ID   A0A3Q3B5W1_KRYMA        Unreviewed;      1403 AA.
AC   A0A3Q3B5W1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Titin {ECO:0008006|Google:ProtNLM};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000024535.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000024535.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   STRING; 37003.ENSKMAP00000024535; -.
DR   Ensembl; ENSKMAT00000024843.1; ENSKMAP00000024535.1; ENSKMAG00000018020.1.
DR   GeneTree; ENSGT01100000263523; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 10.
DR   CDD; cd05748; Ig_Titin_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 14.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   PANTHER; PTHR14340; MICROFIBRIL-ASSOCIATED GLYCOPROTEIN 3; 1.
DR   PANTHER; PTHR14340:SF21; MYOSIN BINDING PROTEIN C2; 1.
DR   Pfam; PF00041; fn3; 10.
DR   Pfam; PF07679; I-set; 4.
DR   PRINTS; PR00014; FNTYPEIII.
DR   SMART; SM00060; FN3; 10.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF49265; Fibronectin type III; 7.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   PROSITE; PS50853; FN3; 9.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   4: Predicted;
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          44..137
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          141..227
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          236..330
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          336..430
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          434..530
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          534..623
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          630..729
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          730..824
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          828..924
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1028..1121
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1297..1390
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          513..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1403 AA;  155348 MW;  99B3085BC22E7E2E CRC64;
     MSWKVESLPE GGIFFFRVLA ENEYGVGLQA KTIEPIKISE KPQPPGKVSV VDVTHSTVTL
     TWEKSQYDGG SRISHYEVEI APKDSETWSP CASVKGTETE VSNLLKGEEY QFRVIAVNEK
     GKSDPRQLVQ SVVAKDLVIE PSVRPKVSSY SVQVGYDLKI EVPIAGHPKP TITWTKNGVA
     LKQTTRVNVT DSAHQTTLTI KDATREDSGM YTINIANSLG SKDATIEVIT LDKPGPPTGP
     VKIEDISAES MTLSWEAPTY TGGCPISNYV VEKRDTTTTN WVVVSATVAR TTLKVSNLKT
     GGEYQFRIFA ENRYGKSYAI DSQPVVAQYP FQEPGPPGTP FVSSYTKDYM VVEWHKPPSD
     GGSAILGYHL ERKEKNSILW TKINKMVIQD CKFKSTPLEE SIEYEYRVYA ENIVGIGKCS
     KVSEVYVARD PCDPPGRPEA VIVTRHSVKL KWSPPQYDGG SLVTGYIVEK RDLPEGKWMK
     ASFANIIERE FTITGLTEDN KYDFRVIARN AAGAASKPSE TTGSITAKDE VEPPKCETDP
     MYNQTLVINA GDTFSLEASV EGKPIPTAQW FKGSVEIENS ARSEIKNTDF KLVIKDANKE
     DSGKYTITAT SSIGTTTEEI TVVILDKPGP PTGPVKIEEV SCNFVTLSWE PPEYTGGCQI
     NNYIVEKRDT TTTAWQIVSA TIARTTIKVT NLKTGVEYQF RVSAENRYGK SSAIVSPAVV
     AKYPFSEPAA PGSPVITAAT KDSMVVEWKP PTNSGGSPII GYHLERKEKN SLLWTKLNKL
     LIPDTRFKTT ELEEGIEYEF RVYAENIAGI SPASKVSETT VARDPCDPPG TPEAIEITRN
     HVTLQWTRPQ YDGGSAITGY VIERRKHPDT RWMKASFTNI IDTQFTITGL TEDCVYEFRV
     IAKNSAGISS RPSGSTGEIT AKDAIEAPDA TMDSKFKDLT VVHAGESFVI DADYTGKPLP
     EVMWLKDGKE IDKTTPRMEI KTTLTRTILT VKDCIRVDGG HFVLKLVNVG GIKMIPVNVK
     VLDRPGPPDG PLEVKGVTAE KCYLHWNHPS HDGGASISHY IIEKRETSRL SWTVVEPKIQ
     AISYKITKLL PGNEYIFRVI AVNKYGVGEP LESDAPSTPE ASAITRDSMV LTWERPENNG
     GAEIEGYVLE KRDKDGVRWT KCNKKRLTDL RFRFTSSYTI IKLFPSLTFL HIFSLEPPEV
     NMKDFPYNTV YVRAGSTLKC EIPLTGRPMP KVSLSKDNVL LKSTMRFNSE VTPDSIKITL
     RESVAGDSGR YDITASNSSG TTKSYIKIVV LDRPSAPLGP VELFDVTEDS VSLTWLPPAY
     DGGSPITNYI VQKRETTTAN WMDVSSAVAR CTMKIMKLTT GLEYQFRIRA ENKYGISEHI
     DSPAVTVNLP YSKDCLFCSY FQM
//