ID A0A1S3MKK5_SALSA Unreviewed; 1403 AA.
AC A0A1S3MKK5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Early endosome antigen 1-like isoform X1 {ECO:0000313|RefSeq:XP_014003722.1};
GN Name=LOC106573307 {ECO:0000313|RefSeq:XP_014003722.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014003722.1};
RN [1] {ECO:0000313|RefSeq:XP_014003722.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014003722.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014003722.1; XM_014148247.1.
DR STRING; 8030.ENSSSAP00000014017; -.
DR PaxDb; 8030-ENSSSAP00000014017; -.
DR GeneID; 106573307; -.
DR KEGG; sasa:106573307; -.
DR CTD; 8411; -.
DR OrthoDB; 2881467at2759; -.
DR Proteomes; UP000087266; Chromosome ssa16.
DR Bgee; ENSSSAG00000006905; Expressed in brain and 13 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15730; FYVE_EEA1; 1.
DR Gene3D; 1.20.5.390; L1 transposable element, trimerization domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23164; EARLY ENDOSOME ANTIGEN 1; 1.
DR PANTHER; PTHR23164:SF17; EARLY ENDOSOME ANTIGEN 1; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 36..65
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1344..1402
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 440..758
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 787..846
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1256..1332
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1403 AA; 159700 MW; 9670BE41F00BD4FB CRC64;
MLRRILQMTP GKGGSQNSES DQPSADLNND QTSEGFICPQ CMKSHNSAEE LFKHYELYHD
SGDQPSHTGP GREDLVLLRQ ELQELQTSLK EEKWFSAELK KELDKVQGHL KQGPQNDGQT
GLEDSALAIK LNEAETETFN IKQMKDLFEQ KAAQLATDIV DVKSRYDEEK SLREAADQRL
ANLSQELQRE RQDKDRLHTE LLQRPGVEDV EVLQKELIQV QTLMDRMTRE REEESEHLKS
KYEQLQADHT SSEIRKLEKT ISQLKAELEK GPQEAAVYTQ QIHQLQSSLN NLQQQSQLLS
EKLLRREKEF QELEEGLRAE QVSKKTAQAS LHQRELEVQE LQARAVGAET SLQRAQAELG
ERGEEAERLR REVAELEAKH REVKTERKQL QQQREERESQ GLAQQSEICQ LHAKLLEAER
QLGEVHGRLK EQRQLSGEKL KDREQQAADL QIKLSRSEEQ LKENSSKTLD LQHQLEKAKQ
QHQELQGLQQ NTNTKLREAQ NDLEQVLRQI GDKDQTIQNL EALLQKTKDS VSQLEAERED
LVAKIQAGEG ETAVLNQLQE KNHTLQTQVT HLTDKLKNQS ESHKQAQDNL HKQVQEQKTL
LRATQDQAQA VETSIKEVNT QLTESREKVA QLDTQLKAKT EMLLSAEAAK ATQRVDLENH
LETAQHALQD KQQELSKSQA CVEEQGRGLQ ARQEQCGQLE ASLKEVKDKL LISEQRVEQL
EVRAKKAEAE GGELRAAREQ AQQEVQKLQK QGSEVKGKLK ELGCLLETEK AGTAALQVEL
KRKTFSLSDT RQQLEQCEQE KTSLQANLDK LAQEGQAQQA ELDRKAQGLA RELQTAQQEK
EAQGKELAAV KDGLAKAYKA MKDSQSQLDK ERKSSKAVLE EKEKSHEKAR QELLKATEAT
TKEMAEVKGQ LDKIREAEKG LNMQLTALTE QHTKTQEALK EKEKGVQQLQ AQLTTAQGSF
SQEKKKLESQ VTKLQGSHAK KAEEEGRLRE QVSALGQDLS SERARTTELQ EVLEQSQQGL
AKLQSEYYGK ESELSSLRQD LKASEERLTL SQEELSANRV QLTGLEGQVQ EVKAARASLE
QELAKRDQKL GQQETALKDL QKQQGVTQEE LQKERSRAEE LSQTKAALEK DTTRLGSELK
ALRERSDKEL RELREAKQLL IQQKLETQCR VEEVQAALEQ EETLHQATRD RVTQREEKLR
AETQEIQAQL ASERNAREGQ AKRGEEAEAR LGLQVTALNE NVATLKREWQ GSQRHCGELE
KQTDELRGEI AVLEATVQNN QEERRALLER CVKGEGEMEK LQAKVVEMRR KLDDTTAAMQ
ELGRENQSLQ IKQSQSLTRK WAEDHEVQNC MDCGKGFSLA IRKHHCRHCG NIFCAECSAK
NALIPSSKKP VRVCETCFED LQA
//
