIKNEVA DQLKEEELEK EARKRKKERG ELEENIEDVE
     WKDFCEFDEI CHNFRKFVNQ YDLTDWSVDD HIQLISAFHI SDQTECQEYY HPLTFVMGPL
     FRLWRPSPQA WARLCVAIVE LLKECVDMEE VIQAWNAALD DCEIEDENYE PDSEESESDE
     DFTEDEENEH VVIEELGDLC VYLQEMVKLE IEDLSAAANL TLEEVIQSLP HDIVEPHIMD
     PDQEDEDSWF TALTEVEYKE NDSEDLDYEP EESEGDDEET IAQEEAEADE AAVKEELQDL
     EAMAQMSKEE LLSSLPPEVL QPPVAESEDD EEEEEEEEEE EDEDEGVAGD MAEDEDQEEE
     EEVDDGIGEE EEEEYWAVAL ATDRELYDED DLEDKDYEPA EEEGTTDEDS TSAETDEESL
     RRELKELEEM AEIPFEEFVS SLPPEILRNY GIEMEDIPIP ASSSPDTDTN NNDEGIKKET
     EETQEDDAQN SEKKDEEKTF EDDKHEQTIP DNETEKTEPE KPGSENEAEQ SKLEVSLDVP
     EPRRKSAPLL AMLMAKKYTD AEVFIGGLLA GLLQLNHPDW GNKEVAHLFQ KLEEGGYNCL
     DRARALLGMS MYLSVDEMAQ FVNEYVKLTY GIQDPYECRC KTPECTCEME VDWEYSTDVF
     KELADMAGWD RENKILFFQK ASYQLWHTDC LSSALEKYGL LDRSRGDMDE EAVRAILKGC
     TPLPYTMEYI LKYYGDEPGL VQELMKHIPE SEAKPKSSGN TGSHCAGRSG NCKNSAKKMC
     ENGMCSKCCR HSKRMCEIHG HNLGFEDGVG HIDIPNHHRY VSVKPFLHIL SNADWGEALQ
     KKGEQGYRNI KFGPDVDLKD HHIELLASKC PKLEVLEMGS SDTGSGARVS DRAIKCLADR
     CPKLRKLKLE SFTSITDESL QRLFKMCSNL ECFEISGNDK VCGRLTEKLV KQLFNKKLLP
     KLRFLSLQDQ LNISPDVIFR LRRCRTNVKI IHSQ
//